In:
Angewandte Chemie, Wiley, Vol. 132, No. 23 ( 2020-06-02), p. 9262-9270
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0044-8249
,
1521-3757
DOI:
10.1002/ange.v132.23
DOI:
10.1002/ange.202001363
Language:
English
Publisher:
Wiley
Publication Date:
2020
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505868-5
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514305-6
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505872-7
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1479266-7
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506259-7
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