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Nickel(II)‐Mediated Reversible Thiolate/Disulfide Conversion as a Mimic for a Key Step of the Catalytic Cycle of Methyl‐Coenzyme M Reductase
Author(s) -
Bhandari Anirban,
Mishra Saikat,
Maji Ram Chandra,
Kumar Akhilesh,
Olmstead Marilyn M.,
Patra Apurba K.
Publication year - 2020
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.202001363
Subject(s) - chemistry , catalytic cycle , catalysis , disulfide bond , nickel , thiol , cofactor , reductase , combinatorial chemistry , stereochemistry , enzyme , organic chemistry , biochemistry
According to the well‐accepted mechanism, methyl‐coenzyme M reductase (MCR) involves Ni‐mediated thiolate‐to‐disulfide conversion that sustains its catalytic cycle of methane formation in the energy saving pathways of methanotrophic microbes. Model complexes that illustrate Ni‐ion mediated reversible thiolate/disulfide transformation are unknown. In this paper we report the synthesis, crystal structure, spectroscopic properties and redox interconversions of a set of Ni II complexes comprising a tridentate N 2 S donor thiol and its analogous N 4 S 2 donor disulfide ligands. These complexes demonstrate reversible Ni II ‐thiolate/Ni II ‐disulfide (both bound and unbound disulfide‐S to Ni II ) transformations via thiyl and disulfide monoradical anions that resemble a primary step of MCR's catalytic cycle.