Component B binding to the soluble methane monooxygenase hydroxylase by saturation-recovery EPR spectroscopy of spin-labeled MMOB

Ryan MacArthur; Matthew H. Sazinsky; Henriette Kühne; Douglas A. Whittington; Stephen J. Lippard; Gary W. Brudvig

doi:10.1021/ja0279904

Component B binding to the soluble methane monooxygenase hydroxylase by saturation-recovery EPR spectroscopy of spin-labeled MMOB

Ryan MacArthur, Matthew H. Sazinsky, Henriette Kühne, Douglas A. Whittington, Stephen J. Lippard, Gary W. Brudvig

Yale University

Research output: Contribution to journal › Article › peer-review

18 Citations (Scopus)

Abstract

Spin-labeled Cys89 of the soluble methane monooxygenase regulatory protein (MMOB) from Methylococcus capsulatus (Bath) binds within 15 ± 4 Å of the hydroxylase (MMOH) diiron center, placing the MMOB docking site in the MMOH "canyon" region on iron-coordinating helices E and F of the α-subunit.

Original language	English
Pages (from-to)	13392-13393
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	124
Issue number	45
DOIs	https://doi.org/10.1021/ja0279904
Publication status	Published - Nov 13 2002

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja0279904

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Component B binding to the soluble methane monooxygenase hydroxylase by saturation-recovery EPR spectroscopy of spin-labeled MMOB. / MacArthur, Ryan; Sazinsky, Matthew H.; Kühne, Henriette; Whittington, Douglas A.; Lippard, Stephen J.; Brudvig, Gary W.

In: Journal of the American Chemical Society, Vol. 124, No. 45, 13.11.2002, p. 13392-13393.

Research output: Contribution to journal › Article › peer-review

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abstract = "Spin-labeled Cys89 of the soluble methane monooxygenase regulatory protein (MMOB) from Methylococcus capsulatus (Bath) binds within 15 ± 4 {\AA} of the hydroxylase (MMOH) diiron center, placing the MMOB docking site in the MMOH {"}canyon{"} region on iron-coordinating helices E and F of the α-subunit.",

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AU - Lippard, Stephen J.

AU - Brudvig, Gary W.

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