Explorations of the nonheme high-valent iron-oxo landscape: crystal structure of a synthetic complex with an [FeIV2(μ-O)₂] diamond core relevant to the chemistry of sMMOH.

ABSTRACT: Methanotrophic bacteria utilize methane monooxygenase (MMO) to carry out the first step in metabolizing methane. The soluble enzymes employ a hydroxylase component (sMMOH) with a nonheme diiron active site that activates O₂ and generates a powerful oxidant capable of converting methane to methanol. It is proposed that the diiron(II) center in the reduced enzyme reacts with O₂ to generate a diferric-peroxo intermediate called P that then undergoes O-O cleavage to convert into a diiron(IV) derivative called Q, which carries out methane hydroxylation. Most (but not all) of the spectroscopic data of Q accumulated by various groups to date favor the presence of an FeIV2(μ-O)₂ unit with a diamond core. The Que lab has had a long-term interest in making synthetic

SUBMITTER: Rohde GT 

PROVIDER: S-EPMC9117492 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature