A Comparative Analysis of the CO‐Reducing Activities of MoFe Proteins Containing Mo‐ and V‐Nitrogenase Cofactors
- Department of Molecular Biology and Biochemistry University of California 2230/2236 McGaugh Hall Irvine CA 92697-3900 USA
- Department of Molecular Biology and Biochemistry University of California 2230/2236 McGaugh Hall Irvine CA 92697-3900 USA, Department of Chemistry University of California 2236 McGaugh Hall Irvine CA 92697-2025 USA
Abstract The Mo and V nitrogenases are structurally homologous yet catalytically distinct in their abilities to reduce CO to hydrocarbons. Here we report a comparative analysis of the CO‐reducing activities of the Mo‐ and V‐nitrogenase cofactors (i.e., the M and V clusters) upon insertion of the respective cofactor into the same, cofactor‐deficient MoFe protein scaffold. Our data reveal a combined contribution from the protein environment and cofactor properties to the reactivity of nitrogenase toward CO, thus laying a foundation for further mechanistic investigation of the enzymatic CO reduction, while suggesting the potential of targeting both the protein scaffold and the cofactor species for nitrogenase‐based applications in the future.
- Sponsoring Organization:
- USDOE
- Grant/Contract Number:
- SC0014470
- OSTI ID:
- 1421569
- Journal Information:
- ChemBioChem: a European journal of chemical biology, Journal Name: ChemBioChem: a European journal of chemical biology Journal Issue: 7 Vol. 19; ISSN 1439-4227
- Publisher:
- Wiley Blackwell (John Wiley & Sons)Copyright Statement
- Country of Publication:
- France
- Language:
- English
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