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

Research output: Contribution to journalArticle

16 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 languageEnglish
Pages (from-to)13392-13393
Number of pages2
JournalJournal of the American Chemical Society
Volume124
Issue number45
DOIs
Publication statusPublished - Nov 13 2002

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methane monooxygenase
Methylococcus capsulatus
Mixed Function Oxygenases
Baths
Paramagnetic resonance
Spectrum Analysis
Methane
Iron
Spectroscopy
Proteins
Recovery

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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 journalArticle

MacArthur, Ryan ; Sazinsky, Matthew H. ; Kühne, Henriette ; Whittington, Douglas A. ; Lippard, Stephen J. ; Brudvig, Gary W. / Component B binding to the soluble methane monooxygenase hydroxylase by saturation-recovery EPR spectroscopy of spin-labeled MMOB. In: Journal of the American Chemical Society. 2002 ; Vol. 124, No. 45. pp. 13392-13393.
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