Development of a cell-free system reveals an oxygen-labile step in the maturation of [NiFe]-hydrogenase 2 of Escherichia coli

被引：16

作者：

Soboh, Basem ^{[1
]}

Krueger, Sara ^{[1
]}

Kuhns, Martin ^{[1
]}

Pinske, Constanze ^{[1
]}

Lehmann, Anne ^{[1
]}

Sawers, R. Gary ^{[1
]}

机构：

[1] Univ Halle Wittenberg, Inst Mikrobiol, D-06120 Halle, Saale, Germany

来源：

FEBS LETTERS | 2010年 / 584卷 / 18期

关键词：

NiFe]-hydrogenase; In vitro processing; Hydrogen oxidation; Hyp maturation proteins; HYDROGENASE ISOENZYMES; ACTIVE-SITE; CRYSTAL-STRUCTURES; PROTEINS HYPC; NICKEL; CN; ACTIVATION; EXPRESSION; COMPLEX; ENZYME;

D O I：

10.1016/j.febslet.2010.08.037

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

By combining extracts from strains lacking genes encoding either the maturation enzymes or the large subunits of hydrogenases 1, 2 and 3 we could reconstitute in vitro under strictly anaerobic conditions 10-15% of the hydrogenase activity present in wild type Escherichia coli extracts. Purified, unprocessed Strep-tagged variants of the hydrogenase 2 large subunit, HybC, isolated from either a Delta hybD (encoding the hydrogenase 2-specific protease) mutant or a strain deficient in HypF could also be matured to active, processed enzyme using this system. These studies reveal that minimally one step early on the hydrogenase maturation pathway is oxygen-labile. (c) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：4109 / 4114

页数：6

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