Role of the flavin domain residues, His689 and Asn732, in the catalytic mechanism of cellobiose dehydrogenase from phanerochaete chrysosporium

Biochemistry

Volumn 42, Issue 14, 2003, Pages 4049-4056

  Rotsaert, Frederik A J ^a   Renganathan, V ^a   Gold, Michael H ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON ACCEPTORS;

CATALYSIS; ENZYMES; MUTAGENESIS; OXIDATION;

BIOCHEMISTRY;

CELLOBIOSE; CELLOBIOSE QUINONE OXIDOREDUCTASE; FLAVOPROTEIN; LACTATE DEHYDROGENASE (CYTOCHROME); LACTOSE; OLIGOSACCHARIDE; QUERCETIN;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ASSAY; ENZYME KINETICS; EPIMER; HYDROGEN BOND; MOLECULAR MECHANICS; MOLECULAR MODEL; NONHUMAN; OXIDATION; PHANEROCHAETE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; STEADY STATE; STEREOCHEMISTRY;

ASPARAGINE; BINDING SITES; CARBOHYDRATE DEHYDROGENASES; CATALYSIS; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MUTAGENESIS, SITE-DIRECTED; PHANEROCHAETE;

CHRYSOSPORIUM; PHANEROCHAETE; PHANEROCHAETE CHRYSOSPORIUM;

EID: 0037446732     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi027092k     Document Type: Article

References (49)

1. Henriksson, G., Johansson, G., and Pettersson, G. (2000) A critical review of cellobiose dehydrogenases, J. Biotechnol. 78, 93-113.
2. Li, B., Nagalla, S. R., and Renganathan, V. (1996) Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium, Appl. Environ. Microbiol. 62, 1329-1335.
3. Dumonceaux, T., Bartholomew, K., Valeanu, L., Charles, T., and Archibald, F. (2001) Cellobiose dehydrogenase is essential for wood invasion and nonessential for kraft pulp delignification by Trametes versicolor, Enzyme Microb. Technol. 29, 478-489.
4. Ayers, A. R., Ayers, S. B., and Eriksson, K. E. (1978) Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum, Eur. J. Biochem. 90, 171-181.
5. Bao, W., Usha, S. N., and Renganathan, V. (1993) Purification and characterization of cellobiose dehydrogenase, a novel extra-cellular hemoflavoenzyme from the white-rot fungus Phanerochaete chrysosporium, Arch. Biochem. Biophys. 300, 705-713.
6. Habu, N., Samejima, M., Dean, J. F., and Eriksson, K. E. (1993) Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium, FEBS Lett. 327, 161-164.
7. Henriksson, G., Pettersson, G., Johansson, G., Ruiz, A., and Uzcategui, E. (1991) Cellobiose oxidase from Phanerochaete chrysosporium can be cleaved by papain into two domains, Eur. J. Biochem. 196, 101-106.
8. Gilkes, N. R., Henrissat, B., Kilburn, D. G., Miller, R. C., Jr., and Warren, R. A. (1991) Domains in microbial β-1,4-glycanases: sequence conservation, function, and enzyme families, Microbiol. Rev. 55, 303-315.
9. Samejima, M., and Eriksson, K. E. (1992) A comparison of the catalytic properties of cellobiose: quinone oxidoreductase and cellobiose oxidase from Phanerochaete chrysosporium, Eur. J. Biochem. 207, 103-107.
10. Rotsaert, F. A., Li, B., Renganathan, V., and Gold, M. H. (2001) Site-directed mutagenesis of the heme axial ligands in the hemoflavoenzyme cellobiose dehydrogenase, Arch. Biochem. Biophys. 390, 206-214.
11. 1H NMR evidence for conversion of β-D-cellobiose to cellobionolactone by cellobiose dehydrogenase from Phanerochaete chrysosporium, FEBS Lett. 351, 128-132.
12. Hallberg, B. M., Bergfors, T., Backbro, K., Pettersson, G., Herriksson, G., and Divne, C. (2000) A new scaffold for binding heam in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase, Structure 8, 79-88.
13. Hallberg, B. M., Henriksson, G., Pettersson, G., and Divne, C. (2002) Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase, J. Mol. Biol. 315, 421-434.
14. Raices, M., Paifer, E., Cremata, J., Montesino, R., Stahlberg, J., Divne, C., Szabo Istvan, J., Henriksson, G., Johansson, G., and Pettersson, G. (1995) Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium, FEBS Lett. 369, 233-238.
15. Kiess, M., Hecht, H. J., and Kalisz, H. M. (1998) Glucose oxidase from Penicillium amagasakiense. Primary structure and comparison with other glucose-methanol-choline (GMC) oxidoreductases, Eur. J. Biochem. 252, 90-99.
16. Cavener, D. R. (1992) GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities, J. Mol. Biol. 223, 811-814.
17. Wohlfahrt, G., Witt, S., Hendle, J., Schomburg, D., Kalisz, H. M., and Hecht, H. J. (1999) 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes, Acta Crystallogr. D 55, 969-977.
18. Li, J., Vrielink, A., Brick, P., and Blow, D. M. (1993) Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases, Biochemistry 32, 11507-11515.
19. Vrielink, A., Lloyd, L. F., and Blow, D. M. (1991) Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution, J. Mol. Biol. 219, 533-554.
20. Akileswaran, L., Alic, M., Clark, E. K., Hornick, J. L., and Gold, M. H. (1993) Isolation and transformation of uracil auxotrophs of the lignin-degrading basidiomycete Phanerochaete chrysosporium, Curr. Genet. 23, 351-356.
21. Li, B., Rotsaert, F. A. J., Gold, M. H., and Renganathan, V. (2000) Homologous expression of recombinant cellobiose dehydrogenase in Phanerochaete chrysosporium, Biochem. Biophys. Res. Commun. 270, 141-146.
22. Sollewijn Gelpke, M. D., Mayfield-Gambill, M., Cereghino, G. P. L., and Gold, M. H. (1999) Homologous expression of recombinant lignin peroxidase in Phanerochaete chrysosporium, Appl. Environ. Microbiol. 65, 1670-1674.
23. Alic, M., Mayfield, M. B., Akileswaran, L., and Gold, M. H. (1991) Homologous transformation of the lignin-degrading basidiomycete Phanerochaete chrysosporium, Curr. Genet. 19, 491-494.
24. Alic, M., Kornegay, J. R., Pribnow, D., and Gold, M. H. (1989) Transformation by complementation of an adenine auxotroph of the lignin-degrading basidiomycete Phanerochaete chrysosporium, Appl. Environ. Microbiol. 55, 406-411.
25. Igarashi, K., Verhagen, M. F., Samejima, M., Schulein, M., Eriksson, K. E., and Nishino, T. (1999) Cellobiose dehydrogenase from the fungi Phanerochaete chrysosporium and Humicola insolens. A flavohemoprotein from Humicola insolens contains 6-hydroxy-FAD as the dominant active cofactor, J. Biol. Chem. 274, 3338-3344.
26. Morpeth, F. F. (1985) Some properties of cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum, Biochem. J. 228, 557-564.
27. Cohen, J. D., Bao, W., Renganathan, V., Subramaniam, S. S., and Loehr, T. M. (1997) Resonance Raman spectroscopic studies of cellobiose dehydrogenase from Phanerochaete chrysosporium, Arch. Biochem. Biophys. 341, 321-328.
28. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
29. Hazzard, J. T., Cusanovich, M. A., Tainer, J. A., Getzoff, E. D., and Tollin, G. (1986) Kinetic studies of reduction of a 1:1 cytochrome c-flavodoxin complex by free flavin semiquinones and rubredoxin, Biochemistry 25, 3318-3328.
30. Fersht, A. (1985) Enzyme Structure and Mechanism, 2nd ed., pp 301-307, W. H. Freeman and Company, New York.
31. Silverman, R. B., Hoffman, S. J., and Catus, W. B., III (1980) A mechanism for mitochondrial monoamine oxidase catalyzed amine oxidation, J. Am. Chem. Soc. 102, 7126-7128.
32. Ghisla, S., and Massey, V. (1989) Mechanisms of flavoprotein-catalyzed reactions, Eur. J. Biochem. 181, 1-17.
33. Hecht, H. J., Kalisz, H. M., Hendle, J., Schmid, R. D., and Schomburg, D. (1993) Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 Å resolution, J. Mol. Biol. 229, 153-172.
34. Yue, Q. K., Kass, I. J., Sampson, N. S., and Vrielink, A. (1999) Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants, Biochemistry 38, 4277-4286.
35. Witt, S., Wohlfahrt, G., Schomburg, D., Hecht, H. J., and Kalisz, H. M. (2000) Conserved arginine-516 of Penicillium amagasakiense glucose oxidase is essential for the efficient binding of β-D-glucose, Biochem. J. 347, 553-559.
36. Yamashita, M., Toyama, M., Ono, H., Fujii, I., Hirayama, N., and Murooka, Y. (1998) Separation of the two reactions, oxidation and isomerization, catalyzed by Streptomyces cholesterol oxidase, Protein Eng. 11, 1075-1081.
37. Kass, I. J., and Sampson, N. S. (1998) Evaluation of the role of His447 in the reaction catalyzed by cholesterol oxidase, Biochemistry 37, 17990-18000.
38. Yin, Y., Sampson, N. S., Vrielink, A., and Lario, P. I. (2001) The presence of a hydrogen bond between asparagine 485 and the π system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidase, Biochemistry 40, 13779-13787.
39. Street, I. P., Armstrong, C. R., and Withers, S. G. (1986) Hydrogen bonding and specificity. Fluorodeoxy sugars as probes of hydrogen bonding in the glycogen phosphorylase-glucose complex, Biochemistry 25, 6021-6027.
40. Johnson, F. A., Lewis, S. D., and Shafer, J. A. (1981) Perturbations in the free energy and enthalpy of ionization of histidine-159 at the active site of papain as determined by fluorescence spectroscopy, Biochemistry 20, 52-58.
41. Kamphuis, I. G., Kalk, K. H., Swarte, M. B., and Drenth, J. (1984) Structure of papain refined at 1.65 Å resolution, J. Mol. Biol. 179, 233-256.
42. Schou, C., Christensen, M. H., and Schulein, M. (1998) Characterization of a cellobiose dehydrogenase from Humicola insolens, Biochem. J. 330, 565-571.
43. Xu, F., Golightly, E. J., Duke, K. R., Lassen, S. F., Knusen, B., Christensen, S., Brown, K. M., Brown, S. H., and Schulein, M. (2001) Humicola insolens cellobiose dehydrogenase: cloning, redox chemistry, and logic gate-like dual functionality, Enzyme Microb. Technol. 28, 744-753.
44. Moukha, S. M., Dumonceaux, T. J., Record, E., and Archibald, F. S. (1999) Cloning and analysis of Pycnoporus cinnabarinus cellobiose dehydrogenase, Gene 234, 23-33.
45. Dumonceaux, T. J., Bartholomew, K. A., Charles, T. C., Moukha, S. M., and Archibald, F. S. (1998) Cloning and sequencing of a gene encoding cellobiose dehydrogenase from Trametes versicolor, Gene 210, 211-219.
46. Subramaniam, S. S., Nagalla, S. R., and Renganathan, V. (1999) Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile, Arch. Biochem. Biophys. 365, 223-230.
47. Yagi, K., Ohishi, N., Nishimoto, K., Choi, J. D., and Song, P. S. (1980) Effect of hydrogen bonding on electronic spectra and reactivity of flavins, Biochemistry 19, 1553-1557.
48. Fraaije, M. W., and Mattevi, A. (2000) Flavoenzymes: diverse catalysts with recurrent features, Trends Biochem. Sci. 25, 126-132.
49. Xu, D., Kohli, R. M., and Massey, V. (1999) The role of threonine 37 in flavin reactivity of the old yellow enzyme, Proc. Natl. Acad. Sci. U.S.A. 96, 3556-3561.