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 LeePublished 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.