title: Spectroscopic identification of the haem ligands of cellobiose oxidase.
abstract: A spectroscopic study of the flavocytochrome b enzyme, cellobiose oxidase, employing optical, NMR, EPR and near infra-red MCD techniques, has identified the axial ligands of the b-type haem. These are a histidine and a methionine, and this ligation set is discussed in relation to the functional role of the haem group.
authors.affiliation: Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences, University of East Anglia, Norwich UK.
authors.forename: M C
authors.initials: MC
authors.lastname: Cox
authors.forename: M S
authors.initials: MS
authors.lastname: Rogers
authors.forename: M
authors.initials: M
authors.lastname: Cheesman
authors.forename: G D
authors.initials: GD
authors.lastname: Jones
authors.forename: A J
authors.initials: AJ
authors.lastname: Thomson
authors.forename: M T
authors.initials: MT
authors.lastname: Wilson
authors.forename: G R
authors.initials: GR
authors.lastname: Moore
mesh_terms: D002237:Carbohydrate Dehydrogenases / Q000737:chemistry*; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D006418:Heme / Q000032:analysis*; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D010084:Oxidation-Reduction
chemical_list: D008024:Ligands; D006418:Heme; D002237:Carbohydrate Dehydrogenases; C019858:cellobiose oxidase