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DOI	10.1126/science.aar2765
	A bound reaction intermediate sheds light on the mechanism of nitrogenase
	Sippel D.; Rohde M.; Netzer J.; Trncik C.; Gies J.; Grunau K.; Djurdjevic I.; Decamps L.; Andrade S.L.A.; Einsle O.
发表日期	2018
ISSN	0036-8075
起始页码	1484
结束页码	1489
卷号	359 期号:6383
英文摘要	Reduction of N2 by nitrogenases occurs at an organometallic iron cofactor that commonly also contains either molybdenum or vanadium. The well-characterized resting state of the cofactor does not bind substrate, so its mode of action remains enigmatic. Carbon monoxide was recently found to replace a bridging sulfide, but the mechanistic relevance was unclear. Here we report the structural analysis of vanadium nitrogenase with a bound intermediate, interpreted as a μ2-bridging, protonated nitrogen that implies the site and mode of substrate binding to the cofactor. Binding results in a flip of amino acid glutamine 176, which hydrogen-bonds the ligand and creates a holding position for the displaced sulfide. The intermediate likely represents state E6 or E7 of the Thorneley-Lowe model and provides clues to the remainder of the catalytic cycle. © The Authors, some rights reserved;.
英文关键词	glutamine; molybdenum; nitrogen; nitrogenase; sulfide; vanadium; carbon monoxide; ligand; nitrogenase; amino acid; carbon monoxide; catalysis; chemical binding; hydrogen; ligand; molybdenum; nitrogen; reduction; sulfide; vanadium; Article; binding site; catalysis; enzyme active site; enzyme mechanism; enzyme substrate complex; hydrogen bond; ligand binding; priority journal; proton transport; structure analysis; biocatalysis; chemistry; oxidation reduction reaction; Binding Sites; Biocatalysis; Carbon Monoxide; Catalytic Domain; Hydrogen Bonding; Ligands; Molybdenum; Nitrogen; Nitrogenase; Oxidation-Reduction
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/245507
作者单位	Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstraße 21, Freiburg, 79104, Germany; BIOSS Centre for Biological Signalling Studies, Schänzlestraße 1, Freiburg, 79104, Germany; Freiburg Institute for Advanced Studies, Freiburg, 79104, Germany
推荐引用方式 GB/T 7714	Sippel D.,Rohde M.,Netzer J.,et al. A bound reaction intermediate sheds light on the mechanism of nitrogenase[J],2018,359(6383).
APA	Sippel D..,Rohde M..,Netzer J..,Trncik C..,Gies J..,...&Einsle O..(2018).A bound reaction intermediate sheds light on the mechanism of nitrogenase.Science,359(6383).
MLA	Sippel D.,et al."A bound reaction intermediate sheds light on the mechanism of nitrogenase".Science 359.6383(2018).