Current status of structure function relationships of vanadium nitrogenase

V-nitrogenase is both genetically and biochemically similar to the more intensively studied Mo-nitrogenase. The VFe protein contains P cluster redox centres and a catalytic FeVco centre, in which V is in polynuclear cluster with Fe, S and homocitrate with a chemical environment similar to Mo in MoFe...

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Bibliographic Details
Published in:Coordination chemistry reviews 2003-02, Vol.237 (1), p.23-30
Main Author: Eady, Robert R.
Format: Article
Language:English
Subjects:
FeMoco
FeVco
Mo-nitrogenase
Nitrogen fixation
Vanadium-nitrogenase
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Summary:V-nitrogenase is both genetically and biochemically similar to the more intensively studied Mo-nitrogenase. The VFe protein contains P cluster redox centres and a catalytic FeVco centre, in which V is in polynuclear cluster with Fe, S and homocitrate with a chemical environment similar to Mo in MoFe proteins. Current preparations of VFe proteins are a mixture of functional and inactive species, hindering mechanistic studies. A rationale for their separation based on the formation of putative transition-state analogues is outlined.
ISSN:0010-8545
1873-3840
DOI:10.1016/S0010-8545(02)00248-5