Format:
1 Online-Ressource (10 Seiten)
ISSN:
0002-7863
,
0002-7863
Content:
Cytochrome c oxidase (CcO) is a heme copper oxidase (HCO) that catalyzes the natural reduction of oxygen to water. A profound understanding of some of the elementary steps leading to the intricate 4e–/4H+ reduction of O2 is presently lacking. A total spin St = 1 FeIII–(O22–)–CuII (IP) intermediate is proposed to reduce the overpotentials associated with the reductive O–O bond rupture by allowing electron transfer from a tyrosine moiety without the necessity of any spin-surface crossing. Direct evidence of the involvement of IP in the CcO catalytic cycle is, however, missing. A number of heme copper peroxido complexes have been prepared as synthetic models of IP, but all of them possess the catalytically nonrelevant St = 0 ground state resulting from antiferromagnetic coupling between the S = 1/2 FeIII and CuII centers. In a complete nonheme approach, we now report the spectroscopic characterization and reactivity of the FeIII–(O22–)–CuII intermediates 1 and 2, which differ only by a single −CH3 versus −H substituent on the central amine of the tridentate ligands binding to copper. Complex 1 with an end-on peroxido core and ferromagnetically (St = 1) coupled FeIII and CuII centers performs H-bonding-mediated O–O bond cleavage in the presence of phenol to generate oxoiron(IV) and exchange-coupled copper(II) and PhO• moieties. In contrast, the μ-η2:η1 peroxido complex 2, with a St = 0 ground state, is unreactive toward phenol. Thus, the implications for spin topology contributions to O–O bond cleavage, as proposed for the heme FeIII–(O22–)–CuII intermediate in CcO, can be extended to nonheme chemistry.
Content:
Peer Reviewed
In:
Washington, DC : American Chemical Society, 146,36, Seiten 24808-24817, 0002-7863
Language:
English
DOI:
10.1021/jacs.4c04492
URN:
urn:nbn:de:kobv:11-110-18452/29998-3
URL:
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