Identification and Characterization of the "Super-Reduced" State of the H-Cluster in [FeFe] Hydrogenase: A New Building Block for the Catalytic Cycle?

被引:164
作者
Adamska, Agnieszka [1 ]
Silakov, Alexey [1 ]
Lambertz, Camilla [2 ]
Ruediger, Olaf [1 ]
Happe, Thomas [2 ]
Reijerse, Edward [1 ]
Lubitz, Wolfgang [1 ]
机构
[1] Max Planck Inst Chem Energiekonvers, D-45470 Mulheim, Germany
[2] Ruhr Univ Bochum, Lehrstuhl Biochem Pflanzen, AG Photobiotechnol, D-44801 Bochum, Germany
关键词
biohydrogen; electron spin resonance; FTIR spectroscopy; hydrogenase; protein film electrochemistry; ACTIVE-SITE; DESULFOVIBRIO-DESULFURICANS; CHLAMYDOMONAS-REINHARDTII; ONLY HYDROGENASE; IRON; SPECTROSCOPY; CO; REDUCTION; LIGAND; NIFE;
D O I
10.1002/anie.201204800
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Super-reduced and super-active: A new redox state in the active site of algal [FeFe] hydrogenases has been identified and characterized by EPR and FTIR spectroscopy. Electrochemical and in-vitro essays show that this species is highly active in hydrogen production and suggest that it is a key intermediate in the catalytic cycle of all [FeFe] hydrogenases. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码:11458 / 11462
页数:5
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