Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase.
about
Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesisThe methylthiolation reaction mediated by the Radical-SAM enzymesSPASM and twitch domains in S-adenosylmethionine (SAM) radical enzymesStructures of lipoyl synthase reveal a compact active site for controlling sequential sulfur insertion reactionsThe ISC [corrected] proteins Isa1 and Isa2 are required for the function but not for the de novo synthesis of the Fe/S clusters of biotin synthase in Saccharomyces cerevisiae.Paramagnetic intermediates generated by radical S-adenosylmethionine (SAM) enzymesRecent advances in radical SAM enzymology: new structures and mechanisms.Biotin and Lipoic Acid: Synthesis, Attachment, and Regulation.The biosynthesis of thiol- and thioether-containing cofactors and secondary metabolites catalyzed by radical S-adenosylmethionine enzymes.Structural and functional comparison of HemN to other radical SAM enzymes.RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli.Self-sacrifice in radical S-adenosylmethionine proteins.Anaerobic functionalization of unactivated C-H bonds.Radical S-adenosylmethionine enzymes.Structural insights into radical generation by the radical SAM superfamily.Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors.Role of the [2Fe-2S]2+ cluster in biotin synthase: mutagenesis of the atypical metal ligand arginine 260Density functional theory calculations on the active site of biotin synthase: mechanism of S transfer from the Fe(2)S(2) cluster and the role of 1st and 2nd sphere residues.Into the Wild: Parallel Transcriptomics of the Tsetse-Wigglesworthia Mutualism within Kenyan Populations.Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthaseReduction of the [2Fe-2S] cluster accompanies formation of the intermediate 9-mercaptodethiobiotin in Escherichia coli biotin synthase.A complex between biotin synthase and the iron-sulfur cluster assembly chaperone HscA that enhances in vivo cluster assembly.9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase.9-Mercaptodethiobiotin is generated as a ligand to the [2Fe-2S]+ cluster during the reaction catalyzed by biotin synthase from Escherichia coli.Loss of iron-sulfur clusters from biotin synthase as a result of catalysis promotes unfolding and degradation.In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters.MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA.The radical-SAM enzyme Viperin catalyzes reductive addition of a 5'-deoxyadenosyl radical to UDP-glucose in vitro.A model study on the possible effects of an external electrical field on enzymes having dinuclear iron cluster [2Fe-2S]
P2860
Q24295080-4913469B-4BE8-40E1-969E-6CFF02578269Q26822523-392EE030-F6E1-43A3-B2EB-EBA281754585Q26865439-14541BF1-7208-4F63-BDA2-EF5A31AEDB52Q27694727-4688ED0E-BABE-445E-AD7E-034582A3E978Q27938255-B2E35C2F-E289-40A2-889F-83F52A358F90Q34070183-91C8A9D8-9B25-45B2-9C86-B4317B0A5E7AQ34211575-23D79BE8-60BD-4F7D-9114-F71A86A1BBD9Q34519665-B33E7EA2-445C-4938-BEE0-BA0BDEC76A69Q35080219-8711D721-6B6B-4A8A-B0E1-AE571B92018BQ36283670-71062B48-35A4-46A8-A24D-AD6A2ED8F8C8Q36882918-7D4454FB-E84F-42B0-A108-8D42E45C2E4BQ36970928-276738D1-0CB5-4833-AECF-BC903F8293AAQ37388852-819C87A0-B020-41E2-963B-46F5AF037304Q37727698-EFCEAFA2-1DFD-461C-B338-3666EFC2B3BAQ37849296-38E9B1CC-AA02-4531-A7EA-D14DC01A7A45Q37878385-6F7F8AF1-9420-49E3-9492-97D28E4EC5FEQ39660280-2E9409F4-745C-497C-A03C-AFB385D37DC7Q40540646-A37278BF-38CB-4344-80A7-E46954108A19Q41692208-8E479ACB-4304-4121-99BE-DB619A036ACBQ41839348-74241E8D-2F48-4052-BFEA-0B9AA2FCFB12Q41884566-54994B59-3CE0-454F-96E1-F30775BC1AA0Q42069948-AAEC0D12-9DBC-47AB-88F7-67BE48820E82Q42132738-44B983BF-607E-4E39-8F00-CCF15BC103B3Q42274127-0ED915E3-8417-40C3-A42B-B82545AA2F69Q43013624-2379FB9C-EF5C-4C55-99A0-321D176C1810Q43151037-89CB8E86-7580-49E9-9D13-3738FC6F174FQ45038651-1A8933C2-9F79-411B-8BF0-4A62C03154A6Q46184968-80CA54B2-AA00-4DE1-AF24-860DD6720373Q58915172-CEC6F044-BCE5-4BB1-AC2D-2D0F635CEA1E
P2860
Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase.
@en
Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase.
@nl
type
label
Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase.
@en
Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase.
@nl
prefLabel
Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase.
@en
Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase.
@nl
P2093
P356
P1433
P1476
Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase.
@en
P2093
Boi Hanh Huynh
Guy N L Jameson
Heather L Hernández
Michael K Johnson
Michele Mader Cosper
P304
P356
10.1021/BI035666V
P407
P577
2004-02-01T00:00:00Z