title: Component B binding to the soluble methane monooxygenase hydroxylase by saturation-recovery EPR spectroscopy of spin-labeled MMOB.
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.
authors.affiliation: Department of Chemistry, Yale University, P.O. Box 208107, New Haven, Connecticut 06520-8107, USA.
authors.forename: Ryan
authors.initials: R
authors.lastname: MacArthur
authors.forename: Matthew H
authors.initials: MH
authors.lastname: Sazinsky
authors.forename: Henriette
authors.initials: H
authors.lastname: Kühne
authors.forename: Douglas A
authors.initials: DA
authors.lastname: Whittington
authors.forename: Stephen J
authors.initials: SJ
authors.lastname: Lippard
authors.forename: Gary W
authors.initials: GW
authors.lastname: Brudvig
mesh_terms: D001665:Binding Sites; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D007700:Kinetics; D020619:Methylococcus capsulatus / Q000201:enzymology; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000378:metabolism; D010105:Oxygenases / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D009097:Multienzyme Complexes; D010105:Oxygenases; C021555:methane monooxygenase