Electrochemical Characterization of Isolated Nitrogenase Cofactors from Azotobacter vinelandii
Journal Article
·
· ChemBioChem: a European journal of chemical biology
- Univ. of California, Irvine, CA (United States); OSTI
- Univ. of California, Irvine, CA (United States)
The nitrogenase cofactors are structurally and functionally unique in biological chemistry. Despite a substantial amount of spectroscopic characterization of protein-bound and isolated nitrogenase cofactors, electrochemical characterization of these cofactors and their related species is far from complete. Herein we present voltammetric studies of three isolated nitrogenase cofactor species: the iron–molybdenum cofactor (M-cluster), iron–vanadium cofactor (V-cluster), and a homologue to the iron–iron cofactor (L-cluster). We observe two reductive events in the redox profiles of all three cofactors. Of the three, the V-cluster is the most reducing. The reduction potentials of the isolated cofactors are significantly more negative than previously measured values within the molybdenum–iron and vanadium–iron proteins. Finally, the outcome of this study provides insight into the importance of the heterometal identity, the overall ligation of the cluster, and the impact of the protein scaffolds on the overall electronic structures of the cofactors.
- Research Organization:
- Univ. of California, Irvine, CA (United States)
- Sponsoring Organization:
- National Science Foundation (NSF); USDOE Office of Science (SC)
- Grant/Contract Number:
- SC0012150
- OSTI ID:
- 1802308
- Journal Information:
- ChemBioChem: a European journal of chemical biology, Journal Name: ChemBioChem: a European journal of chemical biology Journal Issue: 12 Vol. 21; ISSN 1439-4227
- Publisher:
- ChemPubSoc EuropeCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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