Structural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron Protein
- Authors
- Rettberg, Lee A.; Stiebritz, Martin T.; Kang, Wonchull; Lee, Chi Chung; Ribbe, Markus W.; Hu, Yilin
- Issue Date
- Oct-2019
- Publisher
- WILEY-V C H VERLAG GMBH
- Keywords
- all-ferrous; C1 reduction; carbon dioxide; iron proteins; nitrogenase
- Citation
- CHEMISTRY-A EUROPEAN JOURNAL, v.25, no.57, pp.13078 - 13082
- Journal Title
- CHEMISTRY-A EUROPEAN JOURNAL
- Volume
- 25
- Number
- 57
- Start Page
- 13078
- End Page
- 13082
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/40943
- DOI
- 10.1002/chem.201903387
- ISSN
- 0947-6539
- Abstract
- The Fe protein of nitrogenase catalyzes the ambient reduction of CO2 when its cluster is present in the all-ferrous, [Fe4S4](0) oxidation state. Here, we report a combined structural and theoretical study that probes the unique reactivity of the all-ferrous Fe protein toward CO2. Structural comparisons of the Azotobacter vinelandii Fe protein in the [Fe4S4](0) and [Fe4S4](+) states point to a possible asymmetric functionality of a highly conserved Arg pair in CO2 binding and reduction. Density functional theory (DFT) calculations provide further support for the asymmetric coordination of O by the "proximal" Arg and binding of C to a unique Fe atom of the all-ferrous cluster, followed by donation of protons by the proximate guanidinium group of Arg that eventually results in the scission of a C-O bond. These results provide important mechanistic and structural insights into CO2 activation by a surface-exposed, scaffold-held [Fe4S4] cluster.
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Collections - College of Natural Sciences > Department of Chemistry > 1. Journal Articles
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