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

Chaemin LeeSung Chul HaZhili RaoYunha HwangDa Som KimSo Young KimHeeseon YooChungwoon YoonJeong-Geol NaJung Hee ParkSeung Jae Lee
Published in: Dalton transactions (Cambridge, England : 2003) (2021)
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.
Keyphrases
  • electron transfer
  • dna binding
  • high resolution
  • binding protein
  • crystal structure
  • anaerobic digestion
  • dual energy
  • carbon dioxide
  • computed tomography
  • magnetic resonance
  • transcription factor