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Volumn 45, Issue 39, 2006, Pages 11934-11944

Putidaredoxin-to-cytochrome P450cam electron transfer: Differences between the two reductive steps required for catalysis

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYSIS; GENE TRANSFER; MUTAGENESIS; PROTEINS; REDOX REACTIONS;

EID: 33749333744     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0611154     Document Type: Article
Times cited : (63)

References (79)
  • 1
    • 0014429758 scopus 로고
    • A soluble cytochrome P450 functional in methylene hydroxylation
    • Katagiri, M., Ganguli, B. N., and Gunsalus, I. C. (1968) A soluble cytochrome P450 functional in methylene hydroxylation, J. Biol. Chem. 243, 3543-3546.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3543-3546
    • Katagiri, M.1    Ganguli, B.N.2    Gunsalus, I.C.3
  • 2
    • 0015209652 scopus 로고
    • Composition and structure of camphor hydroxylase components and homology between putidaredoxin and adrenodoxin
    • Tsai, R. L., Gunsalus, I. C., and Dus, K. (1971) Composition and structure of camphor hydroxylase components and homology between putidaredoxin and adrenodoxin, Biochem. Biophys. Res. Commun. 45, 1300-1306.
    • (1971) Biochem. Biophys. Res. Commun. , vol.45 , pp. 1300-1306
    • Tsai, R.L.1    Gunsalus, I.C.2    Dus, K.3
  • 3
    • 0015523673 scopus 로고
    • The role of putidaredoxin and P450cam in methylene hydroxylation
    • Tyson, C. A., Lipscomb, J. D., and Gunsalus, I. C. (1972) The role of putidaredoxin and P450cam in methylene hydroxylation, J. Biol. Chem. 247, 5777-5784.
    • (1972) J. Biol. Chem. , vol.247 , pp. 5777-5784
    • Tyson, C.A.1    Lipscomb, J.D.2    Gunsalus, I.C.3
  • 4
    • 0022930461 scopus 로고
    • The involvement of carboxylate groups of putidaredoxin in the reaction with putidaredoxin reductase
    • Geren, L., Tuls, J., O'Brien, P., Millett, F., and Peterson, J. A. (1986) The involvement of carboxylate groups of putidaredoxin in the reaction with putidaredoxin reductase, J. Biol. Chem. 261, 15491-15495.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15491-15495
    • Geren, L.1    Tuls, J.2    O'Brien, P.3    Millett, F.4    Peterson, J.A.5
  • 6
    • 0017295461 scopus 로고
    • Autooxidation and hydroxylation reactions of oxygenated cytochrome P450cam
    • Lipscomb, J. D., Sligar, S. G., Namtvedt, M. J., and Gunsalus, I. C. (1976) Autooxidation and hydroxylation reactions of oxygenated cytochrome P450cam, J. Biol. Chem. 251, 1116-1124.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1116-1124
    • Lipscomb, J.D.1    Sligar, S.G.2    Namtvedt, M.J.3    Gunsalus, I.C.4
  • 8
    • 0017847807 scopus 로고
    • Two univalent electron transfers from putidaredoxin to bacterial cytochrome P450 at subzero temperature
    • Hoa, G. H., Begard, E., Debey, P., and Gunsalus, I. C. (1978) Two univalent electron transfers from putidaredoxin to bacterial cytochrome P450 at subzero temperature, Biochemistry 17, 2835-2839.
    • (1978) Biochemistry , vol.17 , pp. 2835-2839
    • Hoa, G.H.1    Begard, E.2    Debey, P.3    Gunsalus, I.C.4
  • 9
    • 0023867587 scopus 로고
    • Single turnover kinetics of the reaction between oxycytochrome P450cam and reduced putidaredoxin
    • Brewer, C. B., and Peterson, J. A. (1988) Single turnover kinetics of the reaction between oxycytochrome P450cam and reduced putidaredoxin, J. Biol. Chem. 263, 791-798.
    • (1988) J. Biol. Chem. , vol.263 , pp. 791-798
    • Brewer, C.B.1    Peterson, J.A.2
  • 10
    • 0029666288 scopus 로고    scopus 로고
    • Role of Arg112 of cytochrome P450cam in the electron transfer from reduced putidaredoxin. Analyses with site-directed mutants
    • Unno, M., Shimada, H., Toba, Y., Makino, R., and Ishimura, Y. (1996) Role of Arg112 of cytochrome P450cam in the electron transfer from reduced putidaredoxin. Analyses with site-directed mutants, J. Biol. Chem. 271, 17869-17874.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17869-17874
    • Unno, M.1    Shimada, H.2    Toba, Y.3    Makino, R.4    Ishimura, Y.5
  • 13
    • 0025195188 scopus 로고
    • The cytochrome P450cam binding surface as defined by site-directed mutagenesis and electrostatic modeling
    • Stayton, P. S., and Sligar, S. G. (1990) The cytochrome P450cam binding surface as defined by site-directed mutagenesis and electrostatic modeling, Biochemistry 29, 7381-7386.
    • (1990) Biochemistry , vol.29 , pp. 7381-7386
    • Stayton, P.S.1    Sligar, S.G.2
  • 15
    • 0030457189 scopus 로고    scopus 로고
    • A structure-based model for cytochrome P450cam-putidaredoxin interactions
    • Pochapsky, T. C., Lyons, T. A., Kazanis, S., Arakaki, T., and Ratnaswamy, G. (1996) A structure-based model for cytochrome P450cam-putidaredoxin interactions, Biochimie 78, 723-733.
    • (1996) Biochimie , vol.78 , pp. 723-733
    • Pochapsky, T.C.1    Lyons, T.A.2    Kazanis, S.3    Arakaki, T.4    Ratnaswamy, G.5
  • 16
    • 21944432511 scopus 로고    scopus 로고
    • Theoretical perspective on the structure and mechanism of cytochrome P450 enzymes
    • Shaik, S., Kumar, D., de Visser, S. P., Altun, A., and Thiel, W. (2005) Theoretical perspective on the structure and mechanism of cytochrome P450 enzymes, Chem. Rev. 105, 2279-2328.
    • (2005) Chem. Rev. , vol.105 , pp. 2279-2328
    • Shaik, S.1    Kumar, D.2    De Visser, S.P.3    Altun, A.4    Thiel, W.5
  • 18
    • 0034739018 scopus 로고    scopus 로고
    • Roles of the axial push effect in cytochrome P450cam studied with the site-directed mutagenesis at the heme proximal site
    • Yoshioka, S., Takahashi, S., Ishimori, K., and Morishima, I. (2000) Roles of the axial push effect in cytochrome P450cam studied with the site-directed mutagenesis at the heme proximal site, J. Inorg. Biochem. 81, 141-151.
    • (2000) J. Inorg. Biochem. , vol.81 , pp. 141-151
    • Yoshioka, S.1    Takahashi, S.2    Ishimori, K.3    Morishima, I.4
  • 19
    • 0037065303 scopus 로고    scopus 로고
    • Roles of the proximal hydrogen bonding network in cytochrome P450cam-catalyzed oxygenation
    • Yoshioka, S., Tosha, T., Takahashi, S., Ishimori, K., Hori, H., and Morishima, I. (2002) Roles of the proximal hydrogen bonding network in cytochrome P450cam-catalyzed oxygenation, J. Am. Chem. Soc. 124, 14571-14579.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14571-14579
    • Yoshioka, S.1    Tosha, T.2    Takahashi, S.3    Ishimori, K.4    Hori, H.5    Morishima, I.6
  • 20
    • 0037169558 scopus 로고    scopus 로고
    • Complex formation of cytochrome P450cam with putidaredoxin. Evidence for protein-specific interactions involving the proximal thiolate ligand
    • Unno, M., Christian, J. F., Sjodin, T., Benson, D. E., Macdonald, I. D., Sligar, S. G., and Champion, P. M. (2002) Complex formation of cytochrome P450cam with putidaredoxin. Evidence for protein-specific interactions involving the proximal thiolate ligand, J. Biol. Chem. 277, 2547-2553.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2547-2553
    • Unno, M.1    Christian, J.F.2    Sjodin, T.3    Benson, D.E.4    Macdonald, I.D.5    Sligar, S.G.6    Champion, P.M.7
  • 21
    • 5644272669 scopus 로고    scopus 로고
    • L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: The structural changes trigger electron transfer to oxy-P450cam from electron donors
    • Tosha, T., Yoshioka, S., Ishimori, K., and Morishima, I. (2004) L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: the structural changes trigger electron transfer to oxy-P450cam from electron donors, J. Biol. Chem. 279, 42836-42843.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42836-42843
    • Tosha, T.1    Yoshioka, S.2    Ishimori, K.3    Morishima, I.4
  • 22
    • 5644282610 scopus 로고    scopus 로고
    • Crystal structure of the cytochrome P450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding
    • Nagano, S., Tosha, T., Ishimori, K., Morishima, I., and Poulos, T. L. (2004) Crystal structure of the cytochrome P450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding, J. Biol. Chem. 279, 42844-42849.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42844-42849
    • Nagano, S.1    Tosha, T.2    Ishimori, K.3    Morishima, I.4    Poulos, T.L.5
  • 23
    • 0037614992 scopus 로고    scopus 로고
    • A model for effector activity in a highly specific biological electron transfer complex: The cytochrome P450cam-putidaredoxin couple
    • Pochapsky, S. S., Pochapsky, T. C., and Wei, J. W. (2003) A model for effector activity in a highly specific biological electron transfer complex: The cytochrome P450cam-putidaredoxin couple, Biochemistry 42, 5649-5656.
    • (2003) Biochemistry , vol.42 , pp. 5649-5656
    • Pochapsky, S.S.1    Pochapsky, T.C.2    Wei, J.W.3
  • 24
    • 33645451369 scopus 로고    scopus 로고
    • 5 and putidaredoxin, two effectors of camphor hydroxylase activity
    • 5 and putidaredoxin, two effectors of camphor hydroxylase activity, Biochemistry 45, 3887-3897.
    • (2006) Biochemistry , vol.45 , pp. 3887-3897
    • Rui, L.1    Pochapsky, S.S.2    Pochapsky, T.C.3
  • 25
    • 0028307538 scopus 로고
    • An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2Fe-2S ferredoxin from Pseudomonas
    • Pochapsky, T. C., Ye, X. M., Ratnaswamy, G., and Lyons, T. A. (1994) An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2Fe-2S ferredoxin from Pseudomonas, Biochemistry 33, 6424-6432.
    • (1994) Biochemistry , vol.33 , pp. 6424-6432
    • Pochapsky, T.C.1    Ye, X.M.2    Ratnaswamy, G.3    Lyons, T.A.4
  • 26
    • 0141869098 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida
    • Sevrioukova, I. F., Garcia, C., Li, H., Bhaskar, B., and Poulos, T. L. (2003) Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida, J. Mol. Biol. 333, 377-392.
    • (2003) J. Mol. Biol. , vol.333 , pp. 377-392
    • Sevrioukova, I.F.1    Garcia, C.2    Li, H.3    Bhaskar, B.4    Poulos, T.L.5
  • 28
    • 21744459738 scopus 로고    scopus 로고
    • Redox-dependent structural differences in putidaredoxin derived from homologous structure refinement via residual dipolar couplings
    • Jain, N. U., Tjioe, E., Savidor, A., and Boulie, J. (2005) Redox-dependent structural differences in putidaredoxin derived from homologous structure refinement via residual dipolar couplings, Biochemistry 44, 9067-9078.
    • (2005) Biochemistry , vol.44 , pp. 9067-9078
    • Jain, N.U.1    Tjioe, E.2    Savidor, A.3    Boulie, J.4
  • 32
    • 14744286132 scopus 로고    scopus 로고
    • Redox-dependent structural reorganization in putidaredoxin, a vertebrate-type [2Fe-2S] ferredoxin from Pseudomonas putida
    • Sevrioukova, I. F. (2005) Redox-dependent structural reorganization in putidaredoxin, a vertebrate-type [2Fe-2S] ferredoxin from Pseudomonas putida, J. Mol. Biol. 347, 607-621.
    • (2005) J. Mol. Biol. , vol.347 , pp. 607-621
    • Sevrioukova, I.F.1
  • 33
    • 18144391863 scopus 로고    scopus 로고
    • The putidaredoxin reductase-putidaredoxin electron transfer complex: Theoretical and experimental studies
    • Kuznetsov, V. Y., Blair, E., Farmer, P. J., Poulos, T. L., Pifferitti, A., and Sevrioukova, I. F. (2005) The putidaredoxin reductase-putidaredoxin electron transfer complex: theoretical and experimental studies, J. Biol. Chem. 280, 16135-16142.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16135-16142
    • Kuznetsov, V.Y.1    Blair, E.2    Farmer, P.J.3    Poulos, T.L.4    Pifferitti, A.5    Sevrioukova, I.F.6
  • 34
    • 1042264042 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the cytochrome P450cam monooxygenase
    • Sevrioukova, I. F., Li, H., and Poulos, T. L. (2004) Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the cytochrome P450cam monooxygenase, J. Mol. Biol. 336, 889-902.
    • (2004) J. Mol. Biol. , vol.336 , pp. 889-902
    • Sevrioukova, I.F.1    Li, H.2    Poulos, T.L.3
  • 35
    • 24744459452 scopus 로고    scopus 로고
    • Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism
    • Nagano, S., and Poulos, T. L. (2005) Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism, J. Biol. Chem. 280, 31659-31663.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31659-31663
    • Nagano, S.1    Poulos, T.L.2
  • 36
    • 0017831786 scopus 로고
    • Bacterial P450cam methylene monooxygenase components: Cytochrome m, putidaredoxin, and putidaredoxin reductase
    • Gunsalus, I. C., and Wagner, G. C. (1978) Bacterial P450cam methylene monooxygenase components: cytochrome m, putidaredoxin, and putidaredoxin reductase, Methods Enzymol. 52, 166-188.
    • (1978) Methods Enzymol. , vol.52 , pp. 166-188
    • Gunsalus, I.C.1    Wagner, G.C.2
  • 37
    • 0037067760 scopus 로고    scopus 로고
    • Putidaredoxin reductase: A new function for an old protein
    • Sevrioukova, I. F., and Poulos, T. L. (2002) Putidaredoxin reductase: A new function for an old protein, J. Biol. Chem. 277, 25831-25839.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25831-25839
    • Sevrioukova, I.F.1    Poulos, T.L.2
  • 38
    • 0017886452 scopus 로고
    • -2 from equilibrium reactions with flavodoxins, methyl viologen and hydrogen plus hydrogenase
    • -2 from equilibrium reactions with flavodoxins, methyl viologen and hydrogen plus hydrogenase, Eur. J. Biochem. 85, 535-547.
    • (1978) Eur. J. Biochem. , vol.85 , pp. 535-547
    • Mayhew, S.G.1
  • 39
    • 0034691762 scopus 로고    scopus 로고
    • Temperature dependence of the formal reduction potential of putidaredoxin
    • Reipa, V., Holden, M. J., Mayhew, M. P., and Vilker, V. L. (2000) Temperature dependence of the formal reduction potential of putidaredoxin, Biochim. Biophys. Acta 1459, 1-9.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 1-9
    • Reipa, V.1    Holden, M.J.2    Mayhew, M.P.3    Vilker, V.L.4
  • 40
    • 0037180382 scopus 로고    scopus 로고
    • Molecular mechanism of the electron transfer reaction in cytochrome P450cam-putidaredoxin: Roles of glutamine 360 at the heme proximal site
    • Tosha, T., Yoshioka, S., Hori, H., Takahashi, S., Ishimori, K., and Morishima, I. (2002) Molecular mechanism of the electron transfer reaction in cytochrome P450cam-putidaredoxin: roles of glutamine 360 at the heme proximal site, Biochemistry 41, 13883-13893.
    • (2002) Biochemistry , vol.41 , pp. 13883-13893
    • Tosha, T.1    Yoshioka, S.2    Hori, H.3    Takahashi, S.4    Ishimori, K.5    Morishima, I.6
  • 41
    • 0028575449 scopus 로고
    • Hydrophobic docking - A proposed enhancement to molecular recognition techniques
    • Vakser, I. A., and Aflalo, C. (1994) Hydrophobic docking-a proposed enhancement to molecular recognition techniques, Proteins 20, 320-329.
    • (1994) Proteins , vol.20 , pp. 320-329
    • Vakser, I.A.1    Aflalo, C.2
  • 43
    • 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., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A 47, 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
  • 46
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A., and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons, Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 47
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, J. P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, J.P.1
  • 48
    • 0030815133 scopus 로고    scopus 로고
    • RASTER3D: Photorealistic molecular graphics
    • Merritt, E. A., and Bacon, D. J. (1997) RASTER3D: photorealistic molecular graphics, Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 50
    • 0024445808 scopus 로고
    • Dispersed polaron simulations of electron transfer in photosynthetic reaction centers
    • Warshel, A., Chu, Z. T., and Parson, W. W. (1989) Dispersed polaron simulations of electron transfer in photosynthetic reaction centers, Science 246, 112-116.
    • (1989) Science , vol.246 , pp. 112-116
    • Warshel, A.1    Chu, Z.T.2    Parson, W.W.3
  • 51
    • 0028360177 scopus 로고
    • Kinetic and thermodynamic analysis of a physiologic intermolecular electron-transfer reaction between methylamine dehydrogenase and amicyanin
    • Brooks, H. B., and Davidson, V. L. (1994) Kinetic and thermodynamic analysis of a physiologic intermolecular electron-transfer reaction between methylamine dehydrogenase and amicyanin, Biochemistry 33, 5696-5701.
    • (1994) Biochemistry , vol.33 , pp. 5696-5701
    • Brooks, H.B.1    Davidson, V.L.2
  • 52
    • 0038235125 scopus 로고    scopus 로고
    • Effects of viscosity and temperature on the kinetics of the electron-transfer reaction between the triplet state of zinc cytochrome c and cupriplastocyanin
    • Ivkovic-Jensen, M. M., and Kostic, N. M. (1997) Effects of viscosity and temperature on the kinetics of the electron-transfer reaction between the triplet state of zinc cytochrome c and cupriplastocyanin, Biochemistry 36, 8135-8144.
    • (1997) Biochemistry , vol.36 , pp. 8135-8144
    • Ivkovic-Jensen, M.M.1    Kostic, N.M.2
  • 53
    • 0032488605 scopus 로고    scopus 로고
    • Electron transfer in nitrogenase analyzed by Marcus theory: Evidence for gating by MgATP
    • Lanzilotta, W. N., Parker, V. D., and Seefeldt, L. C. (1998) Electron transfer in nitrogenase analyzed by Marcus theory: evidence for gating by MgATP, Biochemistry 37, 399-407.
    • (1998) Biochemistry , vol.37 , pp. 399-407
    • Lanzilotta, W.N.1    Parker, V.D.2    Seefeldt, L.C.3
  • 54
    • 0025049895 scopus 로고
    • Putidaredoxin reduction of cytochrome P450cam-Dependence of electron transfer on the identity of putidaredoxin's C-terminal amino acid
    • Davies, M. D., Qin, L., Beck, J. L., Suslick, K. S., Koga, H., Horiuchi, T., and Sligar, S. G. (1990) Putidaredoxin reduction of cytochrome P450cam-Dependence of electron transfer on the identity of putidaredoxin's C-terminal amino acid, J. Am. Chem. Soc. 112, 7396-7398.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 7396-7398
    • Davies, M.D.1    Qin, L.2    Beck, J.L.3    Suslick, K.S.4    Koga, H.5    Horiuchi, T.6    Sligar, S.G.7
  • 55
    • 0026442895 scopus 로고
    • Genetic variants in the putidaredoxin-cytochrome P450cam electron-transfer complex: Identification of the residue responsible for redox-state-dependent conformers
    • Davies, M. D., and Sligar, S. G. (1992) Genetic variants in the putidaredoxin-cytochrome P450cam electron-transfer complex: identification of the residue responsible for redox-state-dependent conformers, Biochemistry 31, 11383-11389.
    • (1992) Biochemistry , vol.31 , pp. 11383-11389
    • Davies, M.D.1    Sligar, S.G.2
  • 56
    • 0030869074 scopus 로고    scopus 로고
    • Probing the interactions of putidaredoxin with redox partners in camphor P450 5-monooxygenase by mutagenesis of surface residues
    • Holden, M., Mayhew, M., Bunk, D., Roitberg, A., and Vilker, V. (1997) Probing the interactions of putidaredoxin with redox partners in camphor P450 5-monooxygenase by mutagenesis of surface residues, J. Biol. Chem. 272, 21720-21725.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21720-21725
    • Holden, M.1    Mayhew, M.2    Bunk, D.3    Roitberg, A.4    Vilker, V.5
  • 58
    • 0016412951 scopus 로고
    • (Cooper, D. Y., Snyder, O. R., and Witmer, C., Eds.), Plemun Press, New York
    • 5 (Cooper, D. Y., Snyder, O. R., and Witmer, C., Eds.) pp 311-324, Plemun Press, New York.
    • (1975) 5 , pp. 311-324
    • Peterson, J.A.1    Mock, D.M.2
  • 59
    • 0022540099 scopus 로고
    • Single turnover studies with oxy-cytochrome P450cam
    • Brewer, C. B., and Peterson, J. A. (1986) Single turnover studies with oxy-cytochrome P450cam, Arch. Biochem. Biophys. 249, 515-521.
    • (1986) Arch. Biochem. Biophys. , vol.249 , pp. 515-521
    • Brewer, C.B.1    Peterson, J.A.2
  • 61
    • 0018653255 scopus 로고
    • Cytochrome P450cam and putidaredoxin interaction during electron transfer
    • Peterson, J. A., and Mock, D. M. (1979) Cytochrome P450cam and putidaredoxin interaction during electron transfer, Acta Biol. Med. Germ. 38, 153-162.
    • (1979) Acta Biol. Med. Germ. , vol.38 , pp. 153-162
    • Peterson, J.A.1    Mock, D.M.2
  • 62
    • 0035918265 scopus 로고    scopus 로고
    • The role of water molecules in the association of cytochrome P450cam with putidaredoxin
    • Furukawa, Y., and Morishima, I. (2001) The role of water molecules in the association of cytochrome P450cam with putidaredoxin, J. Biol. Chem. 276, 12983-12990.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12983-12990
    • Furukawa, Y.1    Morishima, I.2
  • 63
    • 0035807023 scopus 로고    scopus 로고
    • Laser flash induced electron transfer in P450cam monooxygenase: Putidaredoxin reductase-putidaredoxin interaction
    • Sevrioukova, I. F., Hazzard, J. T., Tollin, G., and Poulos, T. L. (2001) Laser flash induced electron transfer in P450cam monooxygenase: Putidaredoxin reductase-putidaredoxin interaction, Biochemistry 40, 10592-10600.
    • (2001) Biochemistry , vol.40 , pp. 10592-10600
    • Sevrioukova, I.F.1    Hazzard, J.T.2    Tollin, G.3    Poulos, T.L.4
  • 64
    • 0032575274 scopus 로고    scopus 로고
    • Roles of negatively charged surface residues of putidaredoxin in interactions with redox partners in P450cam monooxygenase system
    • Aoki, M., Ishimori, K., and Morishima, I. (1998) Roles of negatively charged surface residues of putidaredoxin in interactions with redox partners in P450cam monooxygenase system, Biochim. Biophys. Acta 1386, 157-167.
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 157-167
    • Aoki, M.1    Ishimori, K.2    Morishima, I.3
  • 65
    • 0019877147 scopus 로고
    • The kinetics of reduction of cytochrome P450cam by reduced putidaredoxin
    • Hintz, M. J., and Peterson, J. A. (1981) The kinetics of reduction of cytochrome P450cam by reduced putidaredoxin, J. Biol. Chem. 256, 6721-6728.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6721-6728
    • Hintz, M.J.1    Peterson, J.A.2
  • 66
    • 0027998799 scopus 로고
    • Significant contribution of arginine 112 and its positive charge of Pseudomonas putida cytochrome P450cam in the electron transport from putidaredoxin
    • Nakamura, K., Horiuchi, T., Yasukochi, T., Sekimizu, K., Hara, T., and Sagara, Y. (1994) Significant contribution of arginine 112 and its positive charge of Pseudomonas putida cytochrome P450cam in the electron transport from putidaredoxin, Biochim. Biophys. Acta 1207, 40-48.
    • (1994) Biochim. Biophys. Acta , vol.1207 , pp. 40-48
    • Nakamura, K.1    Horiuchi, T.2    Yasukochi, T.3    Sekimizu, K.4    Hara, T.5    Sagara, Y.6
  • 67
    • 0025907553 scopus 로고
    • Structural microheterogeneity of a tryptophan residue required for efficient biological electron transfer between putidaredoxin and cytochrome P450cam
    • Stayton, P. S., and Sligar, S. G. (1991) Structural microheterogeneity of a tryptophan residue required for efficient biological electron transfer between putidaredoxin and cytochrome P450cam, Biochemistry 30, 1845-1851.
    • (1991) Biochemistry , vol.30 , pp. 1845-1851
    • Stayton, P.S.1    Sligar, S.G.2
  • 69
    • 0033057343 scopus 로고    scopus 로고
    • Surface-modified mutants of cytochrome P450cam: Enzymatic properties and electrochemistry
    • Lo, K. K., Wong, L. L., and Hill, H. A. (1999) Surface-modified mutants of cytochrome P450cam: enzymatic properties and electrochemistry, FEBS Lett. 451, 342-346.
    • (1999) FEBS Lett. , vol.451 , pp. 342-346
    • Lo, K.K.1    Wong, L.L.2    Hill, H.A.3
  • 70
    • 0032500339 scopus 로고    scopus 로고
    • Binding and electron transfer between putidaredoxin and cytochrome P450cam-Theory and experiments
    • Roitberg, A. E., Holden, M. J., Mayhew, M. P., Kurnikov, I. V., Beratan, D. N., and Vilker, V. L. (1998) Binding and electron transfer between putidaredoxin and cytochrome P450cam-Theory and experiments, J. Am. Chem. Soc. 120, 8927-8932.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8927-8932
    • Roitberg, A.E.1    Holden, M.J.2    Mayhew, M.P.3    Kurnikov, I.V.4    Beratan, D.N.5    Vilker, V.L.6
  • 71
    • 0001127948 scopus 로고
    • A thermodynamic model of regulation: Modulation of redox equilibria in camphor monoxygenase
    • Sligar, S. G., and Gunsalus, I. C. (1976) A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase, Proc. Natl. Acad. Sci. U.S.A. 73, 1078-1082.
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 1078-1082
    • Sligar, S.G.1    Gunsalus, I.C.2
  • 72
    • 0020465726 scopus 로고
    • Equilibrium and kinetic studies of the interaction of cytochrome P450cam and putidaredoxin
    • Hintz, M. J., Mock, D. M., Peterson, L. L., Tuttle, K., and Peterson, J. A. (1982) Equilibrium and kinetic studies of the interaction of cytochrome P450cam and putidaredoxin, J. Biol. Chem. 257, 14324-14332.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14324-14332
    • Hintz, M.J.1    Mock, D.M.2    Peterson, L.L.3    Tuttle, K.4    Peterson, J.A.5
  • 73
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. C., Moser, C. C., Chen, X., and Dutton, P. L. (1999) Natural engineering principles of electron tunnelling in biological oxidation-reduction, Nature 402, 47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 75
    • 0024423650 scopus 로고
    • 15N-) complex of cytochrome P450cam. Effects of d-camphor and putidaredoxin on the iron-ligand structure
    • 15N-) complex of cytochrome P450cam. Effects of d-camphor and putidaredoxin on the iron-ligand structure, J. Am. Chem. Soc. 111, 7707-7711.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 7707-7711
    • Shiro, Y.1    Iizuka, T.2    Makino, R.3    Ishimura, Y.4    Morishima, I.5
  • 77
    • 0024468304 scopus 로고
    • 5-cytochrome P450cam association: A proposed molecular model for a cytochrome P-450cam electron-transfer complex
    • 5-cytochrome P450cam association: a proposed molecular model for a cytochrome P-450cam electron-transfer complex, Biochemistry 28, 8201-8205.
    • (1989) Biochemistry , vol.28 , pp. 8201-8205
    • Stayton, P.S.1    Poulos, T.L.2    Sligar, S.G.3
  • 78
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4. The CCP4 suite programs for protein crystallography
    • CCP4 (1994) Collaborative Computational Project Number 4. The CCP4 suite programs for protein crystallography, Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 79
    • 0022273620 scopus 로고
    • The 2.6 Å crystal structure of Pseudomonas putida cytochrome P450
    • Poulos, T. L., Finzel, B. C., Gunsalus, I. C., Wagner, G. C., and Kraut, J. (1985) The 2.6 Å crystal structure of Pseudomonas putida cytochrome P450, J. Biol. Chem. 260, 16122-30.
    • (1985) J. Biol. Chem. , vol.260 , pp. 16122-16130
    • Poulos, T.L.1    Finzel, B.C.2    Gunsalus, I.C.3    Wagner, G.C.4    Kraut, J.5


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