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

J Am Chem Soc. 2002 Nov 13;124(45):13392-3. doi: 10.1021/ja0279904.

Authors

Ryan MacArthur¹, Matthew H Sazinsky, Henriette Kühne, Douglas A Whittington, Stephen J Lippard, Gary W Brudvig

Affiliation

¹ Department of Chemistry, Yale University, P.O. Box 208107, New Haven, Connecticut 06520-8107, USA.

PMID: 12418885
DOI: 10.1021/ja0279904

Abstract

Spin-labeled Cys89 of the soluble methane monooxygenase regulatory protein (MMOB) from Methylococcus capsulatus (Bath) binds within 15 +/- 4 A 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 alpha-subunit.

Publication types

Research Support, U.S. Gov't, P.H.S.

MeSH terms

Binding Sites
Electron Spin Resonance Spectroscopy / methods
Kinetics
Methylococcus capsulatus / enzymology
Models, Molecular
Multienzyme Complexes / chemistry*
Multienzyme Complexes / metabolism
Oxygenases / chemistry*
Oxygenases / metabolism
Protein Conformation

Substances

Multienzyme Complexes
Oxygenases
methane monooxygenase

Abstract

Publication types

MeSH terms

Substances

Grants and funding