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DOI	10.1126/science.1256679
	Ligand binding to the FeMo-cofactor: Structures of co-bound and reactivated nitrogenase
	Spatzal T.; Perez K.A.; Einsle O.; Howard J.B.; Rees D.C.
发表日期	2014
ISSN	0036-8075
起始页码	1620
结束页码	1623
卷号	345 期号:6204
英文摘要	(D.C.R.). 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 μ2binding 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. © 2014 by the American Association for the Advancement of Science; all rights reserved.
英文关键词	carbon monoxide; ligand; molybdenum iron protein; sulfur; article; chemistry; drug antagonism; enzyme activation; enzyme active site; nitrogen fixation; protein binding; X ray crystallography; Carbon Monoxide; Catalytic Domain; Crystallography, X-Ray; Enzyme Activation; Ligands; Molybdoferredoxin; Nitrogen Fixation; Protein Binding; Sulfur
语种	英语
来源期刊	Science
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/245575
作者单位	Howard Hughes Medical Institute and Division of Chemistry and Chemical Engineering,Mail Code 114-96, California Institute of Technology, Pasadena, CA 91125, United States; Institute für Biochemie, Albert-Ludwlgs-Unlversltät Freiburg, Freiburg, 79104, Germany; BI0SS Centre for Biological Signalling Studies, Albert-Ludwlgs-Unlversltät Freiburg, Freiburg, 79104, Germany; Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, United States
推荐引用方式 GB/T 7714	Spatzal T.,Perez K.A.,Einsle O.,et al. Ligand binding to the FeMo-cofactor: Structures of co-bound and reactivated nitrogenase[J],2014,345(6204).
APA	Spatzal T.,Perez K.A.,Einsle O.,Howard J.B.,&Rees D.C..(2014).Ligand binding to the FeMo-cofactor: Structures of co-bound and reactivated nitrogenase.Science,345(6204).
MLA	Spatzal T.,et al."Ligand binding to the FeMo-cofactor: Structures of co-bound and reactivated nitrogenase".Science 345.6204(2014).