期刊
CHEMBIOCHEM
卷 21, 期 12, 页码 1773-1778出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201900425
关键词
cofactors; electrochemistry; nitrogenases; redox properties; reduction potentials
资金
- NSF [CHE-1608926]
- UCI School of Physical Sciences
- US Department of Energy, Office of Science, Office of Basic Energy Sciences Award [DE-SC0012150]
- Sloan Foundation
- Bioinspired Energy Program
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. 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.
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