Structure-Spectroscopy Correlations for Intermediate Q of Soluble Methane Monooxygenase: Insights from QM/MM Calculations.

ABSTRACT: The determination of the diiron core intermediate structures involved in the catalytic cycle of soluble methane monooxygenase (sMMO), the enzyme that selectively catalyzes the conversion of methane to methanol, has been a subject of intense interest within the bioinorganic scientific community. Particularly, the specific geometry and electronic structure of the intermediate that precedes methane binding, known as intermediate Q (or MMOH_Q), has been debated for over 30 years. Some reported studies support a bis-μ-oxo-bridged Fe(IV)₂O₂ closed-core conformation Fe(IV)₂O₂ core, whereas others favor an open-core geometry, with a longer Fe-Fe distance. The lack of consensus calls for a thorough re-examination and reinterpretation of the spec

SUBMITTER: Schulz CE 

PROVIDER: S-EPMC8154522 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature