期刊
SCIENCE
卷 345, 期 6204, 页码 1620-1623出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1256679
关键词
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资金
- NIH [GM45162]
- Deutsche Forschungsgemeinschaft [EI-520/7, RTG 1976]
- European Research Council N-ABLE project
- Gordon and Betty Moore Foundation
- Beckman Institute
- Sanofi-Aventis Bioengineering Research Program at Caltech
- U.S. Department of Energy, Office of Biological and Environmental Research
- NIH: National Institute of General Medical Sciences [P41GM103393]
- National Center for Research Resources [P41RR001209]
- Center for Environmental Microbial Interactions
The mechanism of nitrogenase remains enigmatic, with a major unresolved issue concerning how inhibitors and substrates bind to the active site. We report a crystal structure of carbon monoxide (CO)-inhibited nitrogenase molybdenum-iron (MoFe)-protein at 1.50 angstrom resolution, which reveals a CO molecule bridging Fe2 and Fe6 of the FeMo-cofactor. The mu(2) binding geometry is achieved by replacing a belt-sulfur atom (S2B) and highlights the generation of a reactive iron species uncovered by the displacement of sulfur. The CO inhibition is fully reversible as established by regain of enzyme activity and reappearance of S2B in the 1.43 angstrom resolution structure of the reactivated enzyme. The substantial and reversible reorganization of the FeMo-cofactor accompanying CO binding was unanticipated and provides insights into a catalytically competent state of nitrogenase.
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