메뉴 건너뛰기




Volumn 8, Issue 1, 2000, Pages 79-88

A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase

Author keywords

Cellobiose dehydrogenase; Cellulose degradation; Cytochrome; Electron transfer; Lignin degradation

Indexed keywords

CELLOBIOSE QUINONE OXIDOREDUCTASE; CYTOCHROME; FUNGAL ENZYME;

EID: 0034650750     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00082-4     Document Type: Article
Times cited : (132)

References (46)
  • 1
    • 0021813669 scopus 로고
    • Some properties of cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum
    • Morpeth F.F. Some properties of cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum. Biochem. J. 228:1985;557-564.
    • (1985) Biochem. J. , vol.228 , pp. 557-564
    • Morpeth, F.F.1
  • 2
    • 0028984129 scopus 로고
    • Cellobiose dehydrogenase (cellobiose oxidase) from Phanerochaete chrysosporium as a wood degrading enzyme - studies on cellulose, xylan and synthetic lignin
    • Henriksson G., Ander P., Pettersson B., Pettersson G. Cellobiose dehydrogenase (cellobiose oxidase) from Phanerochaete chrysosporium as a wood degrading enzyme - studies on cellulose, xylan and synthetic lignin. Appl. Microbiol. Biotechnol. 42:1995;790-796.
    • (1995) Appl. Microbiol. Biotechnol. , vol.42 , pp. 790-796
    • Henriksson, G.1    Ander, P.2    Pettersson, B.3    Pettersson, G.4
  • 4
    • 0030812766 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase, an active agent in cellulose depolymerization
    • Mansfield S.D., de Jong E., Saddler J.N. Cellobiose dehydrogenase, an active agent in cellulose depolymerization. Appl. Environ. Microbiol. 63:1997;3804-3809.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3804-3809
    • Mansfield, S.D.1    De Jong, E.2    Saddler, J.N.3
  • 5
    • 0027424610 scopus 로고
    • A combined cellobiose oxidase/glucose oxidase biosensor for HPLC determination on-line of glucose and soluble cellodextrines
    • Nordling M., Elmgren M., Ståhlberg J., Pettersson G., Lindquist S.-E. A combined cellobiose oxidase/glucose oxidase biosensor for HPLC determination on-line of glucose and soluble cellodextrines. Anal. Biochem. 214:1993;389-396.
    • (1993) Anal. Biochem. , vol.214 , pp. 389-396
    • Nordling, M.1    Elmgren, M.2    Ståhlberg, J.3    Pettersson, G.4    Lindquist, S.-E.5
  • 6
    • 0033166956 scopus 로고    scopus 로고
    • Degradation of chemicals by reactive radicals produced by cellobiose dehydrogenase from Phanerochaete chrysosporium
    • Cameron M.D., Aust S.D. Degradation of chemicals by reactive radicals produced by cellobiose dehydrogenase from Phanerochaete chrysosporium. Arch. Biochem. Biophys. 367:1999;115-121.
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 115-121
    • Cameron, M.D.1    Aust, S.D.2
  • 7
    • 0029085553 scopus 로고
    • Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium
    • Raices M., Pettersson G.et al. Cloning and characterization of a cDNA encoding a cellobiose dehydrogenase from the white rot fungus Phanerochaete chrysosporium. FEBS Lett. 369:1995;233-238.
    • (1995) FEBS Lett. , vol.369 , pp. 233-238
    • Raices, M.1    Pettersson, G.2
  • 8
    • 0029928876 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium
    • Li B., Nagalla S.R., Renganathan V. Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium. Appl. Environ. Microbiol. 62:1996;1329-1335.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1329-1335
    • Li, B.1    Nagalla, S.R.2    Renganathan, V.3
  • 9
    • 0026032346 scopus 로고
    • Cellobiose oxidase from Phanerochaete chrysosporium can be cleaved by papain into two domains
    • Henriksson G., Petterson G., Johansson G., Ruiz A., Uzcategui E. Cellobiose oxidase from Phanerochaete chrysosporium can be cleaved by papain into two domains. Eur. J. Biochem. 196:1991;101-106.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 101-106
    • Henriksson, G.1    Petterson, G.2    Johansson, G.3    Ruiz, A.4    Uzcategui, E.5
  • 10
    • 0016412938 scopus 로고
    • Purification and properties of cellobiose: Quinone oxidoreductase from Sporotrichum pulverulentum
    • Westermark U., Eriksson K.-E. Purification and properties of cellobiose: quinone oxidoreductase from Sporotrichum pulverulentum. Acta Chem. Scan. B. 29:1975;419-424.
    • (1975) Acta Chem. Scan. B , vol.29 , pp. 419-424
    • Westermark, U.1    Eriksson, K.-E.2
  • 11
    • 0026547564 scopus 로고
    • Evidence that that cellobiose:quinone oxidoreductase from Phanerochaete chrysosporium is a breakdown product of cellobiose oxidase
    • Wood J.D., Wood P.M. Evidence that that cellobiose:quinone oxidoreductase from Phanerochaete chrysosporium is a breakdown product of cellobiose oxidase. Biochim. Biophys. Acta. 1119:1992;90-96.
    • (1992) Biochim. Biophys. Acta , vol.1119 , pp. 90-96
    • Wood, J.D.1    Wood, P.M.2
  • 12
    • 0030852180 scopus 로고    scopus 로고
    • Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase I
    • Henriksson G., Salumets A., Divne C., Pettersson G. Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase I. Biochem. J. 324:1997;833-838.
    • (1997) Biochem. J. , vol.324 , pp. 833-838
    • Henriksson, G.1    Salumets, A.2    Divne, C.3    Pettersson, G.4
  • 13
    • 0028169897 scopus 로고
    • Direct 1H NMR evidence for conversion of β-D-cellobiose to cellobionolactone by cellobiose dehydrogenase from Phanerochaete chrysosporium
    • Higham C.W., Gordon-Smith D., Dempsey C.E., Wood P.M. Direct 1H NMR evidence for conversion of β-D-cellobiose to cellobionolactone by cellobiose dehydrogenase from Phanerochaete chrysosporium. FEBS Lett. 351:1994;128-132.
    • (1994) FEBS Lett. , vol.351 , pp. 128-132
    • Higham, C.W.1    Gordon-Smith, D.2    Dempsey, C.E.3    Wood, P.M.4
  • 14
    • 0027324150 scopus 로고
    • Is cellobiose oxidase from Phanerochaete chrysosporium a one-electron reductase?
    • Henriksson G., Johansson G., Pettersson G. Is cellobiose oxidase from Phanerochaete chrysosporium a one-electron reductase? Biochim. Biophys. Acta. 1144:1993;184-190.
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 184-190
    • Henriksson, G.1    Johansson, G.2    Pettersson, G.3
  • 15
    • 0026634164 scopus 로고
    • A comparison of the catalytic properties of cellobiose:quinone oxidoreductase and cellobiose oxidase from Phanerochaete chrysosporium
    • Samejima M., Eriksson K.-E. A comparison of the catalytic properties of cellobiose:quinone oxidoreductase and cellobiose oxidase from Phanerochaete chrysosporium. Eur. J. Biochem. 207:1992;103-107.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 103-107
    • Samejima, M.1    Eriksson, K.-E.2
  • 16
    • 0031570327 scopus 로고    scopus 로고
    • Resonance Raman spectroscopic studies of cellobiose dehydrogenase from Phanerochaete chrysosporium
    • Cohen J.D., Bao W., Renganathan V., Subramaniam S.S., Loehr T.M. Resonance Raman spectroscopic studies of cellobiose dehydrogenase from Phanerochaete chrysosporium. Arch. Biochem. Biophys. 341:1997;321-328.
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 321-328
    • Cohen, J.D.1    Bao, W.2    Renganathan, V.3    Subramaniam, S.S.4    Loehr, T.M.5
  • 17
    • 0026674531 scopus 로고
    • Production of Fenton's reagent by cellobiose oxidase from cellulolytic cultures of Phanerochaete chrysosporium
    • Kremer S.M., Wood P.M. Production of Fenton's reagent by cellobiose oxidase from cellulolytic cultures of Phanerochaete chrysosporium. Eur. J. Biochem. 208:1992;807-814.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 807-814
    • Kremer, S.M.1    Wood, P.M.2
  • 18
    • 0026778258 scopus 로고
    • Spectroscopic identification of the haem ligands of cellobiose oxidase
    • Cox M.C., Moore G.R.et al. Spectroscopic identification of the haem ligands of cellobiose oxidase. FEBS Lett. 307:1992;233-236.
    • (1992) FEBS Lett. , vol.307 , pp. 233-236
    • Cox, M.C.1    Moore, G.R.2
  • 19
    • 0027222127 scopus 로고
    • Purification and characterization of cellobiose dehydrogenase, a novel extracellular hemoflavoenzyme from the white-rot fungus Phanerochaete chrysosporium
    • Bao W., Usha S.N., Renganathan V. Purification and characterization of cellobiose dehydrogenase, a novel extracellular hemoflavoenzyme from the white-rot fungus Phanerochaete chrysosporium. Arch. Biochem. Biophys. 300:1993;705-713.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 705-713
    • Bao, W.1    Usha, S.N.2    Renganathan, V.3
  • 20
    • 0018786276 scopus 로고
    • The structure of cytochrome b562 from Escherichia coli at 2.5 Å resolution
    • Mathews F.S., Bethge P.H., Czerwinski E.W. The structure of cytochrome b562 from Escherichia coli at 2.5 Å resolution. J. Biol. Chem. 254:1979;1699-1706.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1699-1706
    • Mathews, F.S.1    Bethge, P.H.2    Czerwinski, E.W.3
  • 22
    • 0028519153 scopus 로고
    • The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium
    • Chen Z.W., Mathews F.S.et al. The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium. Science. 266:1994;430-432.
    • (1994) Science , vol.266 , pp. 430-432
    • Chen, Z.W.1    Mathews, F.S.2
  • 24
    • 0026071385 scopus 로고
    • Three-dimensional structure of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida at 3.0 Å resolution
    • Mathews F.S., Chen Z.W., Bellamy H.D., McIntire W.S. Three-dimensional structure of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida at 3.0 Å resolution. Biochemistry. 30:1991;238-247.
    • (1991) Biochemistry , vol.30 , pp. 238-247
    • Mathews, F.S.1    Chen, Z.W.2    Bellamy, H.D.3    McIntire, W.S.4
  • 25
    • 0030013409 scopus 로고    scopus 로고
    • 2 intraprotein electron transfer via an interdomain hinge region
    • 2 intraprotein electron transfer via an interdomain hinge region. Biochem. J. 316:1996;507-513.
    • (1996) Biochem. J. , vol.316 , pp. 507-513
    • Sharp, R.E.1    Chapman, S.K.2    Reid, G.A.3
  • 29
    • 0026740536 scopus 로고
    • Cellobiose oxidase from Phanerochaete chrysosporium. Stopped-flow spectrophotometric analysis of pH-dependent reduction
    • Samejima M., Phillips R.S., Eriksson K.-E. Cellobiose oxidase from Phanerochaete chrysosporium. Stopped-flow spectrophotometric analysis of pH-dependent reduction. FEBS Lett. 306:1992;165-168.
    • (1992) FEBS Lett. , vol.306 , pp. 165-168
    • Samejima, M.1    Phillips, R.S.2    Eriksson, K.-E.3
  • 30
    • 0027237670 scopus 로고
    • Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium
    • Habu N., Samejima M., Dean J., Eriksson K.-E. Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium. FEBS Lett. 327:1993;161-164.
    • (1993) FEBS Lett. , vol.327 , pp. 161-164
    • Habu, N.1    Samejima, M.2    Dean, J.3    Eriksson, K.-E.4
  • 31
    • 0030841589 scopus 로고    scopus 로고
    • Detecting folding motifs and similarities in protein structures
    • Kleywegt G.J., Jones T.A. Detecting folding motifs and similarities in protein structures. Methods Enzymol. 277:1997;525-545.
    • (1997) Methods Enzymol. , vol.277 , pp. 525-545
    • Kleywegt, G.J.1    Jones, T.A.2
  • 33
    • 17744417978 scopus 로고    scopus 로고
    • The three-dimensional structures of a polysaccharide binding antibody to Cryptococcus neoformans and its complex with a peptide from a phage display library: Implications for the identification of peptide mimotopes
    • Young A.C., Valadon P., Casadevall A., Scharff M.D., Sacchettini J.C. The three-dimensional structures of a polysaccharide binding antibody to Cryptococcus neoformans and its complex with a peptide from a phage display library: implications for the identification of peptide mimotopes. J. Mol. Biol. 274:1997;622-634.
    • (1997) J. Mol. Biol. , vol.274 , pp. 622-634
    • Young, A.C.1    Valadon, P.2    Casadevall, A.3    Scharff, M.D.4    Sacchettini, J.C.5
  • 34
    • 0028773015 scopus 로고
    • Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation
    • Martinez S.E., Huang D., Szczepaniak A., Cramer W.A., Smith J.L. Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. Structure. 2:1994;95-105.
    • (1994) Structure , vol.2 , pp. 95-105
    • Martinez, S.E.1    Huang, D.2    Szczepaniak, A.3    Cramer, W.A.4    Smith, J.L.5
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 38
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de la Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276:1997;472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 39
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 40
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger A.T., Warren G.L.et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D. 54:1998;905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1    Warren, G.L.2
  • 42
    • 0032988302 scopus 로고    scopus 로고
    • 1.7 Å structure of the stabilized REIv mutant T39K. Application of local NCS restraints
    • Uson I., Sheldrick G.M.et al. 1.7 Å structure of the stabilized REIv mutant T39K. Application of local NCS restraints. Acta Crystallogr. D. 55:1999;1158-1167.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1158-1167
    • Uson, I.1    Sheldrick, G.M.2
  • 45
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl.Crystallogr. 4:1991;946-950.
    • (1991) J. Appl.Crystallogr. , vol.4 , pp. 946-950
    • Kraulis, P.J.1
  • 46
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.