title: Is cellobiose oxidase from Phanerochaete chrysosporium a one-electron reductase?
abstract: The heme domain of cellobiose oxidase (CBO) from Phanerochaete chrysosporium increases the rate of electron transfer to one-electron acceptors. This conclusion was drawn from comparisons of the rates of reduction of 3,5-t-butyl-o-benzoquinone, triiodide ion, cytochrome c and ferricyanide by intact CBO, FAD fragment and CBO with the heme inactivated by cyanide. The oxidation of cellobiose produced hydrogen peroxide, but the enzyme disturbs peroxidase-based assays by reduction of the product or by direct interaction with the peroxidase. CBO can also degrade hydrogen peroxide in the presence of cellobiose. The 1,2,4,5-tetramethoxybenzene cation radical was rapidly reduced by CBO.
authors.affiliation: Department of Biochemistry, University of Uppsala, Sweden.
authors.forename: G
authors.initials: G
authors.lastname: Henriksson
authors.forename: G
authors.initials: G
authors.lastname: Johansson
authors.forename: G
authors.initials: G
authors.lastname: Pettersson
mesh_terms: D002237:Carbohydrate Dehydrogenases / Q000737:chemistry*; D004579:Electron Transport; D005658:Fungi / Q000201:enzymology*; D006418:Heme / Q000737:chemistry; D008956:Models, Chemical
chemical_list: D006418:Heme; D002237:Carbohydrate Dehydrogenases; C019858:cellobiose oxidase