A Comparative Analysis of the CO‐Reducing Activities of MoFe Proteins Containing Mo‐ and V‐Nitrogenase Cofactors. (16th February 2018)

• Record Type: Journal Article
• Authors: Lee, Chi Chung; Tanifuji, Kazuki; Newcomb, Megan; Liedtke, Jasper; Hu, Yilin; Ribbe, Markus W.
• Is Part Of: Chembiochem. Volume 19:Number 7(2018)
• Page Start: 649
• Page End: 653
• Publication Date: 2018-02-16
• Subjects: carbon monoxide -- cofactors -- hydrocarbons -- molybdenum -- nitrogenase -- vanadium; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201800035
• Languages: English
• ISSNs: 1439-4227

Abstract

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. Abstract : 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.