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Volumn 52, Issue 32, 2013, Pages 5396-5402

Synergistic effects of mutations in cytochrome P450cam designed to mimic CYP101D1

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL STATE; ELECTRON TRANSFER; ELECTROSTATIC ENVIRONMENTS; PROTON RELAYS; PUTIDAREDOXIN; REDOX PARTNERS; SYNERGISTIC EFFECT; UV-VIS SPECTROSCOPY;

EID: 84881640034     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400676d     Document Type: Article
Times cited : (17)

References (41)
  • 1
    • 84879051428 scopus 로고    scopus 로고
    • Unusual cytochrome P450 enzymes and reactions
    • Guengerich, F. P. and Munro, A. W. (2013) Unusual cytochrome P450 enzymes and reactions J. Biol. Chem. 288, 17065-17073
    • (2013) J. Biol. Chem. , vol.288 , pp. 17065-17073
    • Guengerich, F.P.1    Munro, A.W.2
  • 2
    • 0022273620 scopus 로고
    • The 2.6-Å crystal structure of Pseudomonas putida cytochrome P-450
    • 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 P-450 J. Biol. Chem. 260, 16122-16130
    • (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
  • 3
    • 27544481297 scopus 로고    scopus 로고
    • Structural biology of heme monooxygenases
    • Poulos, T. L. (2005) Structural biology of heme monooxygenases Biochem. Biophys. Res. Commun. 338, 337-345
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 337-345
    • Poulos, T.L.1
  • 4
    • 77149159443 scopus 로고    scopus 로고
    • A cytochrome P450 class i electron transfer system from Novosphingobium aromaticivorans
    • Bell, S. G., Dale, A., Rees, N. H., and Wong, L.-L. (2010) A cytochrome P450 class I electron transfer system from Novosphingobium aromaticivorans Appl. Microbiol. Biotechnol. 86, 163-175
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 163-175
    • Bell, S.G.1    Dale, A.2    Rees, N.H.3    Wong, L.-L.4
  • 5
    • 34447268241 scopus 로고    scopus 로고
    • P450 enzymes from the bacterium Novosphingobium aromaticivorans
    • Bell, S. G. and Wong, L.-L. (2007) P450 enzymes from the bacterium Novosphingobium aromaticivorans Biochem. Biophys. Res. Commun. 360, 666-672
    • (2007) Biochem. Biophys. Res. Commun. , vol.360 , pp. 666-672
    • Bell, S.G.1    Wong, L.-L.2
  • 6
    • 77956240069 scopus 로고    scopus 로고
    • Molecular characterization of a class i P450 electron transfer system from Novosphingobium aromaticivorans DSM12444
    • Yang, W., Bell, S. G., Wang, H., Zhou, W., Hoskins, N., Dale, A., Bartlam, M., Wong, L. L., and Rao, Z. (2010) Molecular characterization of a class I P450 electron transfer system from Novosphingobium aromaticivorans DSM12444 J. Biol. Chem. 285, 27372-27384
    • (2010) J. Biol. Chem. , vol.285 , pp. 27372-27384
    • Yang, W.1    Bell, S.G.2    Wang, H.3    Zhou, W.4    Hoskins, N.5    Dale, A.6    Bartlam, M.7    Wong, L.L.8    Rao, Z.9
  • 7
    • 84878747590 scopus 로고    scopus 로고
    • Structural basis for effector control and redox partner recognition in cytochrome P450
    • Tripathi, S., Li, H., and Poulos, T. L. (2013) Structural basis for effector control and redox partner recognition in cytochrome P450 Science 340, 1227-1230
    • (2013) Science , vol.340 , pp. 1227-1230
    • Tripathi, S.1    Li, H.2    Poulos, T.L.3
  • 8
    • 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
  • 9
    • 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
  • 10
    • 0017295461 scopus 로고
    • Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam
    • Lipscomb, J. D., Sligar, S. G., Namtvedt, M. J., and Gunsalus, I. C. (1976) Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam 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
  • 11
    • 0027994378 scopus 로고
    • A role for Asp-251 in cytochrome P-450cam oxygen activation
    • Gerber, N. C. and Sligar, S. G. (1994) A role for Asp-251 in cytochrome P-450cam oxygen activation J. Biol. Chem. 269, 4260-4266
    • (1994) J. Biol. Chem. , vol.269 , pp. 4260-4266
    • Gerber, N.C.1    Sligar, S.G.2
  • 12
    • 27544491232 scopus 로고
    • Catalytic mechanism of cytrochrome P450 - Evidence for a distal charge relay system
    • Gerber, N. S. and Sligar, S. G. (1992) Catalytic mechanism of cytrochrome P450-evidence for a distal charge relay system J. Am. Chem. Soc. 174, 725-735
    • (1992) J. Am. Chem. Soc. , vol.174 , pp. 725-735
    • Gerber, N.S.1    Sligar, S.G.2
  • 13
    • 0030917740 scopus 로고    scopus 로고
    • Exceptionally stable salt bridges in cytochrome P450cam have functional roles
    • Lounnas, V. and Wade, R. C. (1997) Exceptionally stable salt bridges in cytochrome P450cam have functional roles Biochemistry 36, 5402-5417
    • (1997) Biochemistry , vol.36 , pp. 5402-5417
    • Lounnas, V.1    Wade, R.C.2
  • 14
    • 0141869098 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida
    • Sevrioukova, I., Gracia, 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.1    Gracia, C.2    Li, H.3    Bhaskar, B.4    Poulos, T.L.5
  • 15
    • 1042264042 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the P450cam monooxygenase system
    • Sevrioukova, I., Li, H., and Poulos, T. L. (2004) Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the P450cam monooxygenase system J. Mol. Biol. 236, 889-902
    • (2004) J. Mol. Biol. , vol.236 , pp. 889-902
    • Sevrioukova, I.1    Li, H.2    Poulos, T.L.3
  • 16
    • 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
  • 17
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura, T. and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature J. Biol. Chem. 239, 2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 18
    • 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
  • 19
    • 0017831786 scopus 로고
    • Bacterial P-450cam methylene monooxygenase components: Cytochrome m, putidaredoxin, and putidaredoxin reductase
    • Gunsalus, I. C. and Wagner, G. C. (1978) Bacterial P-450cam 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
  • 20
    • 0035807023 scopus 로고    scopus 로고
    • Laser flash induced electron transfer in P450cam monoxygenase: Putidaredoxin reductase-putidaredoxin interaction
    • Sevrioukova, I., Hazzard, J. T., Tollin, G., and Poulos, T. L. (2001) Laser flash induced electron transfer in P450cam monoxygenase: putidaredoxin reductase-putidaredoxin interaction Biochemistry 40, 10592-10600
    • (2001) Biochemistry , vol.40 , pp. 10592-10600
    • Sevrioukova, I.1    Hazzard, J.T.2    Tollin, G.3    Poulos, T.L.4
  • 21
    • 73449112665 scopus 로고    scopus 로고
    • Production and characterization of a functional putidaredoxin reductase-putidaredoxin covalent complex
    • Churbanova, I. Y., Poulos, T. L., and Sevrioukova, I. F. (2010) Production and characterization of a functional putidaredoxin reductase-putidaredoxin covalent complex Biochemistry 49, 58-67
    • (2010) Biochemistry , vol.49 , pp. 58-67
    • Churbanova, I.Y.1    Poulos, T.L.2    Sevrioukova, I.F.3
  • 22
    • 33749333744 scopus 로고    scopus 로고
    • Putidaredoxin-to-cytochrome P450cam electron transfer: Differences between the two reductive steps required for catalysis
    • Kuznetsov, V. Y., Poulos, T. L., and Sevrioukova, I. F. (2006) Putidaredoxin-to-cytochrome P450cam electron transfer: differences between the two reductive steps required for catalysis Biochemistry 45, 11934-11944
    • (2006) Biochemistry , vol.45 , pp. 11934-11944
    • Kuznetsov, V.Y.1    Poulos, T.L.2    Sevrioukova, I.F.3
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Macromol. Crystallogr., A 276, 307-326
    • (1997) Macromol. Crystallogr., A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 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
  • 30
    • 0037229513 scopus 로고    scopus 로고
    • Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes
    • Fedorov, R., Ghosh, D. K., and Schlichting, I. (2003) Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes Arch. Biochem. Biophys. 409, 25-31
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 25-31
    • Fedorov, R.1    Ghosh, D.K.2    Schlichting, I.3
  • 31
    • 0017170343 scopus 로고
    • Coupling of spin, substrate, and redox equilibria in cytochrome P450
    • Sligar, S. G. (1976) Coupling of spin, substrate, and redox equilibria in cytochrome P450 Biochemistry 15, 5399-5406
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 32
    • 0025264366 scopus 로고
    • Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation
    • Di Primo, C., Hui Bon Hoa, G., Douzou, P., and Sligar, S. (1990) Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation J. Biol. Chem. 265, 5361-5363
    • (1990) J. Biol. Chem. , vol.265 , pp. 5361-5363
    • Di Primo, C.1    Hui Bon Hoa, G.2    Douzou, P.3    Sligar, S.4
  • 33
    • 0033230093 scopus 로고    scopus 로고
    • Mutations of glutamate-84 at the putative potassium-binding site affect camphor binding and oxidation by cytochrome p450cam
    • Westlake, A. C., Harford-Cross, C. F., Donovan, J., and Wong, L. L. (1999) Mutations of glutamate-84 at the putative potassium-binding site affect camphor binding and oxidation by cytochrome p450cam Eur. J. Biochem. 265, 929-935
    • (1999) Eur. J. Biochem. , vol.265 , pp. 929-935
    • Westlake, A.C.1    Harford-Cross, C.F.2    Donovan, J.3    Wong, L.L.4
  • 34
    • 0037145071 scopus 로고    scopus 로고
    • Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin
    • Deprez, E., Gill, E., Helms, V., Wade, R. C., and Hui Bon Hoa, G. (2002) Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin J. Inorg. Biochem. 91, 597-606
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 597-606
    • Deprez, E.1    Gill, E.2    Helms, V.3    Wade, R.C.4    Hui Bon Hoa, G.5
  • 35
    • 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
  • 36
    • 0032581042 scopus 로고    scopus 로고
    • Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect
    • Vidakovic, M., Sligar, S. G., Li, H., and Poulos, T. L. (1998) Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect Biochemistry 37, 9211-9219
    • (1998) Biochemistry , vol.37 , pp. 9211-9219
    • Vidakovic, M.1    Sligar, S.G.2    Li, H.3    Poulos, T.L.4
  • 37
    • 20444491589 scopus 로고    scopus 로고
    • Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T - Investigation of the proton transfer system in P450eryF
    • Nagano, S., Cupp-Vickery, J. R., and Poulos, T. L. (2005) Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T-investigation of the proton transfer system in P450eryF J. Biol. Chem. 280, 22102-22107
    • (2005) J. Biol. Chem. , vol.280 , pp. 22102-22107
    • Nagano, S.1    Cupp-Vickery, J.R.2    Poulos, T.L.3
  • 38
    • 33845954248 scopus 로고    scopus 로고
    • 2 activation by cytochrome P450cam studied by isotope effects and transient state kinetics
    • 2 activation by cytochrome P450cam studied by isotope effects and transient state kinetics Biochemistry 45, 15793-15806
    • (2006) Biochemistry , vol.45 , pp. 15793-15806
    • Purdy, M.M.1    Koo, L.S.2    De Montellano, P.R.3    Klinman, J.P.4
  • 39
    • 37049036930 scopus 로고    scopus 로고
    • Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry
    • Makris, T. M., von Koenig, K., Schlichting, I., and Sligar, S. G. (2007) Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry Biochemistry 46, 14129-14140
    • (2007) Biochemistry , vol.46 , pp. 14129-14140
    • Makris, T.M.1    Von Koenig, K.2    Schlichting, I.3    Sligar, S.G.4
  • 40
    • 77951247090 scopus 로고    scopus 로고
    • P450cam visits an open conformation in the absence of substrate
    • Lee, Y. T., Wilson, R. F., Rupniewski, I., and Goodin, D. B. (2010) P450cam visits an open conformation in the absence of substrate Biochemistry 49, 3412-3419
    • (2010) Biochemistry , vol.49 , pp. 3412-3419
    • Lee, Y.T.1    Wilson, R.F.2    Rupniewski, I.3    Goodin, D.B.4
  • 41
    • 79952092257 scopus 로고    scopus 로고
    • Three clusters of conformational states in p450cam reveal a multistep pathway for closing of the substrate access channel
    • Lee, Y. T., Glazer, E. C., Wilson, R. F., Stout, C. D., and Goodin, D. B. (2011) Three clusters of conformational states in p450cam reveal a multistep pathway for closing of the substrate access channel Biochemistry 50, 693-703
    • (2011) Biochemistry , vol.50 , pp. 693
    • Lee, Y.T.1    Glazer, E.C.2    Wilson, R.F.3    Stout, C.D.4    Goodin, D.B.5


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