title: Cellobiose oxidase from Phanerochaete chrysosporium. Stopped-flow spectrophotometric analysis of pH-dependent reduction.
abstract: Cellobiose oxidase (CBO) from Phanerochaete chrysosporium can utilize dichlorphenol-indophenol (Cl2Ind) and cytochrome c as effective electron acceptors for the oxidation of cellobiose. However, the pH dependencies of activity for these electron acceptors are significantly different. Both compounds act as effective electron acceptors at pH 4.2, whereas only dichlorophenol-indophenol is active at pH 5.9. To explain this discrepancy, the pH dependencies of the reduction rates of FAD and heme, respectively, in CBO by cellobiose have been investigated by stopped-flow spectrophotometry. Both FAD and heme are reduced with a high rate constant at pH 4.2. In contrast, at pH 5.9, only FAD reduction is fast, while the reduction of the heme is extremely slow. As a conclusion, the reduction of cytochrome c by CBO is dependent on heme, which functions at a lower pH range compared to reduction of FAD.
authors.affiliation: Department of Biochemistry, University of Georgia, Athens 30602-7229.
authors.forename: M
authors.initials: M
authors.lastname: Samejima
authors.forename: R S
authors.initials: RS
authors.lastname: Phillips
authors.forename: K E
authors.initials: KE
authors.lastname: Eriksson
mesh_terms: D002237:Carbohydrate Dehydrogenases / Q000378:metabolism*; D002733:Chlorophenols / Q000378:metabolism; D003574:Cytochrome c Group / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D006418:Heme / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007215:Indophenol / Q000378:metabolism; D007700:Kinetics; D010084:Oxidation-Reduction; D013053:Spectrophotometry; D013175:Sporothrix / Q000201:enzymology*
chemical_list: D002733:Chlorophenols; D003574:Cytochrome c Group; D005182:Flavin-Adenine Dinucleotide; D006418:Heme; D007215:Indophenol; D002237:Carbohydrate Dehydrogenases; C019858:cellobiose oxidase; C004762:2,4-dichlorophenol