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

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          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.

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          Author and article information

          Journal
          Dalton Trans
          Dalton transactions (Cambridge, England : 2003)
          Royal Society of Chemistry (RSC)
          1477-9234
          1477-9226
          Nov 23 2021
          : 50
          : 45
          Affiliations
          [1 ] Department of Chemistry and Institute of Molecular Biology and Genetics, Jeonbuk National University, Jeonju 54796, Republic of Korea. slee026@jbnu.ac.kr.
          [2 ] Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang 37673, Republic of Korea.
          [3 ] Division of Biotechnology, College of Environmental & Bioresources Sciences, Jeonbuk National University, Iksan 54596, Republic of Korea. junghee.park@jbnu.ac.kr.
          [4 ] Department of Chemical and Biomolecular Engineering, Sogang University, Seoul 04107, Republic of Korea. narosu@u.sogang.ac.kr.
          [5 ] Advanced Institute of Environment and Bioscience, College of Environmental & Bioresources Sciences, Jeonbuk National University, Iksan 54596, Republic of Korea.
          Article
          10.1039/d1dt03273a
          34734616
          36b97fee-a04d-4a7b-a8a8-f6fab1fd8bf9
          History

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