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A Major Structural Change of the Homocitrate Ligand of Probable Importance for the Nitrogenase Mechanism
Stockholm University, Faculty of Science, Department of Organic Chemistry.
Number of Authors: 1
2018 (English)In: Inorganic Chemistry, ISSN 0020-1669, E-ISSN 1520-510X, Vol. 57, no 3, p. 1090-1095Article in journal (Refereed) Published
Abstract [en]

Mo-containing nitrogenase is the main enzyme that is able to take N-2 from the air and form ammonia. The active-site cofactor of the enzyme, termed FeMoco, is unique in nature. It has seven Fe and one Mo atoms connected by S bridges, with a C atom in the center of the cofactor. Another unusual feature is that it has a large homocitrate ligand known to be of importance for catalysis. In the present computational study, the role of the homocitrate ligand is investigated. It is found that a large structural change, which makes Mo-III five coordinated, is energetically favorable in the more reduced states. This is of probable importance for the nitrogenase mechanism.

Place, publisher, year, edition, pages
2018. Vol. 57, no 3, p. 1090-1095
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:su:diva-154595DOI: 10.1021/acs.inorgchem.7b02493ISI: 000424730800023PubMedID: 29303565OAI: oai:DiVA.org:su-154595DiVA, id: diva2:1195400
Available from: 2018-04-05 Created: 2018-04-05 Last updated: 2018-04-05Bibliographically approved

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