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

Chaemin Lee; Sung Chul Ha; Zhili Rao; Yunha Hwang; Da Som Kim; So Young Kim; Heeseon Yoo; Chungwoon Yoon; Jeong Geol Na; Jung Hee Park; Seung Jae Lee

doi:10.1039/d1dt03273a

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

Chaemin Lee
, Sung Chul Ha
, Zhili Rao
, Yunha Hwang
, Da Som Kim
, So Young Kim
, Heeseon Yoo
, Chungwoon Yoon
, Jeong Geol Na^*
, Jung Hee Park^*
, Seung Jae Lee^*

^*Corresponding author for this work

Research output: Contribution to journal › Journal article › peer-review

9 Scopus citations

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.

Original language	English
Pages (from-to)	16493-16498
Number of pages	6
Journal	Dalton Transactions
Volume	50
Issue number	45
DOIs	https://doi.org/10.1039/d1dt03273a
State	Published - 2021.12.7

Quacquarelli Symonds(QS) Subject Topics

Chemistry

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title = "Elucidation of the electron transfer environment in the MMOR FAD-binding domain from: Methylosinus sporium 5",

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.",

author = "Chaemin Lee and Ha, \{Sung Chul\} and Zhili Rao and Yunha Hwang and Kim, \{Da Som\} and Kim, \{So Young\} and Heeseon Yoo and Chungwoon Yoon and Na, \{Jeong Geol\} and Park, \{Jung Hee\} and Lee, \{Seung Jae\}",

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year = "2021",

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day = "7",

doi = "10.1039/d1dt03273a",

language = "English",

volume = "50",

pages = "16493--16498",

journal = "Dalton Transactions",

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TY - JOUR

T1 - Elucidation of the electron transfer environment in the MMOR FAD-binding domain from

T2 - Methylosinus sporium 5

AU - Lee, Chaemin

AU - Ha, Sung Chul

AU - Rao, Zhili

AU - Hwang, Yunha

AU - Kim, Da Som

AU - Kim, So Young

AU - Yoo, Heeseon

AU - Yoon, Chungwoon

AU - Na, Jeong Geol

AU - Park, Jung Hee

AU - Lee, Seung Jae

PY - 2021/12/7

Y1 - 2021/12/7

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/85120477794

U2 - 10.1039/d1dt03273a

DO - 10.1039/d1dt03273a

M3 - Journal article

C2 - 34734616

AN - SCOPUS:85120477794

SN - 1477-9226

VL - 50

SP - 16493

EP - 16498

JO - Dalton Transactions

JF - Dalton Transactions

IS - 45

ER -

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

Abstract

Quacquarelli Symonds(QS) Subject Topics

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