Recent advances in fungal cellobiose oxidoreductases

Eriksson, Karl–Erik L.; Habu, Naoto; Samejima, Masahiro

doi:10.1016/0141-0229(93)90046-5

Cited by 52 publications

(29 citation statements)

References 38 publications

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“…The most studied CDH is that of the white rot fungus Phanerochaete chrysosporium, however, the enzyme is produced by several other wood-degrading fungi as well. CDH oxidises cellodextrins, lactose and mannodextrins, and can employ a wide variety of electron acceptors including cytochrome c, quinones, triiodine ions, phenoxy radicals and complexed Fe(III) [2][3][4][5][6]. Interestingly, the enzyme binds strongly to cellulose, and the *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium

et al. 1995

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The eDNA of cellobiose dehydrogenase (CDH) fromPhanerochaete chrysosporium has been cloned and sequenced.The 5' end was obtained by PCR amplification. The cDNA contains 2310 translated bases excluding the poly(A) tail. The deduced mature protein contains 770 amino acid residues and is preceded by a 18 residue long signal peptide. The regions of the amino acid sequence corresponding to the heme and FAD domains of CDH were identified as well as the nucleotide-binding motif, the disulfide pairing and a methionine residue chelating the heme iron. No homologous sequences were found for the heme domain, however, the FAD domain appears to be distantly related to the GMC nxidoreductase family.

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Section: Introductionmentioning

confidence: 99%

Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium

et al. 1995

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“…Besides laccase, the ligninolytic system of these fungi includes several peroxidases (9,16,36,48), known as lignin peroxidase and manganese peroxidase (MnP), and oxidases that produce the hydrogen peroxide (H 2 O 2 ) needed for peroxidase activities (18,29). Another enzyme produced by these fungi, which functions in the degradation of not only lignin but also cellulose, is cellobiose dehydrogenase (11). Laccase catalyzes the one-electron oxidation of a wide range of phenolic compounds and aromatic amines (47).…”

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Oxygen Activation during Oxidation of Methoxyhydroquinones by Laccase from Pleurotus eryngii

Guillén

Muñoz

Gómez-Toribio

et al. 2000

Appl Environ Microbiol

105

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Oxygen activation during oxidation of the lignin-derived hydroquinones 2-methoxy-1,4-benzohydroquinone (MBQH 2 ) and 2,6-dimethoxy-1,4-benzohydroquinone (DBQH 2 ) by laccase from Pleurotus eryngii was examined. Laccase oxidized DBQH 2 more efficiently than it oxidized MBQH 2 ; both the affinity and maximal velocity of oxidation were higher for DBQH 2 than for MBQH 2 . Autoxidation of the semiquinones produced by laccase led to the activation of oxygen, producing superoxide anion radicals (

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“…In the course of cellulose degradation, many cellulolytic fungi produce extracellular cellobiose-oxidizing enzymes as well as cellulose-hydrolyzing enzymes such as cellulases (3)(4)(5). Cellobiose dehydrogenase (CDH, 1 EC 1.1.99.18) is a flavohemoprotein that oxidizes cellobiose using molecular oxygen as an electron acceptor (3).…”

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Cellobiose Dehydrogenase from the Fungi Phanerochaete chrysosporium and Humicola insolens

Igarashi¹,

Verhagen²,

Samejima³

et al. 1999

Journal of Biological Chemistry

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Cellobiose dehydrogenases (CDH) were purified from cellulose-grown cultures of the fungi Phanerochaete chrysosporium and Humicola insolens. The pH optimum of the cellobiose-cytochrome c oxidoreductase activity of P. chrysosporium CDH was acidic, whereas that of H. insolens CDH was neutral. The absorption spectra of the two CDHs showed them to be typical hemoproteins, but there was a small difference in the visible region. Limited proteolysis between the heme and flavin domains was performed to investigate the cofactors. There was no difference in absorption spectrum between the heme domains of P. chrysosporium and H. insolens CDHs. The midpoint potentials of heme at pH 7.0 were almost identical, and no difference in pH dependence was observed over the range of pH 3-9. The pH dependence of cellobiose oxidation by the flavin domains was similar to that of the native CDHs, indicating that the difference in the pH dependence of the catalytic activity between the two CDHs is because of the flavin domains. The absorption spectrum of the flavin domain from H. insolens CDH has absorbance maxima at 343 and 426 and a broad absorption peak at 660 nm, whereas that of P. chrysosporium CDH showed a normal flavoprotein spectrum. Flavin cofactors were extracted from the flavin domains and analyzed by high-performance liquid chromatography. The flavin cofactor from H. insolens was found to be a mixture of 60% 6-hydroxy-FAD and 40% FAD, whereas that from P. chrysosporium CDH was normal FAD. After reconstitution of the deflavo-proteins it was found that flavin domains containing 6-hydroxy-FAD were clearly active but their cellobiose oxidation rates were lower than those of flavin domains containing normal FAD. Reconstitution of flavin cofactor had no effect on the optimum pH. From these results, it is concluded that the pH dependence is not because of the flavin cofactor but is because of the protein molecule.

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Recent advances in fungal cellobiose oxidoreductases

Cited by 52 publications

References 38 publications

Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium

Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium

Oxygen Activation during Oxidation of Methoxyhydroquinones by Laccase from Pleurotus eryngii

Cellobiose Dehydrogenase from the Fungi Phanerochaete chrysosporium and Humicola insolens

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