A5101544859- Metal-Catalyzed Oxygenation Mechanisms
- Microbial metabolism and enzyme function
- Photosynthetic Processes and Mechanisms
- Metalloenzymes and iron-sulfur proteins
- Eicosanoids and Hypertension Pharmacology
- Heme Oxygenase-1 and Carbon Monoxide
- Diet, Metabolism, and Disease
- Liver Disease Diagnosis and Treatment
- Microbial bioremediation and biosurfactants
- Alcohol Consumption and Health Effects
Korea University
2025
Jeonbuk National University
2018-2021
Jeonju University
2021
Government of the Republic of Korea
2021
Soluble methane monooxygenase in methanotrophs converts to methanol under ambient conditions. The maximum catalytic activity of hydroxylase (MMOH) is achieved through the interplay its regulatory protein (MMOB) and reductase. An additional auxiliary protein, MMOD, functions as an inhibitor MMOH; however, inhibitory mechanism remains unknown. Here, we report crystal structure MMOH-MMOD complex from
The electronic structures of two cofactors, the FAD radical and [2Fe–2S]<sup>+</sup> reduced MMOR from <italic>Methylosinus sporium</italic> strain 5 were investigated by advanced EPR spectroscopy. findings provide long overdue detailed structural information MMOR.
Methane, an important greenhouse gas, has a 20-fold higher heat capacity than carbon dioxide. Earlier, through advanced spectroscopy and structural studies, the mechanisms underlying extremely stable C–H activation of soluble methane monooxygenase (sMMO) have been elucidated in Methylosinus trichosporium OB3b Methylococcus capsulatus Bath. Here, sMMO components—including hydroxylase (MMOH), regulatory (MMOB), reductase (MMOR)—were expressed purified from type II methanotroph, sporium strain...
By facilitating electron transfer to the hydroxylase diiron center, MMOR-a reductase-serves as an essential component of catalytic cycle soluble methane monooxygenase. Here, X-ray structure analysis FAD-binding domain MMOR identified crucial residues and its influence on cycle.