Synergic Binding of Carbon Monoxide and Cyanide to the FeMo Cofactor of Nitrogenase: Relic Chemistry of an Ancient Enzyme?
| Autor: | Shirley A. Fairhurst, Kylie A. Vincent, Stephen P. Best, Christopher J. Pickett, Barry E. Smith, C.A. Gormal, Saad Khalil Ibrahim |
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| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Molybdoferredoxin Hydrogenase FeMoco Stereochemistry Cyanide Photochemistry Catalysis Cofactor chemistry.chemical_compound Nitrogenase Spectroscopy Fourier Transform Infrared chemistry.chemical_classification Carbon Monoxide Cyanides biology Organic Chemistry Electron Spin Resonance Spectroscopy Active site General Chemistry Klebsiella pneumoniae Enzyme chemistry biology.protein Carbon monoxide |
| Zdroj: | Chemistry - A European Journal. 10:4770-4776 |
| ISSN: | 1521-3765 0947-6539 |
| Popis: | The first electrochemical and infra-red data on the binding of cyanide to the isolated iron-molybdenum cofactor of nitrogenase, FeMoco, is described. It is shown that cyanide stabilises a hitherto unrecognised, low-spin, EPR-active (S= 1/2), superoxidised form of FeMoco, and we provide the first evidence that carbon monoxide and cyanide bind synergically to the oxidised and semireduced states of the isolated cofactor, states which are unreactive to carbon monoxide alone. |
| Databáze: | OpenAIRE |
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