Abstract:
:Cellobiose dehydrogenase (CDH), an extracellular hemoflavoenzyme produced by the cellulose-degrading cultures of Phanerochaete chrysosporium, oxidizes cellobiose to cellobionolactone. CDH has been purified to homogeneity by a five-step purification procedure. The homogeneous CDH is monomeric and has a relative molecular mass of 90,000. It is also a glycoprotein with a neutral carbohydrate content of 9.4%. Purified CDH contains one heme b and one flavin adenine dinucleotide per monomer. Homogeneous CDH has a specific activity of 10.3 mumol min-1 mg-1 for cytochrome c reduction, in the presence of cellobiose. Cellotriose, cellotetraose, cellopentaose, and lactose also serve as substrates for CDH, in addition to cellobiose. Cytochrome c, dichlorophenol-indophenol, Mn3+, and benzoquinones can function as electron acceptors in these oxidations. Kinetic studies suggest that cellobiose is the preferred substrate and cytochrome c is the preferred electron acceptor. In the absence of these electron acceptors, oxygen serves as a poor electron acceptor and is reduced to H2O2. CDH is very stable in the pH range 3-10 and up to 50 degrees C. At lower pH or at higher temperature, CDH is inactivated due to the release of flavin from the active site. The native ferric form of the enzyme has absorption maxima at 420, 529, and 570 nm. With the addition of cellobiose, these absorptions shift to 428, 534, and 564 nm. The ferric enzyme does not bind azide or cyanide, implying that the heme iron is probably hexacoordinate.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Bao W,Usha SN,Renganathan Vdoi
10.1006/abbi.1993.1098subject
Has Abstractpub_date
1993-02-01 00:00:00pages
705-13issue
2eissn
0003-9861issn
1096-0384pii
S0003986183710982journal_volume
300pub_type
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