Redox properties and electron paramagnetic resonance spectroscopy of the transition state complex of Azotobacter vinelandii nitrogenase

被引：25

作者：

Spee, JH ^{[1
]}

Arendsen, AF ^{[1
]}

Wassink, H ^{[1
]}

Marritt, SJ ^{[1
]}

Hagen, WR ^{[1
]}

Haaker, H ^{[1
]}

机构：

[1] Agr Univ Wageningen, Dept Biomol Sci, Biochem Lab, NL-6703 HA Wageningen, Netherlands

来源：

FEBS LETTERS | 1998年 / 432卷 / 1-2期

关键词：

nitrogenase (Azotobacter vinelandii); transition state complex; redox potential; electron paramagnetic resonance;

D O I：

10.1016/S0014-5793(98)00827-8

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：

Nitrogenase is a two-component metalloenzyme that catalyzes a MgATP hydrolysis driven reduction of substrates, Aluminum fluoride plus MgADP inhibits nitrogenase by stabilizing an intermediate of the on-enzyme MgATP hydrolysis reaction. We report here the redox properties and electron paramagnetic resonance (EPR) signals of the aluminum fluoride-MgADP stabilized nitrogenase complex of Azotobacter vinelandii. Complex formation lowers the midpoint potential of the [4Fe-4S] cluster in the Fe protein. Also, the two-electron reaction of the unique [8Fe-7S] cluster in the MoFe protein is split in two one-electron reactions both with loner midpoint potentials. Furthermore, a change in spin-state of the tno-electron oxidized [8Fe-7S] cluster is observed. The implications of these findings for the mechanism of MgATP hydrolysis driven electron transport within the nitrogenase protein complex are discussed. (C) 1998 Federation of European Biochemical Societies.

引用

页码：55 / 58

页数：4

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