The [FeFe]-hydrogenase maturation protein HydF contains a H-cluster like [4Fe4S]-2Fe site

被引：47
作者：
Czech, Ilka [1 ]
Stripp, Sven [1 ]
Sanganas, Oliver [2 ]
Leidel, Nils [2 ]
Happe, Thomas [1 ]
Haumann, Michael [2 ]
机构：
[1] Ruhr Univ Bochum, Lehrstuhl Biochem Pflanzen, D-44780 Bochum, Germany
[2] Free Univ Berlin, Inst Expt Phys, D-14195 Berlin, Germany
来源：
FEBS LETTERS | 2011年 / 585卷 / 01期
关键词：
FeFe]-hydrogenase; H-cluster; Maturation; HydF; X-ray absorption spectroscopy; RAY-ABSORPTION SPECTROSCOPY; IRON-SULFUR CLUSTER; FEFE HYDROGENASE; ACTIVE-SITE; CHLAMYDOMONAS-REINHARDTII; MANGANESE COMPLEX; CLOSTRIDIUM-ACETOBUTYLICUM; THERMOTOGA-MARITIMA; PHOTOSYSTEM-II; GREEN-ALGAE;
D O I：
10.1016/j.febslet.2010.11.052
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：
Formation of the catalytic six-iron complex (H-cluster) of [FeFe]-hydrogenase (HydA) requires its interaction with a specific maturation protein, HydF. Comparison by X-ray absorption spectroscopy at the Fe K-edge of HydF from Clostridium acetobutylicum and HydA1 from Chlamydomonas reinhardtii revealed that the overall structure of the iron site in both proteins is highly similar, comprising a [4Fe4S] cluster (Fe-Fe distances of similar to 2.7 angstrom) and a di-iron unit (Fe-Fe distance of similar to 2.5 angstrom). Thus, a precursor of the whole H-cluster is assembled on HydF. Formation of the core structures of both the 4Fe and 2Fe units may require only the housekeeping [FeS] cluster assembly machinery of the cell. Presumably, only the 2Fe cluster is transferred from HydF to HydA1, thereby forming the active site. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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页码：225 / 230
页数：6
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