[FeFe]-Hydrogenase Cyanide Ligands Derived From S-Adenosylmethionine-Dependent Cleavage of Tyrosine

被引：123

作者：

Driesener, Rebecca C. ^{[1
]}

Challand, Martin R. ^{[1
]}

McGlynn, Shawn E. ^{[2
,3
]}

Shepard, Eric M. ^{[2
,3
]}

Boyd, Eric S. ^{[2
,3
]}

Broderick, Joan B. ^{[2
,3
]}

Peters, John W. ^{[2
,3
]}

Roach, Peter L. ^{[1
]}

机构：

[1] Univ Southampton, Sch Chem, Southampton SO17 1BJ, Hants, England

[2] Montana State Univ, Dept Chem, Bozeman, MT 59717 USA

[3] Montana State Univ, Biochem & Astrobiol Biogeocatalysis Res Ctr, Bozeman, MT 59717 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2010年 / 49卷 / 09期

基金：

英国生物技术与生命科学研究理事会;

关键词：

bioinorganic chemistry; biosynthesis; cyanides; hydrogenases; metalloenzymes; ESCHERICHIA-COLI; H-CLUSTER; IN-VITRO; BIOSYNTHESIS; HYDROGENASE; METABOLISM; ACTIVATION; PROTEINS; SYNTHASE; MARITIMA;

D O I：

10.1002/anie.200907047

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

"Chemical Equation Presented" What's your poison? Hydrogenases catalyze the reversible formation of dihydrogen from two electrons and two protons. The maturation of the [FeFe]-hydrogenase active-site cofactor (H cluster) requires three gene products, HydE, HydF, and HydG. Cyanide has been characterized as one of the products of tyrosine cleavage by the S-adenosylmethionine-dependent enzyme HydC, clarifying its role in H-cluster biosynthesis. DOA = deoxyadenosine. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：1687 / 1690

页数：4

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