Probing the Active Site of an O2-Tolerant NAD+-Reducing [NiFe]-Hydrogenase from Ralstonia eutropha H16 by In Situ EPR and FTIR Spectroscopy

被引：52

作者：

Horch, Marius ^{[2
]}

Lauterbach, Lars ^{[1
]}

Saggu, Miguel ^{[2
]}

Hildebrandt, Peter ^{[2
]}

Lendzian, Friedhelm ^{[2
]}

Bittl, Robert ^{[3
]}

Lenz, Oliver ^{[1
]}

Zebger, Ingo ^{[2
]}

机构：

[1] Humboldt Univ, Inst Biol Mikrobiol, Sekr PC14, D-10115 Berlin, Germany

[2] Tech Univ Berlin, Inst Chem, D-10623 Berlin, Germany

[3] Free Univ Berlin, Inst Phys, D-10115 Berlin, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2010年 / 49卷 / 43期

关键词：

biocatalysis; EPR spectroscopy; FTIR spectroscopy; hydrogenases; oxygen tolerance; NAD-REDUCING HYDROGENASE; VULGARIS MIYAZAKI-F; NIFE HYDROGENASE; OXYGEN; ACTIVATION; OXIDATION; STATE; INSIGHTS; HYSCORE; ENDOR;

D O I：

10.1002/anie.201002197

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A clear picture: In situ EPR and FTIR spectroscopic studies on the soluble, NAD+-reducing [NiFe]-hydrogenase of Ralstonia eutropha reveal that the catalytic site resides predominantly in the intermediate Nia-C state within whole cells. This state, can either be reversibly oxidized to a Nir-B-like state or further reduced to various Nia-SR species. The data suggest that the iron center in the active site contains a standard set (one CO and two CN-) of inorganic ligands. © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：8026 / 8029

页数：4

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