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Electron-transfer chemistry of the iron-molybdenum cofactor of nitrogenase: delocalized and localized reduced states of FeMoco which allow binding of carbon monoxide to iron and molybdenum.

Abstract:

The electron-transfer chemistry of the isolated iron-molybdenum cofactor of nitrogenase (FeMoco) has been studied by electrochemical and spectroelectrochemical methods. Two interconverting forms of the cofactor arise from a redox-linked ligand isomerism at the terminal iron atom; this is attributed to rotamerism of an anionic N-methyl formamide ligand bound at this site. FeMoco in its EPR-silent oxidised state is shown to undergo three successive one-electron transfer steps. We argue that the...

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Publication status:
Published

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Publisher copy:
10.1002/chem.200390033

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
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Journal:
Chemistry (Weinheim an der Bergstrasse, Germany)
Volume:
9
Issue:
1
Pages:
76-87
Publication date:
2003-01-01
DOI:
EISSN:
1521-3765
ISSN:
0947-6539
Source identifiers:
51656
Language:
English
Keywords:
Pubs id:
pubs:51656
UUID:
uuid:cea58978-f7d3-4710-94e1-25b6069e9c88
Local pid:
pubs:51656
Deposit date:
2012-12-19

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