2025年度
4/14 相場
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4/21 一宮
Wagschal, et al., “Chromohalobacter salixigens uronate dehydrogenase: directed evolution for improved thermal stability and mutant CsUDH-inc X-ray crystal structure” Process Biochem. 2022.
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4/28 杉崎
Ohara, et al., “Reversible assembly of an artificial protein nanocage using alkaline earth metal ions” J. Am. Chem. Soc. (2023).
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2024年度
4/22 吉田
Purcell, et al., “Iron-sulfur cluster assembly scaffold protein IscU is required for activation of ferric updtake regulator (Fur) in Escherichia coli” J. Biol. Chem. 2024, 300, 107142.
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6/3 相塲
Wang, et al., “One-pot de novo synthesis of [4Fe-4S] protein using a recombinant SUF system under aerobic conditioins.” ACS Synth. Biol. 2023.
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6/10 吉田
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7/1 宍戸
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7/29 相塲
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8/6 田尻
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9/2 田尻
Ida, et al. “Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling” PNAS (2014) 111(21) , 7606-7611.
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9/9 宍戸
Siepi, et al., “Fluorescent peptide dH3w: A sensor for environmental monitoring of mercury (II)” PLos One (2018) 13(10) e0204164.
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10/7 相塲
Saini, J., et al., “The minimal SUF system is not required for Fe-S cluster biogenesis in the methanogenic archaeon Methanosarcina acetivorans”. Sci. Rep. (2023), 13, 15120.
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10/28 宍戸
Fatima, S., et al. “Engineering a Conformationally Switchable Artifficial Metalloprotein”
J. Am. Chem. Soc. (2022), 144, 21606-21616.
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10/28 田尻
Shaposhnikov, M. V., et al., “Simultaneous activation off the hydrogen sulfide biosynthesis ggenes (CBS and CSE) induces sex-specific geroprotective efffects in Drosophila melanogaster.” Biogeromtology, (2023), 24, 275-292.
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11/25 宍戸
Wang, L., et al. “Exploring the interaction between Cry1Ac protein and Zn2+, Cd2+ metal ions by fluorescence quenching and molecular docking approaches”
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11/25 田尻
Araki, S., et al., Cystathionine γ-lyase self-inactivates by polysulfidation during cystine metabolism”,
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12/23 吉田
Bu, et al., “Structural Basisi of the Inhibition of L-methionine γ-lyase from Fusobacterium nucleatum” Int. J. Mol. Sci. (2023) 24, 1651.
https://www.mdpi.com/1422-0067/24/2/1651
12/23 相塲
Wu, et al. “Characterization of membrane-bound sulfane reductase: A missing link in the evolution of modern day respiratory complexes” J. Biol. Chem. (2018) 293 ,16687-16696
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1/6 吉田
2023年度
5/1 大塚
Hsiao, et al., “Crystal structure of the α-ketoglutarate-dependent non-heme iron oxygenase CmnC in capreomycin biosynthesis and its engineering to catalyze hydroxylation of the substrate enantiomer” Frontier.Chem. 2022
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5/15 吉田
Vaccaro, et al., “Biological iron-sulfur storage in a thioferrate-protein nanoparticle” Nat. Commun. 2017
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5/29 小川
Jespersen, et al. “Structures of the sulfite detoxifying F420-dependent enzyme from Methanococcales” Nat. Chem. Biol. 2022
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6/19 宍戸
Biester, et al. “Visualizing the gas channel of a monofunctional carbon monoxide dehydrogenase” J. Inorg. Biochem. 2022
https://www.sciencedirect.com/science/article/pii/S0162013422000630
6/26 林
Pang, Y. et al., “Roles of conserved active site residues in the IscS Cysteine desulfurase reaction” Front. Microbiol. (2023)
https://www.frontiersin.org/articles/10.3389/fmicb.2023.1084205/full
7/6 大塚
Matoba, Y., et al. “Cyclization mechanisms catalyzed by an ATP-grasp enzyme essential for D-cycloserine biosynthesis” FEBS J. (2020), 287, 2763-2778.
https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15163
7/31 吉田
Vali, SW, et al., “The Pyrococcus furiosus ironome is dominated by [Fe4S4]2+ clusters or thioferrate-like iron depndening on the availability of elemental sulfur” J. Biol. Chem. (2021) 296, 100710
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8/28 小川
Nim, et al., “Delivering a toxic metal to the active site of urease” Sci. Adv. (2023) 9 eadf7790
https://www.science.org/doi/10.1126/sciadv.adf7790
10/2 宍戸
Kim, et al., “Metal-induced fluorescence quenching of photoconvertible fluorescent protein DendFP”
https://www.mdpi.com/1420-3049/27/9/2922
10/23 林
Bennett, et al., “Native mass spectrosmetric studies of IscSU reveal a cncerted, sulfur-initiated mechanism of iron-sulfur cluster assembly”
https://pubs.rsc.org/en/content/articlelanding/2023/sc/d2sc04169c
10/23 大塚
Shatalin, et al. “Inhibitors of bacterial H2S biogenesis targeting antibiotic resistance and tolerance”
https://www.science.org/doi/full/10.1126/science.abd8377
11/6 林
Karunakaran, et al. “ Structurall analysis of Atopobium parvulum SufS cystgeine desulfurase linked to Crohn’s disease” FEBS Lett. 2022
https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.14295
11/13 小川
Gabler, et al., “Iron insertion into coproporphyrin III-ferrochelatase complex: Evidence for an intermediate distorted catalytic species” Protein Sci. (2023)
https://onlinelibrary.wiley.com/doi/full/10.1002/pro.4788
11/13 吉田
Martic, et al., “Heterometallic [AgFe3S4] ferredoxin variants: synthesis, characterization , and the first crystal structure of an engineered heterometallic iron-sulfur protein” J. Biol. Inorg. Chem. (2013)
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11/20 宍戸
Zou, et al, “Mutant Flavin-based fluorescent protein sensors for detedting intracellular zinc and copper in Escherichia coli” (2022)
https://pubs.acs.org/doi/10.1021/acssensors.2c01376
12/11 大塚
Matoba, et al., “Cyclization mechanism catalyzed by an ATP-grasp enzyme essential for D-cycloserine biosynthesis” (2020) FEBS J.
https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15163
12/18 林
Silva, et al., “Structural basis of RICs iron donation for iron-sulfur cluster biogenesis” Front. Microbiol. (2021)
https://www.frontiersin.org/articles/10.3389/fmicb.2021.670681/full
12/15 大塚
Pederick, et al., “D-alanine-D-alanine ligase as a model for the activation of ATP-grasp enzymes by monovalet cations” J. Biol. Chem. (2023)
https://www.jbc.org/article/S0021-9258(17)49431-2/fulltext
12/25 吉田
Basak, et al,, “Stepwise O2-induced rearrangement and disassembly of the [NiFe4(OH)(u3-S)4] Active site cluster of CO dehydrogenase” (2023)
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2022年度
4/20 （水） 大塚
Kawakamim, R., et al., “Crystal structure of a novel type of ornithine δ-amino transferase from the hyperthemophilic archaeon Pyrococcus horikoshii” Int. J. Biol. Macromol. 208, 731-740, 2022.
https://www.sciencedirect.com/science/article/pii/S0141813022005840?via%3Dihub
4/20 （水） 小川
Fyfe, CD., et al., “Crystallographic snapshots of a B12-dependent radical SAM methyltransferase” Nature 602, 336- 342, 2022.
https://www.nature.com/articles/s41586-021-04355-9
4/27 （水） 村上
Zhou, J., et al., “Structural evidence for a [4Fe-5S] intermediate in the non-redox desulfuration of thiouracil” Angew Chem Int Ed , 60, 424- 431, 2021.
https://onlinelibrary.wiley.com/doi/full/10.1002/anie.202011211
4/27 （水） 國近
Barra, L., et al., “β-NAD as a building block in natural product biosynthesis” Nature , 600, 754- 758, 2021.
https://www.nature.com/articles/s41586-021-04214-7
5/25 （水） 小山田
Shisaka, Y., et al. “Tetraphenylporphyrin enters the ring: first example of a complex between
highly bulky porphyrins and a protein” ChemBioChem 2022, e202200095.
https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202200095
5/25 （水） 槇
Olmos, J., et al., “A highly conserved iron-sulfur cluster assembly machinery between humans
and amoeba Dictyostelium discoideum: the characteriation of frataxin.” Int. J. Mol. Sci. 2020, 21, 6821.
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6/1 （水） 佐々木
Solomon, J.B., et al., “Characterization of a nitrogenase iron protein substituted with a synthetic [Fe4Se4] cluster” Angew. Chem. Int. Ed. 2022 134, e202202271.
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6/8 （水） 鄭
Deere, T.M., et al., “Methanosarcina acetivorans contains a functional ISC system for iron-sulfur cluster biogenesis”BMC Microbiology (2020), 20:323.
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6/8 （水）向井
Fontenot, et al., “Ferric uptake regulators (Fur) from Vibrio cholerae and Helicobacter pylori bind a [2Fe-2S] cluster in response to elevation of intracellular free iron content” Biometals (2022), in press.
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6/15 (水）宍戸
Oohora, K., et al., “Reactivity of myoglobin reconstituted with cobalt corrole toward hydrogen peroxide” Int. J. Mol. Sci. (2022), 23, 4829.
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6/15 (水）村上
Benoit, S., et al., “A two-hybrid system reveals previously uncharacterized protein-protein interactions within the Helicobacter pylori NIF iron-sulfur maturation system” Sci. Rep. (2021), 11, 10794.
https://www.nature.com/articles/s41598-021-90003-1
6/22 (水）大塚
Yadav, P. K., et al., “S-3-carboxypropyl-L-cysteine specifically inhibits cystathionine γ-lyase-dependent hydrogen sulfide synthesis” J. Biol. Chem. (2019), 294, 11011-11022.
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6/22 (水）小川
Robescu, M. S., et al., “Asymmetric proton transfer catalysis by stereocomlementary old yellow enzymes for C=C bond isomerization reaction” ACS Catal. (2022), 12, 7396-7405.
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6/29 齋藤
Gabler, T., et al., “Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen-bonding interactions of the four propoionate groups” FEBS J. (2022)
289, 1680-1699.
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6/29 槇
Wittenborn, E.C., et al., “The solvent-exposed Fe-S D-cluster contributes to oxygen-resistance in Desulfovibrio vulgaris Ni-Fe carbon monoxide dehydrogenase” ACS Catal. (2020) 10, 7328-7335.
https://pubs.acs.org/doi/10.1021/acscatal.0c00934
7/7 小山田
Yang, J., et al. “Crucial roles of a pendant imidazole ligand of a cobalt porphyrin complex in the stoichiometeric and catalytic reduction of dioxygen” Angew. Chem. Int. Ed. accepted.
https://onlinelibrary.wiley.com/doi/10.1002/anie.202208143
7/7 吉岡
Uzarska, M. A., et al. “During FeS cluster biogenesis, ferredoxin and frataxin use overalpping binding sites on yeast cysteine desulfurase Nfs1” J. Biol. Chem. (2022), 298(2), 101570.
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9/28 大塚
Shen, W., et al. “2-Aminoacylate stress damages diverse PLP-dependent enzymes in vivo” J. Biol. Chem. (2022). 298, 101970.
https://www.sciencedirect.com/science/article/pii/S0021925822004100?via%3Dihub
9/28 村上
Fan, X., et al. “Iron-regulated assembly of the cytosolic iron-sulfur cluster biogenesis machinery” J. Biol. Chem., (2022) 298, 102094
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10/5 斎藤
Evans, R., et al. “Selective cystine-to-selenocysteine changes in a [NiFe]-hydrogenase confirm a special position for catalysis and oxygen tolerance” Proc. Natl. Acad. Sci. USA (2022). 118, e21009211.
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10/5 佐々木
Karunakaran, G., et al. “Structural analysis of Atopobium parvulum SufS cysteine desulfurase linked to Crohn’s disease” FEBS Lett., (2022) 596, 898-909
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10/19宍戸
Wittenborn, E., et al. “Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase”eLife (2018). 7, e39451
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10/19 鄭
Ren, X., et al. “Identification of an intermediate form of ferredoxin that binds only iron suggests that conversion to holo-ferredoxin is independent of the ISC system in Escherichia coli ” Appl. Environmental Microbiol., (2021) 87, e03153-20
10/26 小川
Lubner, et al., Site-Differentiated [4Fe-4S] Cluster Controls Electron Transfer Reactivity of Clostridium acetobutylicum [FeFe]-hydrogenase I Chem. Sci. 2022. 16, 4581
https://pubs.rsc.org/en/content/articlelanding/2022/sc/d1sc07120c
10/26 槇
Jeoung, et al., A Morphing [4Fe-3S-nO]-Cluster within a Carbon Monoxide Dehydrogenase Scaffold, Angew. Chem. Int. Ed. 2022, 61, e202117000
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11/2 小山田
Tria, et al., “Gene duplication s are at least 50 times less frequent than gene transfers in prokaryotic genomes” Genome Biol. Evol. 2021 evab224.
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11/16 向井
Wang, et al.,“The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone” J. Biol. Chem. (207.17) 292 10061-10067.
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11/16 小川
Funck et al., “Discovery of a Ni2+-dependent guanidine hydrolase in bacteria” Nature (2002) 603 515-521.
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11/24 宍戸
Soon, et al., “A disulphide bond-mediated hetero-dimer of a hemoprotein and a fluorescent protein exhibiting efficient energy transfer” RSC advances
https://pubs.rsc.org/en/content/articlelanding/2022/ra/d2ra05249k#fn1
11/24 鄭
Tripathi, et al, “Mycobacterium tuberculosis requires SufT for Fe-S cluster maturation, metabolism, and survival in vivo” PLoS Pathogens
https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1010475
11/30 佐々木
He, et al., “Structural and Functional Analysis of the Pyridoxal Phosphate
Homeostasis Protein YggS from Fusobacterium nucleatum” Molecules
https://www.mdpi.com/1420-3049/27/15/4781
11/30 Xu, et al., “Gene Fusion and Directed Evolution to Break Structural Symmetry
and Boost Catalysis by an Oligomeric C-C Bond-Forming Enzyme” Angew. Chem. Int. Ed.
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12/7 大塚
Pederick, et al., “Discovery of an ʟ-amino acid ligase implicated in Staphylococcal sulfur amino acid metabolism” J. Biol. Chem.
https://www.jbc.org/article/S0021-9258(22)00835-3/fulltext
12/7 向井
Tasnim, et al., “Exploring the FMN binding site in the mitochondrial outer membrane
protein mitoNEET” Free Radic. Biol. Med.
https://www.sciencedirect.com/science/article/abs/pii/S0891584920308522?via%3Dihub
12/14 村上
Gomkale, et al., “Mapping protein interactions in the active TOM-TIM23 supercomplex” Mat Commun. 2021
https://www.nature.com/articles/s41467-021-26016-1
12/21 小山田
Milenkin, et al., “Translational frameshifting in the chlD gene gives a clue to the coevolution of the chlorophyll and cobalamin biosyntheses” Microorganisms 2022, 10, 1200.
https://www.mdpi.com/2076-2607/10/6/1200?type=check_update&version=1
12/21 槇
Baek, et al., “Structural analysis of the overoxidized Cu/Zn-superoxide dismutase in ROS-induced ALS filament formation” Commun. Biol. 2022, 5, 1085.
https://www.nature.com/articles/s42003-022-04017-0
2021年度
4/19 （月）小山田
Osman, D., et al., “Bacterial sensors define intracellular free energies for correct enzyme metalation.” Nat. Chem. Biol. 2019, 15, 241-249.
https://www.nature.com/articles/s41589-018-0211-4
4/26 （月）吉岡
Konarev, P. V., et al., “Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS” J. Biol. Chem. 2013, 288, 24777-24787.
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4/26 （月）槇
Jagilinki, B. P., et al., “In vivo biogenesis of a de novo iron-sulfur cluster protein” ACS Synth. Biol. 2020, 9, 3400-3407.
https://pubs.acs.org/doi/10.1021/acssynbio.0c00514
5/10 （月）村上
Cranford-Smith, T., et al., “Iron is a ligand of SecA-like metal-binding domains in vivo” J. Biol. Chem. 2020, 295, 7516-7528.
https://www.sciencedirect.com/science/article/pii/S0021925817502811?via%3Dihub
5/10 （月）國近
Wensien, M., et al., “A lysine-cysteine redox switch with an NOS bridge regulates enzyme function” in press.
https://www.nature.com/articles/s41586-021-03513-3
5/31 （月）小山田
Perkins, L., et al., “De novo biosynthesis of a nonnatural cobalt porphyrin cofactor in E. coli and incorporation into hemoproteins” Proc. Natl. Acad. Sci. USA 2021, 118, e2017625118.
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5/31 （月） 槇
Fidai, I., et al., “Glutathione-complexed [2Fe-2S] clusters function in Fe-S cluster storage and trafficking” J. Biol. Inorg. Chem. 2016, 21, 887-901.
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6/7 （月）吉岡
Eshelman, K., et al., “Inhibiting the BfrB:Bfd interaction in Psedomonas aeruginosa causes irreversible iron accumulation in bacterioferritin and iron defficiency in the bacterial cytosol” Metallomics 2017, 9, 646-659.
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6/7 （月） 村上
Stevens C.A. et al., “A minimalistic cyclic ice-binding peptide from phage display” Nat. Commun. 2021, 12, 2675.
https://www.nature.com/articles/s41467-021-22883-w
6/14 （月） 葛
Moore, S., et al., “Elucidation of the anaerobic pathway for the corrin component of cobalamin (vitamin B12)” Proc. Natl. Acad. Sci. USA 2013, 110, 14906-14911.
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6/14 （月） 高原
Sushuko, T. et al., “A new twist of rubredoxin function in M. tuberculosis” Bioorg. Chem. 2021, 109, 104721.
https://www.sciencedirect.com/science/article/pii/S0045206821000973
6/21 （月） 大塚
Cepeda, M. R., et al., “The role of extended Fe4S4 cluster ligands in mediating sulfite reductase hemoprotein activity” Biochim. Biophys. Acta, 2018, 1866, 933-940.
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6/21 （月） 倉知
Sushuko, T. et al., “Methanosarcina acetivorans contains a functional ISC system for iron-sulfur cluster biogenesis” BMC Microbiol. 2020, 20, article number:323
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6/28 （月） 高岡
Cohen, S. E., et al., “Crystallographic characterization of the carbonylated A-cluster in carbon monoxide dehydrogenase/acetyl-CoA synthase” ACS Catal. 2020, 10, 9741-9746.
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6/28 （月） 國近
Sushuko, T. et al., “Dph3 enables aerobic diphthamide biosynthesis by donating one iron atom to transform a [3Fe-4S] to a [4Fe-4S] cluster in Dph1-Dph2” J. Am. Chem. Soc. in press.
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7/5 （月） 市原
Sadik, M. et al., “[Fe-S] biogenesis and unusual assembly of the ISC scaffold complex in the Plasmodium falciparum mitochondrion” Mol. Microbiol. in press.
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9/27 （月） 大塚
Brewster J. L., et al., “Structures and kinetics of Thermotoga maritima MetY reveal new insights into the predominant sulfurylation enzyme of bacterial methionine biosynthesis” J. Biol. Chem. 2021, 296, 100797.
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9/27 （月） 倉知
Anand K, et al., “Mycobacterium tuberculosis SufR responds to nitric oxide via its 4Fe-4S cluster and regulates Fe-S cluster biogenesis for persistence in mice” Redox Biol. 2021, 46, 102062.
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10/4 （月） 高原
Ittarat W., et al., “Rubredoxin from the green sulfur bacterium Chlorobaculum tepidum do9nates a redox equivalent to the flavodiiron protein in an NAD(P)H dependent manner via ferredoxin-NAD(P)+ oxidoreductase” Arch. Microbiol. 2021, 203, 799-808.
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10/4 （月） 葛
Gashiri, G, et al., “A revised biosynthetic pathway for the cofactor F420 in prokaryotes” Nat. Commun. 2019, 10, 1558.
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10/11 （月） 吉岡
Phuong N. L VO, et al., “Optimized expression of Hfq protein increases Escherichia coli growth.” J. Biol. Enginner. 2021, 15, 7.
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10/11 （月） 村上
Zhao, et al., “The Nbp35/ApbC homolog acts as a nonessential [4Fe-4S] transfer protein inmethanogenic archaea.” FEBS Lett. 2020, 594, 924-932.
https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13673
10/11 （月） 槇
Rosenbach, et al., “The Asp1 pyrophosphatase from S. pombe hosts a [2Fe-2S]2+ cluster in vivo. 2021, 26, 93-108.
https://link.springer.com/article/10.1007/s00775-020-01840-w
10/18 （月） 小山田
Inaba, et al., “Calix[3]pyrrole: A missing link in porphyrin-related chemistry” J. Am. Chem. Soc. 2021, 143, 12355-12360.
https://pubs.acs.org/doi/10.1021/jacs.1c06331
10/18 （月） 小川
Zhao, et al., “Design of an in-cell protein crystal for the environmentally responsible construction of a supramolecular filament.” Angew. Chem. Int. Ed. 2021, 60, 12341-12345.
https://onlinelibrary.wiley.com/doi/full/10.1002/anie.202102039
10/25 （月） 市原
Zhang, et al. “Structural snapshots ofTRPV1 reveal mechanism of polymodal functionality” Cell 2021, 184, 5138-5150.
https://www.sciencedirect.com/science/article/pii/S009286742100982X?via%3Dihub
10/25（月） 高岡
Wittenborn, et al., “Structural insight into metallocofactor maturation in carbon monoxide dehydrogenase.” J. Biol. Chem. 2019, 294, 13017-13026.
https://www.sciencedirect.com/science/article/pii/S0021925820432375?via%3Dihub
11/1（月） 相羽
Maio, et al., “Fe-S cofadctors in the SARS-CoV-2 RNA-dependent RNA polymerase are potential antiviral targets.” Science 2021, 373, 236-241.
11/1（月） 國近
Esakova, et al., “Sructural basis for tRNA methylthiolation by the radical SAM enzyme MiaB.” Nature 2021, 597, 566-570.
https://www.nature.com/articles/s41586-021-03904-6
11/8 （月) 倉知
Liu, G., et al. “Heme biosynthesis depends on previously unrecognized acquisition of iron-sulfur cofactors in human amino-levulinic acid dehydratase” Nat. Commun.
https://www.nature.com/articles/s41467-020-20145-9
11/15（月) 大塚
Wang, H., et al., “Crystal structures clarifiy cofactor binding of plant tyrosine decarboxyase” Biochem. Biophys. Res. Commun. 2020, 523, 500-505.
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11/15（月) 高原
Scheurer, M., et al., “The rupture mechanism of rubredoxin is more complex than previously thought” Chem. Sci. 2020, 11, 6036.
https://pubs.rsc.org/en/content/articlelanding/2020/sc/d0sc02164d
11/15（月) 葛
Allen, K.D., et al., “Discovery of multiple modified F430 coenzymes in methanogens an anaerobic methanotrophic arcaea suggests possible new roles for F430 in nature” Appl. Environ. Microbiol. 2014, 80, 6403-6412.
https://journals.asm.org/doi/10.1128/AEM.02202-14
11/22（月) 高原
Williams, S.C., et al., “Investigation of the prevalence and catalytic activity of rubredoxin-fused alkane monoxygenases (AlkBs)” J. Inorg. Biochem. 2021, 219, 111409.
https://www.sciencedirect.com/science/article/pii/S0162013421000568
11/22（月) 吉岡
Vo, C.-D.-T., et al., “The O2-independent pathway of ubiquinone biosynthesis is essential for denitrification in Pseudomonas aeruginosa” J. Biol. Chem. 2020, 295, 9021-9032.
11/22（月) 小山田
Mayer, R. J., et al., “Mechanistic Insight into Metal Ion-Catalyzed Transamination” J. Am. Chem. Soc. 2021,143, 19099-19111.
12/6 槇
Hendricks, A. L., et al., “Characterization and Reconstitution of Human Lipoyl Synthase (LIAS) Supports ISCA2 and ISCU as Primary Cluster Donors and an Ordered Mechanism of Cluster Assembly” Int. J. Mol. Sci. 2021, 22, 1598.
https://www.mdpi.com/1422-0067/22/4/1598
12/6 村上
Reddy, S. S., et al., “Hydrogen bond surrogate-constrained dynamic antiparallel β-sheets” ChemBioChem 2021, 22, 2111-2115.
https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202100028
12/13 小川
Patwardan, et al., “Nickel–Sulfonate Mode of Substrate Binding for Forward and Reverse Reactions of Methyl-SCoM Reductase Suggest a Radical Mechanism Involving Long-Range Electron Transfer” J. Am. Chem. Soc. 2021, 143, 5481-5496.
https://pubs.acs.org/doi/10.1021/jacs.1c01086
12/13 市原
Jordan, et al., “Spontaneous assembly of redox-active iron-sulfur clusters at low concentrations of cysteine” Nat. Commun. 2021, 12, 5925.
https://www.nature.com/articles/s41467-021-26158-2
12/20 國近
Freibert, et al., “N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization” Nat. Commun. 2021, 12, 6902. https://www.nature.com/articles/s41467-021-27122-w
12/20 高岡
Hagen, et al., “EPR spectrscopy of putative enzyme intermediates in the NO reductase and the auto-nitrosylation reaction of Desulfovibrio vulgaris hybrid cluster protein” FEBS Lett., 2019, 593, 3075-3083.
https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.13539
12/20 相羽
Jain, et al., “Assembly of the [4Fe-4S] cluster of NFU1 requires the coordinated donation of two [2Fe-2S] clusters from the scaffold proteins, ISCU2 and ISCA1” Human Molecular genetics, 2020, 29, 3165-3182.
https://academic.oup.com/hmg/article/29/19/3165/5889935
2020年度
5/18 （月）相羽
Roland, V., et al., “The plastidial Arabidopsis thaliana NFU1 protein binds and delivers [4Fe-4S] clusters to specific client proteins” J. Biol. Chem. 2020, 295, 1727-1742. DOI: 10.1074/jbc.RA119.011034
5/18 （月）小川
Radle, M., et al., “Methanogenesis marker protein 10 (Mmp 10) from Methanosarcina acetivorans is a radical S-adenosylmethionine methylase that unexpectedly requires cobalamin” J. Biol. Chem. 2019, 294, 11712-11725. DOI: 10.1074/jbc.RA119.007609
5/25（月）市原
Martínez-Alcántar L., et al., “Over-expression of Isu1p and Jac1p increases the ethanol tolerance and yield by superoxide and iron homeostasis mechanism in an engineered Saccharomyces cerevisiae yeast.” J. Industrial. Microbiol. Biotechnol. 2019, 46, 925-934. DOI: 10.1007/s10295-019-02175-5
5/25 （月）髙岡
van Lis, R., et al., “Hybrid cluster proteins in a photosynthetic microalga” FEBS J. 2020, 287, 721-735. DOI: https://doi.org/10.1111/febs.15025
6/1（月）槇
Miyanaga, A., et al., “Structure-based analysis of the molecular interactions between acyltransferase and acyl carrier protein in vicenistatin biosynthesis” Proc. Natl. Acad. Sci. USA 2016, 113, 1802-1807. DOI:10.1073/pnas.1520042113
6/1 （月）小山田
Galambas, A., et al., “Radical S-adenosylmethionine maquette chemistry: Cx3Cx2C peptide coordinated redox active [4Fe–4S] clusters” J. Biol. Inorg. Chem. 2019, 24, 793-807. DOI: 10.1007/s00775-019-01708-8
6/1 （月）吉岡
Corless, E.I., et al., “Elevated Expression of a Functional Suf Pathway in Escherichia coli BL21(DE3) Enhances Recombinant Production of an Iron-Sulfur Cluster-Containing Protein” J. Bacteriol. 2020, 202, e00496-19. DOI: 10.1128/JB.00496-19
6/8 （月）國近
Lin, C.-W., et al., “Molecular Mchanism of ISC Iron-Sulfur Cluster Biogenesis Revealed by High-Resolution Native Mass Spectrometry” J. Am. Chem. Soc. 2020, 142, 6018-6029. DOI: 10.1021/jacs.9b11454
6/8 （月）中村
de Chiara, C., et al., “D-Cycloserine destruction by alanine racemase and the limit of irreversible inhibition” Nat. Chem. Biol. 2020,16, 686-694. DOI: 10.1038/s41589-020-0498-9
6/15 （月）小川
Pennington, J.M., et al., “Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site” Nat. Commun. 2020,16, 686-694. DOI: 10.1038/s41467-020-14722-1
6/15 （月）森
Nonaka, G., et al., “Cysteine degradation gene yhaM, encoding cysteine desulfidase, serves as a genetic engineering target to improve cysteine production in Escherichia coli” AMB Express. 2017,7, 90. DOI:10.1186/s13568-017-0389-y
6/22 （月）村上
Nie, X., et al., “Multiple Sense and Antisense Promoters Contribute to the Regulated Expression of the isc-suf operon for iron-sulfur cluster assembly in Rhodobacter” Microorganisms. 2019, 7, 671. DOI: 10.3390/microorganisms7120671
6/22 （月）高岡
Ross Belvin, B., et al., “The Porphyromonas gingivalis Hybrid Cluster Protein Hcp Is Required for Growth with Nitrite and Survival with Host Cells” Infecct. Immun. 2019, 87, e00572-18. DOI: 10.1128/IAI.00572-18
6/29 （月）市原
Gervason, S., et al., “Physioilogically relevant reconstitution of iron-sulfur cluster biosynthesis uncovers persulfide-processing functions of ferredoxin-2 and frataxin ” Nat. Commun. 2019, 10, 3566. DOI: 10.1038/s41467-019-11470-9
6/29 （月）相羽
Pourciau, C., et al., “Regulation of Iron Storage by CsrA Supports Exponential Growth in Escherichia coli ” mBio 2019, 10, e01034-19. DOI: 10.1128/mBio.01034-19
7/ 27（月）室賀
Jasper, J., et al., “Chimeric Interaction of Nitrogenase-Like Reductases with the MoFe Protein of Nitrogenase” ChemBioChem 2020, 21, 1733-1741. DOI: 10.1002/cbic.201900759
7/27 （月）入江
depaula, C.P., et al., “Glutaredoxin-like protein (GLP)- a novel bacteria sulfurtransferase that protects cells against cyanide and oxidative stresses” Appl. Microbiol. Biotechnol. 2020, 104, 5477-5492. DOI: 10.1007/s00253-020-10491-5
9/28 （月）村上
Chen, M., et al., “The [4Fe-4S] cluster of sulfurtransferase TtuA desulfurizes TtuB during tRNA modification in Thermus thermophilus” Comm. Biol. 2020, 3, 168.
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9/28 （月）小川
Dong, C.-S., et al., “Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase” Proc. Natl. Acad. Sci. USA 2020, 117, 8455-8461. DOI: 10.1073/pnas.1920244117
10/5 （月）槇
Dunkle, J., et al., “Structural evidence for dimer-interface driven regulation of the type II cysteine desulfurase, SufS”Biochemistry 2019, 58, 687-696.
https://pubs.acs.org/doi/10.1021/acs.biochem.8b01122
10/5 （月）市原
Weiler, B. D., et al., “Mitochondrial [4Fe-4S] protein assembly involves reductive [2Fe-2S] cluster fusion on ISCA1-ISCA2 by electron flow from ferredoxin FDX2” Proc. Natl. Acad. Sci. USA 2020, 117, 20555-20565.
https://www.pnas.org/content/117/34/20555
10/5 （月）吉岡
Friedrich T., et al., “ErpA is important but not essential for the Fe/S cluster biogenesis of escherichia coli NADH:ubiquinone oxidoreductase (complex I)” BBA Bioenergetics 2020, 1861, 148286.
https://www.sciencedirect.com/science/article/pii/S0005272820301365
10/12 （月）森
Kondoh, M., et al., “L-Cysteine production by metabolically engineered Corynebacterium glutamicum” Appl. Microbiol. Biotechnol. 2019, 103, 2609-2619.
https://link.springer.com/article/10.1007/s00253-019-09663-9
10/12 （月） 小山田
Kondoh, M., et al., “Probing the structural plasticity of an archaeal primordial cobaltochelatase CbiXS” Protein Engineer. Des. Sel. 2007, 20, 257-265.
https://academic.oup.com/peds/article/20/6/257/2964607
10/19 （月） 國近
Kang, W., et al., “Structural evidence for a dynamic metallocobactor during N2 reduction by Mo-nitrogenase” Science 2020, 6497, 1381-1385.
https://science.sciencemag.org/content/368/6497/1381.long
10/19 （月） 室賀
Kang, W., et al., “Defining Intermediates of Nitrogenase MoFe protein during N2 reduction under Photochemical Electron Delivery from CdS quantum dots”
J. Am. Chem. Soc. 2020, 142, 14324-14330.
https://pubs.acs.org/doi/10.1021/jacs.0c06343
10/26 （月） 中村
North, J. A., et al., “A nitrogenase-like enzyme system catalyzes methionine, ethylene, and methane biogenesis” Science 2020, 369, 1094-1098.
https://science.sciencemag.org/content/369/6507/1094
10/26 （月） 入江
Martinez-Alcantar, L., et al., “The isc gene cluster expression ethanol tolerance associated improves its ethanol production by organic acids flux redirection in the ethanologenic Escherichia coli KO11 strain”
World J. Microbiol. Biotechnol. 2019, 35, 189.
https://link.springer.com/article/10.1007/s11274-019-2769-8
11/2 （月） 高岡
Tosha, T., et al., “Capturing an initial intermediate during the P450nor enzymatic reaction using time-resolved XFEL crystallography and caged-substrate” Nat. Commun. 2017, 8, 1585.
https://www.nature.com/articles/s41467-017-01702-1
11/2 （月） 小山田
Romao, C. V., et al., “Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization” Proc. Natl. Acad. Sci. USA 2011, 108, 97-102.
https://www.pnas.org/content/108/1/97
11/2 （月） 槇
Shinohara, F., et al., “Structural basis for the isotype-specific interactions of ferredoxin and ferredoxin: NADP+ oxidoreductase: an evolutionary switch between photosynthetic and heterotrophic assimilation” Photosynth. Res. 2017, 134, 281-289.
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11/9 （月） 國近
Kang, W., et al., “Crystallographic analysis of NifB with a full complement of clusters: Structural insights into the radial SAM-dependent carbide insertion during nitrogenase cofactor assembly” Angew. Chem. Int. Ed. accepted.
https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.202011367
11/9 （月） 吉岡
Rontenot, C. R., et al., “Ferric uptake regulator (Fur) reversibly binds a [2Fe-2S] cluster to sense intracellular iron homeostasis in Escherichia coli” J. Biol. Chem. in press.
https://www.jbc.org/content/295/46/15454.long
11/16 （月） 森
Beauchene, N. A., et al., “O2 availability impacts iron homeostasis in Escherichia coli” Proc. Natl. Acad. Sci. USA, 114, 12261-12266, 2017
https://www.pnas.org/content/114/46/12261
11/30 （月） 村上
Liu, L., et al., “Structural analysis of an L-cysteine desulfurase from an Ssp DNA phosphorothioation system” mBio 11, e00488-20, 2020
https://mbio.asm.org/content/11/2/e00488-20
11/30 （月） 市原
Kleczewska, M., et al., “Biochemical convergence of mitochondrial Hsp70 system specialized in iron-sulfur cluster biogenesis” Int. J. Mol. Sci., 21, 3326, 2020
https://www.mdpi.com/1422-0067/21/9/3326
12/7 （月） 中村
Liu, L., et al., “The molecular basis of thioalcohol production in human body odour” Sci. Rep. 10, 12500 (2020).
https://www.nature.com/articles/s41598-020-68860-z
12/7 （月） 入江
Bali, A.P., et al., “Improved biotin, thiamin, and lipoic acid biosynthesis by engineering the global regulator IscR” Metabolic Engineering, 60, 97-109, 2020.
https://www.sciencedirect.com/science/article/pii/S1096717620300549
12/14 （月） 小川
Chen., J.-H., et al., “Architecture of the photosynthetic complex from a green sulfur bacterium” Science 370, eabb6350, (2020).
https://science.sciencemag.org/content/370/6519/eabb6350/tab-pdf
12/14 （月） 室賀
Brown, K. A., et al., “Light-driven dinitorgen reduction catalyzed by a CdS:nitrogenase MoFe protein hybrid”, 352, 448-450, 2020.
https://science.sciencemag.org/content/352/6284/448.long
12/21（月） 高岡
Olson, A. C., et al., “The Involvement of hybrid cluster protein 4, HCP4, in Anaerobic Metabolism in Chlamydomonas reinhardtii” PLoS ONE 11, e0149816, (2016).
https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0149816
12/14 （月） 相羽
Wachnowsky, C., et al., “Iron-sulfur cluster exchange reactions mediated by the human Nfu protein”, 21, 825-836, 2016.
https://link.springer.com/article/10.1007%2Fs00775-016-1381-8
2019年度
4/22 （月）入江
Li, J., et al., “Zinc toxicity and iron-sulfur cluster biogenesis in Escherichia coli” Appl. Environ. Microbiol. 2019, in press. DOI: 10.1128/AEM.01967-18
4/22 （月）室賀
Rajeshkumar., P. et al., “Functional analysis of iron-sulfur cluster biogenesis (SUF pathway) from Plasmodium vivax clinical isolates” Experimental Parasitology 2019, 198, 53-62. DOI: https://doi.org/10.1016/j.exppara.2019.01.015
5/20 （月）入江
Giordano N., et al., “Cysteine Desulfurase IscS2 Plays a Role in Oxygen Resistance in Clostridium difficile” Infect. lmmun. Vol. 86, Issue 8, e00326-18
https://iai.asm.org/content/86/8/e00326-18.long
5/20 （月）室賀
Kim., D. et al., “Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems” Biochemistry, vol.57, issue 35, pp.5210-5217.
https://pubs.acs.org/doi/10.1021/acs.biochem.7b01275
5/27 （月）市原
Nyvltova, E., et al., “NIF-type iron-sulfur cluster assembly system is duplicated and distributed in the mitochondria and cytosol of Mastigamoeba balamuthi” Proc. Natl. Acad. Sci. USA 2013, vol.110, pp.7371-7376.
https://www.pnas.org/content/110/18/7371.long
5/27 （月）小川
Charan., M. et al., “[Fe-S] cluster assembly in the apicoplast and its indispensability in mosquito stages of the malaria parasite” FEBS J., 2017 vol.284,, pp.2629-2648.
https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.14159
6/3 （月）中島
Nonaka., A. et al., “Accessory Proteins of the Nitrogenase Assembly, NifW, NifX/NafY, and NifZ, Are Essential for Diazotrophic Growth in the Nonheterocystous Cyanobacterium Leptolyngbya boryana” Front. Microbiol., 2019 vol.10, article 495.
https://www.frontiersin.org/articles/10.3389/fmicb.2019.00495/full
6/3 （月）中村
Marchand., J.A. et al., “Discovery of a pathway for terminal-alkyne amino acid biosynthesis” Nature, 2019 vol.567,, pp.420-424.
https://www.nature.com/articles/s41586-019-1020-y
6/17 （月）相羽
Xu, L. et al., “Crystal structure of S. aureus YlaN, an essential leucine rich protein involved in the control of cell shape” Structure, 2007 vol.68, pp.438-445.
https://onlinelibrary.wiley.com/doi/full/10.1002/prot.21377
6/17（月）國近
Fox, N.G. et al., “Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism” Nat. Commun., 2019 vol.10, article number:2210.
https://www.nature.com/articles/s41467-019-09989-y
6/24 （月）櫻井
Pandey, A. K. et al., “Mitochondria export iron-sulfur and sulfur intermediates to the cytoplasm for iron-sulfur cluster assembly and tRNA thiolation in yeast” J. Biol. Chem., 2019 in press.
http://www.jbc.org/content/early/2019/04/30/jbc.RA119.008600.abstract
6/24（月）村田
Pardoux, R. et al., “The bacterial MrpORP is a novel Mrp/NBP35 protein involved in iron-sulfur biogenesis” Sci. Rep., 2019, 9, Article number: 712
https://www.nature.com/articles/s41598-018-37021-8
10/7 （月）市原
Vacek, V., et al., “Fe-S cluster assembly in oxymonads and related protists” Mol. Viol. Evol. 2018, 35(11), 2712-2718. DOI: 10.1093/molbev/msy168.
10/7 （月）村田
Zupok, A., et al., “Iron-Dependent Regulation of Molybdenum Cofactor Biosynthesis Genes in Escherichia coli” J. Bacteriol. 2019, 201(17), e00382-19. DOI: 10.1128/JB.00382-19.
10/14 （月） 中島
Zang, S., et al., “Characterization of the sulfur-formation (suf) genes in Synechocystis sp. PCC 6803 under photoautotrophic and heterotrophic growth conditions” Planta. 2017, 246(5), 927-938. DOI: 10.1007/s00425-017-2738-0
10/14 （月） 國近
Rutledge, H., et al., “Redox-Dependent Metastability of the Nitrogenase P-Cluster” J. Am. Chem. Soc. 2019, 141, 10091-10098. DOI:10.1021/jacs.9b04555
10/20 （月） 入江
Burkhart, BW., et al., “Distinct Physiological Roles of the Three Ferredoxins Encoded in the Hyperthermophilic Archaeon Thermococcus kodakarensis” mBio. 2019, 10, e02807-18. DOI:10.1128/mBio.02807-18
10/20 （月） 室賀
Blahut, M., et al., “Direct observation of intermediates in the SufS cysteine desulfurase reaction reveals functional roles of conserved active-site residues” J. Biol. Chem. 2019, 294, 12444-12458. DOI: 10.1074/jbc.RA119.009471
10/28 （月） 小川
Collins, R. et al., “Biochemical discrimination between selenium and sulfur 1:A single residue provides selenium specificity to human selenocysteine lyase” PLoS One. 2012, 7, e30581. DOI: 10.1371/journal.pone.0030581
10/28 （月） 櫻井
Zheng, C. et al., “The thioredoxin systen reduces protein persulfide intermediates formed during the synthesis of thio-cofactors in Bacillus subtilis” Biochemistry 2019, 58, 1892-1904. DOI: 10.1021/biochem.9b00045
11/11 （月） 中村
Safarian, S. et al., “Active site rearrangement and structural divergence in prokaryotic respiratory oxidases” Science. 2019, 366, 100-104. DOI: 10.1126/science.aay0967
11/11 （月）相羽
Mashruwala A.A. et al., “The DUF59 containing protein SufT is involved in the maturation of iron-sulfur (FeS) proteins during conditions of high FeS cofactor demand in Staphylococcus aureus” PLoS Genetics 2016, e1006233. DOI:10.1371/journal.pgen.1006233
11/18 （月） 中島
Hu, X. et al., “The iron–sulfur cluster biosynthesis protein SUFB is required for chlorophyll synthesis, but not phytochrome signaling” Plant J. 2017, 89, 1184-1194. DOI: 10.1111/tpj.13455
11/25 （月） 山之内
Grossman, J.D. et al., “Coupling nucleotide binding and hydrolysis to iron-sulfur cluster acquisition and transfer revealed through genetic dissection of the Nbp35 ATPase site” Biochemistry. 2019, 58, 2017-2027. DOI:10.1021/acs.biochem.8b00737
11/25 （月）國近
Volbeda, A. et al., “Crystal structure of the transcription regulator RsrR reeals a [2Fe-2S] cluster coordinated by Cys, Glu, and His residues” J. Am. Chem. Soc. 2019, DOI: 10.1021/jacs.8b10823
12/2 （月） 村田
Osorio, H. et al., “Identification and unusual properties of the master regulator FNR in the extreme acidophile Acidithiobacillus ferrooxidans” Front. Microbiol. 2019, 10, 1642. DOI:10.3389/fmicb.2019.01642
12/2 （月） 中村
Ciurli, S. et al., “The structure of the elusive urease-urea complex unveils the mechanism of a paradigmatic nickel-dependent enzyme” Angew. Chem. Int. Ed. 58, 7415-7419, 2019, DOI:10.1002/anie.201903565
2018年度
4/16 (月） 櫻井
Do, E., et al, “The mitochondrial ABC transporter Atm1 plays a role in iron metabolism and virulence in the human fungal pathogen Cryptococcus neoformans” Med. Mycol., myx073, (2017). DOI: 10.1093/mmy/myx073.
4/16 (月） 國近
Feliciano, P. R., et al., “Crystal structure of an Fe-S cluster-containing fumarate hydratase enzyme from Leishmania major reveals a unique protein fold” Proc. Natl. Acad. Sci. USA 113, 9804-9809 (2016). DOI: https://doi.org/10.1073/pnas.1605031113
4/23 (月） 村田
Sengupta, S., et al., “Phylogenetic analysis of the CDGSH iron-sulfur binding domain reveals its ancient origin” Sci. Rep. 8, article number 4848, (2018) . DOI: 10.1038/s41598-018-23305-6.
4/23 (月） 中村
Chen, P. Y., et al., “Binding site for coenzyme A revealed in the structure if otryvate:ferredoxin oxidoreductase from Moorella thermoacetica” Proc. Natl. Acad. Sci. USA in press. DOI: 10.1073/pnas.1722329115.
5/7 （月）小谷
Martinez, M.T.P, et al., “Sensing iron availability via the fragile [4Fe-4S] cluster of the bacterial transcriptional repressor RirA” Chem. Sci. 8, 8451-8463, (2017).
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5/7 （月）國近
Chen, M., et al, “Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by an iron-sulfur protein TtuA” Proc. Natl. Acad. Sci. USA 114, 4954-4959, (2017). DOI: 10.1073/pnas.1615585114
5/14 (月）櫻井
Upadhyay, A. S., et al., “Cellular requirements for iron-sulfur cluster insertion in to the antiviral radical SAM protein viperin” J. Biol. Chem., 292, (2017).
5/21 (月） 高田
Juernas, D. et al., “AtaT blocks translation initiation by N-acetylation of the initiator tRNAMet”, Nat. Chem. Biol., (2017). DOI: 10.1038/NCHEMBIO.2346.
5/21（月） 村田
Akaike, T., et al, “Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics” Nat. Commun., article number: 1177, (2017), DOI: 10.1038/s41467-017-01311-y.
6/4 (月）水島
B. Py, et al., “The ErpA/NfuA complex builds an oxidation-resistant Fe-S cluster delivery pathway” J. Biol. Chem. 293, 7689-7702, (2018). doi: 10.1074/jbc.RA118.002160
6/4 (月）安藤
J. Jeoung, et al., “ATP-dependent substrate reduction at an [Fe8S9] double-cubane cluster” Proc. Natl. Acad. Sci. USA, 115, 2994-2999, (2018). DOI: 10.1073/pnas.1720489115
6/11 （月） 河野
G. Jankevicius, et al., “The Toxin-Antitoxin System DarTG Catalyzes Reversible ADP-Ribosylation of DNA” Mol. Cell 64, 1109-1116, (2016).
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6/11 （月）関
S. Adinolfi, et al., “The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX” Front. Mol. Biosci.. 4, article 97, (2018).
6/25 (月） 入江
Liu, H., et al., “L-Cysteine production in Escherichia coli based on rational etabolic engineering and modular strategy” Biotechnol. J., 13, 1700695, (2018). DOI: 10.1002/biot.201700695.
6/25 （月） 佐藤
Benoit, S.L., et al., “Iron-sulfur protein maturation in Helicobacter pylori,: identifying a Nfu-type cluster carrier protein and its iron-sulfur protein targets” Mol. Microbiol. 108, 379-396, (2018). DOI: 10.1111/mmi.13942
7/2 (月） 大井
A. M. van den Berg, et al., “The hybrid-cluster protein (‘prismane protein’) from Escherichia coli, characterization of the hybrid cluster protein, redox properties of the [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]” Eur. J. Biochem. 267, 666-676, (2000). DOI: https://doi.org/10.1046/j.1432-1327.2000.01032.x
7/2 (月）鈴木
L. R. Walling, et al., “Homologous VapC Toxins Inhibit Translation and Cell Growth by Sequence-Specific Cleavage of tRNAfMet”, 200, e00582-17, (2018). doi: 10.1128/JB.00582-17 .
7/9（月） 志慶真
M. Howarth, et al., “A monovalent streptavidin with a single femtmolar biotin binding site”, Nat. Methods (2006) 3, 267-273. DOI: https://doi.org/10.1038/nmeth861
7/9（月） 島田
P. Roy, et al., “Comparison of the response of bacterial IscU and SufU to Zn2+ and select transition-metal ions” 13, 591-599, (2018). DOI: 10.1021/acschembio.7b00442
10/8（月） 大井
Gong, W., et al., “Structure of the a2e2 Ni-dependent CO dehydrogenase component of the Methanosarcina barkeri acetyl-CoA decarbonylase/synthase complex” Proc. Natl. Acad. Sci. USA 105, 9558-9563, (2008). DOI: 10.1073/pnas.0800415105
10/8（月） 安藤
Latorre, M., et al., “The role of Fur in the transcriptional and iron homeostatic response of Enterococcus faecalis”, Front. Microbiol., 9, 1580, (2018). DOI: 10.3389/fmicb.2018.01580.
10/15 （月） 小谷
Johnson, N. B., et al., “A synergistic role of IRP1 and FBXL5 proteins in coordinating iron metabolism during cell proliferation” J. Biol. Chem., 292, 15976-15989, (2017). DOI: 10.1074/jbc.M117.785741
10/15 （月）島田
Fox, N. G., et al., “Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activiy” Biochimie, 152, 211-218, (2018). DOI: 10.1016/j.biochi.2018.07.012
10/23 （月） 村田
Crooks, D. R., et al., “Acute loss of iron-sulfur clusters results in metabolic reprogramming and generation of lipid droplets in mammalian cells” J. Biol. Chem. 293, 8297-8311. DOI: http://www.jbc.org/content/293/21/8297.abstract
10/23 （月） 佐藤
Mosbahi, K., et al., “Bacterial iron acquisition mediated by outer membrane translocation and cleavage of a host protein” Proc. Natl. Acad. Sci. USA 115, 6840-6845. DOI: http://www.pnas.org/content/early/2018/06/05/1800672115
10/30（月） 関
Vo, A., et al., “Identifying the Protein Interactions of the Cytosolic Iron-Sulfur Cluster Targeting Complex Essential for Its Assembly and Recognition of Apo-Targets” Biochemistry, 57, 2349-2358., 2018.
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10/30（月） 國近
Dong, M., et al., “Organometallic and radical intermediates reveal mecanism of diphthamide biosynthesis” Science, 359, 1247-1250., 2018.
11/5 (月) 水島
Romsang, A., et al., “Pseudomonas aeruginosa nfuA: Gene regulation and its physiological roles in sustaining growth under stress and anaerobic conditions and maintaining bacterial viruence” PLoS One, 13, e0202151, (2018).
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11/5 (月) 入江
da Silva, S. M., et al., Batista-Nascimento, L., Gaspar-Cordeiro, A., Vernis, L., Pimentel, C., Rodrigues-Pousada, C., “Transcriptional regulation of Fe-S biogenesis genes: A possible shield against arsenate toxicity activated by Yap1” BBA-General Subjects 1862, 2152-2161, (2018). DOI: 10.1016/j.bbagen.2018.07.013.
11/12（月） 大井
Wang, J., et al., “The roles of the hybrid cluster protein, Hcp and its reductase, Hcr, in high affinity nitric oxide reduction that protects anaerobic cultures of Escherichia coli against nitrosative stress.” Mol. Microbiol. 100, 877-892 (2018).
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11/12（月） 志慶真
Jaroschinsky, M., et al., “Differential effects of isc operon mutations on the biosynthesis and activity of key anaerobic metalloenzymes in Escherichia coli” Microbiology, 163, 878-890, (2017). DOI: 10.1099/mic.0.000481
11/19 (月）中村
Grell, T. A. J., et al., “Biochemical and Structural Characterization of a Schiff Base in the Radical-Mediated Biosynthesis of 4-Demethylwyosine by TYW1” J. Am. Chem. Soc., 140, 6842-6852, (2018). DOI: 10.1021/jacs.8b01493
12/3 （月） 島田
Park, M., et al., “Understanding the Mechanism of Action of the Anti-Dandruff Agent Zinc Pyrithione against Malassezia restricta” Sci. Rep. 8, articile no:12086, (2018). DOI: 10.1038/s41598-018-30588-2
12/3 （月）安藤
Watanabe, T., et al., “N-terminal specific fluorescence labeling of proteins through incorporation of fluorescent hydroxy acid and subsequent ester cleavage” ChemBioChem, 9, 1235-1242, (2008). DOI: 10.1002/cbic.200700578
12/10 （月）小谷
Misslinger, M., et al., “ Iron-sensing is governed by mitochondrial, not by cytosolic iron-sulfur cluster biogenesis in Aspergillus fumigatus” Metallomics, 10, 1687, (2018). DOI: 10.1039/c8mt00263k
12/10 （月）入江
Tan, G., et al., “Anaerobic Copper Toxicity and Iron-Sulfur Cluster Biogenesis in Escherichia coli” 83, e00867, (2017). DOI: 10.1128/AEM.00867-17
12/10 （月）水島
Roberts, C. A., et al., “The Suf Iron-Sulfur Cluster Biosynthetic System Is Essential in Staphylococcus aureus, and Decreased Suf Function Results in Global Metabolic Defects and Reduced Survival in Human Neutrophils” 85, e00100-17, (2017). DOI: 10.1128/IAI.00100-17
2017年度
4/17 (月） 中村
Takao, H., et al., “A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity” Nat. Commun. 8, article number:14397, (2017). DOI: 10.1038/ncomms14397
4/24 (月） 関
Fujikawa, M., et al., “Rational tuning of superoxide sensitivity in SoxR, the [2Fe-2S] transcription factor: Implications of species-specific lysine residues” Biochemistry 56, 403–410, (2016). DOI: 10.1021/acs.biochem.6b01096
4/24 (月） 横山
Tanner, A. W., et al., “The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S]2+ clusters and may respond to redox changes” Mol. Microbiol. (2017). DOI: 10.1111/mmi.13667.
5/8 (月） 志慶真
Choi-Rhee, E., et al., “Promiscuous protein biotinylation by Escherichia coli biotin protein ligase” Protein Sci. (2004). DOI: 10.1110/ps.04911804
5/8 (月） 佐藤
Iametti, S., et al., “Functional implications of the interaction between HscB and IscU in the biosynthesis of FeS clusters” J. Biol. Inorg. Chem. (2015). DOI: 10.1007/s00775-015-1285-z
5/15 (月）林
Hu, X., et al., “The SUFBC2D complex is required for the biogenesis of all major classes of plastid Fe-S proteins” Plant J. (2017). DOI: 10.1111/tpj.13483
5/22 （月）村田
López-Torrejón, G., et al., “Expression of a functional oxygen-labile nitrogenase component in the mitochondrial matrix of aerobically grown yeast” Nat. Commun. (2016). DOI: 10.1038/ncomms11426
5/22 （月）中村
Dong, M., et al., “Substrate-dependent cleavage site selection by unconventional radical S-adenosylmethionine enzymes in diphthamide biosynthesis” J. Am. Chem. Soc. (2017). DOI: 10.1021/jacs.7b0172
5/29 （月）寺畑
Uchida, T., et al., “The iron chaperone protein CyaY from Vibrio cholerae is a heme-binding protein” Biochemistry (2017). DOI:10.1021/acs.biochem.6b01304
6/5 (月） 志慶真
Cao, D., et al., “Escherichia coli nfuA is essential for maintenance of Shiga toxin phage Min27 lysogeny under iron-depleted condition” FEMS Microbiol. Lett. (2015). DOI: 10.1093/femsle/fnv149
6/12（月） 櫻井
Black, K. A., et al., “Abbreviated pathway for biosynthesis of 2-thiouridine in Bacillus subtilis” J. Bacteriol. (2015). DOI: 10.1128/JB.02625-14
6/12 (月） 國近
Wagner, T., et al., “The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters” Science (2016). DOI: 10.1126/science.aaf9284
6/19 (月） 李
Zhang, Y., et al., “EPR studeies of wild type and mutant Dre2 identify essential [2Fe-2S] and [4Fe-4S] clusters and their cysteine residues” J. Biochem. (2017). DOI: https://doi.org/10.1093/jb/mvw054
6/19 (月）関
Wang, Q., et al., “Iron response regulator protein IrrB in Magnetospirillum gryphiswaldense MSR-1 helps control the iron/oxygen balance, oxidative stress tolerance, and magnetosome formation” Appl. Environ. Microbiol. (2015). DOI: 10.1128/AEM.02585-15
6/26（月）佐藤
Dlouhy, A. C., et al., “The Escherichia coli BolA protein IbaG forms a histidine-ligated [2Fe-2S]-bridged complex with Grx4” Biochemistry (2016). DOI: 10.1021/acs.biochem.6b00812
7/3（月）野上
Kim, D., et al., “An improved smaller biotin ligase for BioID proximity labelling” Mol. Biol. Cell (2016) DOI: 10.1091/mbc.E15-12-0844
7/10 (月）陳
Feliciano, F. R., et al., “Crystal structure of an Fe-S cluster-containing fumarate hydratase enzyme from Leishmania major reveals a unique protein fold” Proc. Natl. Acad. Sci. USA (2016) DOI: 10.1073/pnas.1605031113
7/10 （月）野上
Cory, S. A., et al., “Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions” Proc. Natl. Acad. Sci. USA (2017) DOI: 10.1073/pnas.1702849114
7/20 （木）小松
Franco, T., et al., “Mechanism-based inhibition of the Mycobacterium tuberculosis branched-chain aminotransferase by D- and L-cycloserine” ACS Chem. Biol. (2017) DOI: 10.1021/acschembio.7b00142
7/20 （木）陳
Arragain, S., et al., “Nonredox thiolation in tRNA occuring via sulfur activation by a [4Fe-4S] cluster” Proc. Natl. Acad. Sci. USA (2017) DOI:10.1073/pnas.1700902114
7/20 （木）寺畑
Volbeda, A., et al., “Crystal structures of the NO sensor NsrR reveal how its iron-sulfur cluster modulates DNA binding” Nat. Commun. (2017) DOI:10.1038/ncomms15052
10/2 （月） 林
Beilschmidt, L. K., et al., “ISCA1 is essential for mitochondrial Fe4S4 biogenesis in vivo” Nat. Commun. (2017) DOI:10.1038/ncomms15124.
10/2 （月） 國近
Shomura, Y., et al., “Structural basis of the redox switches in the NAD+-reducing soluble [NiFe]-hydrogenase” Science (2017) DOI: 10.1126/science.aan4497 .
10/9 （月）櫻井
Shigi, N., et al., “Identification of a rhodanese-like protein involved in thiouridine biosynthesis in Thermus thermophilus tRNA” FEBS Lett. (2016) DOI: 10.1002/1873-3468.12499
10/9 （月）李
Buehning, M., et al., “Functional complementation studies reveal different interaction partners of Escherichia coli IscS and human NFS1” Biochemistry (2017) DOI: 10.1021/acs.biochem.7b00627
10/9 （月）中村
Fellner, M., et al., “Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE” Proc. Ntal. Acad. Sci. USA (2017) DOI: 10.1073/pnas.1704967114
10/16 （月）野上
Liu, J., et al., “Coupling between distant biofilms and emergence of nutrient time-sharing” Science (2017) DOI: 10.1126/science.aah4204
10/16 （月） 志慶真
Cheah J. S. and Yamada, S. “A simple elusion strategy for biotinylated proteins bound to streptavidin conjugated beads using excess biotin and heat” Biochem. Biophys. Res. Commun. (2017), DOI:10.1016/j.bbrc.2017.09.168
10/23 （月） 寺畑
Stempler, O., et al., “Interspecies nutrient extraction and toxin delivery between bacteria” Nat. Commun. (2017) DOI: 10.1038/s41467-017-00344-7
10/23 （月） 村田
Wagner, T., et al., “Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction” Science (2017) DOI:10.1126/science.aan0425
10/30 （月） 陳
Erez, Z., et al., “Communication between viruses guides lysis-lysogeny decisions” Nature (2017) DOI: 10.1038/nature21049
10/30 （月） 佐藤
Vaccaro, B. J., et al., “Biological iron-sulfur storage in a thioferrate-protein nanoparticle” Nat. Commun. (2017) DOI: 10.1038/ncomms16110
10/30 （月） 小松
Deka, G., et al., “Structural studies on the decameric S. typhimurium arginine decarboxylase (ADC): Pyridoxal 5’-phosphate binding induces conformational changes” Biochem. Biophys. Res. Commun. (2017) DOI: 10.1016/j.bbrc.2017.07.032
11/6 （月） 関
Rocha, A.G., et al., “Cysteine desulfurase is regulated by phosphorylation of Nfs1 in yeast mitochondria” Mitochondrion, in press. DOI: 10.1016/j.mito.2017.09.003
11/6 （月） 志慶真
Bandyopadhyay, S., et al., “A proposed role for the Azotobacter vinelandii NfuA protein as an intermediate iron-sulfur cluster carrier” J. Biol. Chem. (2008) DOI: 10.1074/jbc.M709161200
11/20 (月） 櫻井
Freibert, S.-A., et al., “Evolutionary conservation and in vitro reconstitution of microsporidian iron-sulfur cluster biosynthesis” Nat. Commun. (2017) DOI:10.1038/ncomms13932
11/20 (月） 野上
McCarthy, E. L. and Booker, S. J. “Destruction and refomation of an iron-sulfur cluster during catalysis by lipoyl synthase” Science (2017) DOI:10.1126/science.aan4574
11/20 （月） 寺畑
Chung, B. C., et al., “Structural insight into inhibition of lipid I production in bacterial cell wall synthesis” Nature (2016) DOI:10.1038/nature17636
12/4 (月） 李
Jiang, T., et al., “A bacterial multidomain NAD-independent D-lactate dehydrogenase utilizes flavin adenine dinucleotide and Fe-S clusters as cofactors and quinone as an electron acceptor for D-lactate oxidization” J. Bacteriol. (2017) DOI:10.1128/JB.00342-17.
12/4 (月） 村田
O’Brien, E. et al., “The [4Fe-4S] cluster of human DNA primase functions as a redox switch using DNA charge transport” Science (2017) DOI:10.1126/science.aag1789
12/4 (月) 佐藤
Lin, T., et al., “IscR regulation of type 3 fimbriae expression in Klebsiella pneumonie CG43” Front. Microbiol. (2017) DOI: 10.3398/fmicb.2017.01984
12/11（月）関
Dwidar, M., et al., “Controlling Bdellovibrio bacteriovorus Gene Expression and Predation Using Synthetic Riboswitches” ACS Synth. Biol. (2017) DOI:10.1021/acssynbio.7b00171
12/11 （月） 國近
Shi, R., et al., “Structural Basis for Fe-S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein-Protein Interaction” PLoS Biol. (2010) DOI:10.1371/journal.pdio.1000354
12/11（月）林
Holzer, S., et al., “Primer synthesis by a eukaryotic-like archaeal primase is independent of its Fe-S cluster” Nat. Commun. (2017) DOI: 10.1038/s41467-017-01707-w
12/18（月）小松
Tremiño, L., et al., “Studies on cyanobacterial protein PipY shed light on structure, potential functions, and vitamin B6-dependent epilepsy” FEBS Lett., (2017). DOI: 10.1002/1873-3468.12841
12/18（月）中村
Boniecki, M. T., “Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex” Nat. Commun. (2017). DOI: 10.1038/s41467-017-01497-1
12/18（月）陳
Ling, L. L., et al., “A new antibiotic kills pathogens without detectable resistance” Nature (2015) DOI: 10.1038/nature14098
