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Publication Abstract from PubMed

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 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 E6 or E7 of the Thorneley-Lowe model and provides clues to the remainder of the catalytic cycle.

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 SLA, Einsle O Science. 2018 Mar 30;359(6383):1484-1489. doi: 10.1126/science.aar2765. PMID:29599235^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.