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

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2012年 / 51卷 / 46期

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

页码：11458 / 11462

页数：5

共 27 条

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