The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor

被引：76

作者：

Czech, Ilka ^{[1
]}

Silakov, Alexey ^{[2
]}

Lubitz, Wolfgang ^{[2
]}

Happe, Thomas ^{[1
]}

机构：

[1] Ruhr Univ Bochum, Lehrstuhl Biochem Pflanzen, AG Photobiotechnol, D-44801 Bochum, Germany

[2] Max Planck Inst Bioanorgan Chem, D-45470 Mulheim, Germany

来源：

FEBS LETTERS | 2010年 / 584卷 / 03期

关键词：

FeFe] Hydrogenase; H-Cluster; Maturation; Fourier-transform infrared spectroscopy; Electron paramagnetic resonance spectroscopy; Clostridium acetobutylicum; ALGA CHLAMYDOMONAS-REINHARDTII; FEFE HYDROGENASE; ACTIVE-SITE; H-CLUSTER; THERMOTOGA-MARITIMA; SULFUR PROTEINS; BIOSYNTHESIS; SPECTROSCOPY; ACTIVATION; ENZYMES;

D O I：

10.1016/j.febslet.2009.12.016

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：

Biosynthesis of the [FeFe] hydrogenases active site (H-cluster) requires three maturation factors whose respective roles are not understood yet. The clostridial maturation enzymes (CaHydE, CaHydF and CaHydG) were homologously overexpressed in their native host Clostridium acetobutylicum. CaHydF was able to activate Chlamydomonas reinhardtii [FeFe] hydrogenase apoprotein (CrHy-dA1(apo)) to almost 100% compared to the native specific hydrogen evolution activity. Based on electron paramagnetic resonance spectroscopy and Fourier-transform infrared spectroscopy data the existence of a [4Fe4S] cluster and a CO and CN- ligand coordinated di-iron cluster is suggested. This study contains the first experimental evidence that the bi-nuclear part of the H-cluster is assembled in HydF. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：638 / 642

页数：5

共 28 条

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