期刊
SCIENCE
卷 359, 期 6383, 页码 1484-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aar2765
关键词
-
资金
- European Research Council [310656]
- Deutsche Forschungsgemeinschaft [RTG 1976, PP 1927]
- BIOSS Centre for Biological Signalling Studies at Albert-Ludwigs-Universitat Freiburg
Reduction of N-2 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 mu(2)-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 E-6 or E-7 of the Thorneley-Lowe model and provides clues to the remainder of the catalytic cycle.
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