A Comparative Analysis of the CO‐Reducing Activities of MoFe Proteins Containing Mo‐ and V‐Nitrogenase Cofactors

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 c...

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Published in:Chembiochem : a European journal of chemical biology 2018-04, Vol.19 (7), p.649-653
Main Authors: Lee, Chi Chung, Tanifuji, Kazuki, Newcomb, Megan, Liedtke, Jasper, Hu, Yilin, Ribbe, Markus W.
Format: Article
Language:English
Subjects:
Azotobacter vinelandii - enzymology
Biocatalysis
carbon monoxide
Carbon Monoxide - chemistry
Coenzymes - metabolism
Cofactors
Comparative analysis
Enzyme Assays
Homology
Hydrocarbons
MoFe protein
molybdenum
Molybdenum - chemistry
Nitrogenase
Nitrogenase - chemistry
Oxidation-Reduction
Proteins
Scaffolds
vanadium
Vanadium - chemistry
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Summary: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. CO‐workers: A comparison between nitrogenase MoFe proteins containing Mo‐ and V‐nitrogenase cofactors reveals a combined impact of the protein environment and the cluster properties on the reactivity of nitrogenase toward CO.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.201800035