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
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
收藏
页码:8026 / 8029
页数:4
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