Structural highlights
Publication Abstract from PubMed
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.
Elucidation of the electron transfer environment in the MMOR FAD-binding domain from Methylosinus sporium 5.,Lee C, Ha SC, Rao Z, Hwang Y, Kim DS, Kim SY, Yoo H, Yoon C, Na JG, Park JH, Lee SJ Dalton Trans. 2021 Nov 23;50(45):16493-16498. doi: 10.1039/d1dt03273a. PMID:34734616[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee C, Ha SC, Rao Z, Hwang Y, Kim DS, Kim SY, Yoo H, Yoon C, Na JG, Park JH, Lee SJ. 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. PMID:34734616 doi:http://dx.doi.org/10.1039/d1dt03273a
