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阐明来自 5 的 MMOR FAD 结合域中的电子转移环境。

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

机构信息

Department of Chemistry and Institute of Molecular Biology and Genetics, Jeonbuk National University, Jeonju 54796, Republic of Korea.

Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang 37673, Republic of Korea.

出版信息

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

DOI:10.1039/d1dt03273a
PMID:34734616
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.

摘要

通过促进电子向羟化酶双核铁中心的转移，MMOR-还原酶作为可溶性甲烷单加氧酶催化循环的必需组成部分。在此，对 MMOR 的 FAD 结合结构域的 X 射线结构分析确定了关键残基及其对催化循环的影响。

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