Elucidation of the electron transfer environment in the MMOR FAD-binding domain from Methylosinus sporium 5

Dalton Trans. 2021 Nov 23;50(45):16493-16498. doi: 10.1039/d1dt03273a.

Abstract

By facilitating electron transfer to the hydroxylase diiron center, MMOR-a reductase-serves as an essential component of the catalytic cycle of soluble methane monooxygenase. Here, the X-ray structure analysis of the FAD-binding domain of MMOR identified crucial residues and its influence on the catalytic cycle.

MeSH terms

  • Binding Sites
  • Catalysis
  • Crystallography, X-Ray
  • Electron Transport
  • Flavin-Adenine Dinucleotide / chemistry
  • Flavin-Adenine Dinucleotide / metabolism*
  • Methylosinus / enzymology
  • Methylosinus / metabolism*
  • Oxidoreductases / chemistry
  • Oxidoreductases / metabolism*
  • Oxygenases / metabolism
  • Protein Conformation
  • Protein Domains

Substances

  • Flavin-Adenine Dinucleotide
  • Oxidoreductases
  • Oxygenases
  • methane monooxygenase

Supplementary concepts

  • Methylosinus sporium