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Volumn 45, Issue 26, 2006, Pages 7949-7958

Electrostatic environment of hemes in proteins: pKas of hydroxyl ligands

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; ELECTROCHEMISTRY; ELECTROSTATICS; HEMOGLOBIN; MOLECULAR STRUCTURE; PERMITTIVITY; STOICHIOMETRY;

EID: 33745622986     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052182l     Document Type: Article
Times cited : (29)

References (89)
  • 1
    • 1542274547 scopus 로고    scopus 로고
    • Heme protein assemblies
    • Reedy, C. J., and Gibney, B. R. (2004) Heme protein assemblies, Chem. Rev. 104, 617-649.
    • (2004) Chem. Rev. , vol.104 , pp. 617-649
    • Reedy, C.J.1    Gibney, B.R.2
  • 3
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase. Characterization of the enzyme
    • Tenhunen, R., Marver, H. S., and Schmid, R. (1969) Microsomal heme oxygenase. Characterization of the enzyme, J. Biol. Chem. 244, 6388-6394.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 4
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder, K. G. (1992) Superfamily of plant, fungal and bacterial peroxidases, Curr. Opin. Struct. Biol. 2, 338-393.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 338-393
    • Welinder, K.G.1
  • 5
    • 0032042908 scopus 로고    scopus 로고
    • Substrate binding and catalysis in heme peroxidases
    • Smith, A. T., and Veitch, N. C. (1998) Substrate binding and catalysis in heme peroxidases, Curr. Opin. Chem. Biol. 2, 269-278.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 269-278
    • Smith, A.T.1    Veitch, N.C.2
  • 6
    • 3242763877 scopus 로고    scopus 로고
    • Redox-driven membrane-bound proton pumps
    • Brzezinski, P. (2004) Redox-driven membrane-bound proton pumps, Trends Biochem. Sci. 29, 380-387.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 380-387
    • Brzezinski, P.1
  • 7
    • 0242657394 scopus 로고    scopus 로고
    • Some recent contributions of FTIR difference spectroscopy to the study of cytochrome oxidas
    • Genius, R. B. (2003) Some recent contributions of FTIR difference spectroscopy to the study of cytochrome oxidas, FEBS Lett. 555, 2-7.
    • (2003) FEBS Lett. , vol.555 , pp. 2-7
    • Genius, R.B.1
  • 8
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • Ferguson-Miller, S., and Babcock, G. T. (1996) Heme/copper terminal oxidases, Chem. Rev. 96, 2889-2907.
    • (1996) Chem. Rev. , vol.96 , pp. 2889-2907
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 9
    • 1942472486 scopus 로고    scopus 로고
    • Cytochrome c oxidase: 25 Years of the elusive proton pump
    • Wikstrom, M. (2004) Cytochrome c oxidase: 25 years of the elusive proton pump, Biochim. Biophys. Acta 1655, 241-247.
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 241-247
    • Wikstrom, M.1
  • 10
    • 0034684238 scopus 로고    scopus 로고
    • Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods
    • Montfort, W. R., Weichsel, A., and Andersen, J. F. (2000) Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods, Biochim. Biophys. Acta 1482, 110-118.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 110-118
    • Montfort, W.R.1    Weichsel, A.2    Andersen, J.F.3
  • 11
    • 0343807261 scopus 로고
    • Regulation of intramitochondrial cholesterol transfer to side-chain cleavage cytochrome P-450 in rat adrenal gland
    • Priyalle, C. T., Crivello, J. F., and Jefcoate, C. R. (1983) Regulation of intramitochondrial cholesterol transfer to side-chain cleavage cytochrome P-450 in rat adrenal gland, Proc. Natl. Acad. Sci. U.S.A. 80, 702-706.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 702-706
    • Priyalle, C.T.1    Crivello, J.F.2    Jefcoate, C.R.3
  • 12
    • 0033070951 scopus 로고    scopus 로고
    • Cytochromes P450 in synthesis of steroid hormones, bile acids, vitamin D3 and cholesterol
    • Pikuleva, I., and Waterman, M. (1999) Cytochromes P450 in synthesis of steroid hormones, bile acids, vitamin D3 and cholesterol, Mol. Aspects Med. 20, 33-42, 43-37.
    • (1999) Mol. Aspects Med. , vol.20 , pp. 33-42
    • Pikuleva, I.1    Waterman, M.2
  • 13
    • 0033120934 scopus 로고    scopus 로고
    • Heme-based sensors in biological systems
    • Rodgers, K. R. (1999) Heme-based sensors in biological systems, Curr. Opin. Chem: Biol. 3, 158-167.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 158-167
    • Rodgers, K.R.1
  • 14
    • 0035313335 scopus 로고    scopus 로고
    • Recent advances in heme-protein sensors
    • Chan, M. K. (2001) Recent advances in heme-protein sensors, Curr. Opin. Struct. Biol. 5, 216-222.
    • (2001) Curr. Opin. Struct. Biol. , vol.5 , pp. 216-222
    • Chan, M.K.1
  • 15
    • 0023044641 scopus 로고
    • Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins
    • Churg, A. K., and Warshel, A. (1986) Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins, Biochemistry 25, 1675-1681.
    • (1986) Biochemistry , vol.25 , pp. 1675-1681
    • Churg, A.K.1    Warshel, A.2
  • 17
    • 0346447734 scopus 로고    scopus 로고
    • The role of the axial ligand in heme-based catalysis
    • Rietjens, I. (1996) The role of the axial ligand in heme-based catalysis, J. Biol. Inorg. Chem. 1, 355.
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 355
    • Rietjens, I.1
  • 19
    • 0018129356 scopus 로고
    • Haem exposure as the determinate of oxidation-reduction potential of haem proteins
    • Stellwagen, E. (1978) Haem exposure as the determinate of oxidation-reduction potential of haem proteins, Nature 275, 73-74.
    • (1978) Nature , vol.275 , pp. 73-74
    • Stellwagen, E.1
  • 20
    • 0041972670 scopus 로고    scopus 로고
    • How cytochromes with different folds control heme redox potentials
    • Mao, J., Hauser, K., and Gunner, M. R. (2003) How cytochromes with different folds control heme redox potentials, Biochemistry 42, 9829-9840.
    • (2003) Biochemistry , vol.42 , pp. 9829-9840
    • Mao, J.1    Hauser, K.2    Gunner, M.R.3
  • 21
    • 0025944990 scopus 로고
    • Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center
    • Gunner, M. R., and Honig, B. (1991) Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center, Proc. Natl. Acad. Sci. U.S.A. 88, 9151-9155.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9151-9155
    • Gunner, M.R.1    Honig, B.2
  • 22
    • 0346101799 scopus 로고    scopus 로고
    • Tuning heme redox potentials in the cytochrome c subunit of photosynthetic reaction centers
    • Voigt, P., and Knapp, E. W. (2003) Tuning heme redox potentials in the cytochrome c subunit of photosynthetic reaction centers, J. Biol. Chem. 278, 51993-52001.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51993-52001
    • Voigt, P.1    Knapp, E.W.2
  • 23
    • 0015928945 scopus 로고
    • A theoretical model for the effects of local nonpolar heme environments on the redox potentials in cytochromes
    • Kassner, R. J. (1973) A theoretical model for the effects of local nonpolar heme environments on the redox potentials in cytochromes, J. Am. Chem. Soc. 95, 7959-7975.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 7959-7975
    • Kassner, R.J.1
  • 24
    • 0015385789 scopus 로고
    • Effects of nonpolar environments on the redox potentials of heme complexes
    • Kassner, R. J. (1972) Effects of nonpolar environments on the redox potentials of heme complexes, Proc. Natl. Acad. Sci. U.S.A. 69, 2263-2267.
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 2263-2267
    • Kassner, R.J.1
  • 25
    • 18144394277 scopus 로고    scopus 로고
    • Are acidic and basic groups in buried proteins predicted to be ionized?
    • Kim, J., Mao, J., and Gunner, M. R. (2005) Are acidic and basic groups in buried proteins predicted to be ionized?, J. Mol. Biol. 348, 1283-1298.
    • (2005) J. Mol. Biol. , vol.348 , pp. 1283-1298
    • Kim, J.1    Mao, J.2    Gunner, M.R.3
  • 27
    • 0001539904 scopus 로고
    • On the action of cytochrome c: Correlating geometry changes upon oxidation with activation energies of electron transfer
    • Churg, A. K., Weiss, R. M., Warshel, A., and Takano, T. (1983) On the action of cytochrome c: correlating geometry changes upon oxidation with activation energies of electron transfer, J. Phys. Chem. 87, 1683-1694.
    • (1983) J. Phys. Chem. , vol.87 , pp. 1683-1694
    • Churg, A.K.1    Weiss, R.M.2    Warshel, A.3    Takano, T.4
  • 29
    • 0020475509 scopus 로고
    • Calculation of the electric potential in the active site cleft due to a α-helix dipoles
    • Warwicker, J., and Watson, H. C. (1982) Calculation of the electric potential in the active site cleft due to a α-helix dipoles, J. Mol. Biol. 157, 671-679.
    • (1982) J. Mol. Biol. , vol.157 , pp. 671-679
    • Warwicker, J.1    Watson, H.C.2
  • 30
    • 0034640465 scopus 로고    scopus 로고
    • A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins
    • Gunner, M. R., and Alexov, E. (2000) A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins, Biochim. Biophys. Acta 1458, 63-87.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 63-87
    • Gunner, M.R.1    Alexov, E.2
  • 31
    • 0030996290 scopus 로고    scopus 로고
    • Control of reduction potential by protein matrix: Lesson from a spherical protein model
    • Zhou, H. X. (1997) Control of reduction potential by protein matrix: lesson from a spherical protein model, J. Biol. Inorg. Chem. 2, 109-113.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 109-113
    • Zhou, H.X.1
  • 32
    • 0030890485 scopus 로고    scopus 로고
    • Microscopic and semimacroscopic redox calculations: What can and can not be learned from continuum models
    • Warshel, A., Papazyan, A., and Muegge, I. (1997) Microscopic and semimacroscopic redox calculations: what can and can not be learned from continuum models, J. Biol. Inorg. Chem. 2, 143-152.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 143-152
    • Warshel, A.1    Papazyan, A.2    Muegge, I.3
  • 33
    • 0030970305 scopus 로고    scopus 로고
    • Simulation of protein conformational freedom as a function of pH: Constant-pH molecular dynamics using implicit titration
    • Baptista, A. M., Martel, P. J., and Peterson, S. B. (1997) Simulation of protein conformational freedom as a function of pH: constant-pH molecular dynamics using implicit titration, Proteins: Struct., Funct., Genet. 27, 523-544.
    • (1997) Proteins: Struct., Funct., Genet. , vol.27 , pp. 523-544
    • Baptista, A.M.1    Martel, P.J.2    Peterson, S.B.3
  • 37
    • 0035800031 scopus 로고    scopus 로고
    • Factors determining the orientation of axially coordinated imidazoles in heme proteins
    • Zaric, S. D., Popovic, D. M., and Knapp, E. W. (2001) Factors determining the orientation of axially coordinated imidazoles in heme proteins, Biochemistry 40, 7914-7928.
    • (2001) Biochemistry , vol.40 , pp. 7914-7928
    • Zaric, S.D.1    Popovic, D.M.2    Knapp, E.W.3
  • 38
    • 10044230751 scopus 로고    scopus 로고
    • Calculated coupling of transmembrane electron and proton transfer in dihemic quinol: Fumarate reductase
    • Haas, A. H., and Lancaster, C. R. (2004) Calculated coupling of transmembrane electron and proton transfer in dihemic quinol: fumarate reductase, Biophys. J. 87, 4298-4315.
    • (2004) Biophys. J. , vol.87 , pp. 4298-4315
    • Haas, A.H.1    Lancaster, C.R.2
  • 40
    • 0024281204 scopus 로고
    • On the energetics of conformational changes and pH dependent redox behaviour of electron transfer proteins
    • Rogers, N. K., and Moore, G. R. (1988) On the energetics of conformational changes and pH dependent redox behaviour of electron transfer proteins, FEBS Lett. 228, 69-73.
    • (1988) FEBS Lett. , vol.228 , pp. 69-73
    • Rogers, N.K.1    Moore, G.R.2
  • 41
    • 0031880698 scopus 로고    scopus 로고
    • The coupling of electron transfer and proton translocation: Electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase
    • Kannt, A., Lancaster, C. R. D., and Michel, H. (1998) The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase, Biophys. J. 74, 708-721.
    • (1998) Biophys. J. , vol.74 , pp. 708-721
    • Kannt, A.1    Lancaster, C.R.D.2    Michel, H.3
  • 42
    • 1242314254 scopus 로고    scopus 로고
    • Electrostatic study of the proton pumping mechanism in bovine heart cytochrome c oxidase
    • Popovic, D. M., and Stuchebrukhov, A. A. (2004) Electrostatic study of the proton pumping mechanism in bovine heart cytochrome c oxidase, J. Am. Chem. Soc. 126, 1858-1871.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1858-1871
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 43
    • 33745605230 scopus 로고    scopus 로고
    • Calculated proton uptake on anaerobic reduction of cytochrome c oxidase: Is the reaction electroneutral?
    • Song, Y., Michonova-Alexova, E., and Gunner, M. R. (2006) Calculated proton uptake on anaerobic reduction of cytochrome c oxidase: Is the reaction electroneutral?, Biochemistry 45, XXXX-XXXX.
    • (2006) Biochemistry , vol.45
    • Song, Y.1    Michonova-Alexova, E.2    Gunner, M.R.3
  • 44
    • 0037496170 scopus 로고    scopus 로고
    • The catalytic cycle of tyrosinase: Peroxide attack on the phenolate ring followed by O-O cleavage
    • Siegbahn, P. E. (2003) The catalytic cycle of tyrosinase: peroxide attack on the phenolate ring followed by O-O cleavage, J. Biol. Inorg. Chem. 8, 567-576.
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 567-576
    • Siegbahn, P.E.1
  • 45
    • 0032556227 scopus 로고    scopus 로고
    • Role of the axial ligand in determining the spin state of resting cytochrome P450
    • Green, M. T. (1998) Role of the axial ligand in determining the spin state of resting cytochrome P450, J. Am. Chem. Soc. 120, 10772-10773.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10772-10773
    • Green, M.T.1
  • 46
    • 3142761726 scopus 로고    scopus 로고
    • Cytochrome P450CAM enzymatic catalysis cycle: A quantum mechanics/molecular mechanics study
    • Guallar, V., and Friesner, R. A. (2004) Cytochrome P450CAM enzymatic catalysis cycle: a quantum mechanics/molecular mechanics study, J. Am. Chem. Soc. 126, 8501-8508.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8501-8508
    • Guallar, V.1    Friesner, R.A.2
  • 48
    • 0034692380 scopus 로고    scopus 로고
    • A model "rebound" mechanism of hydroxylation by cytochrome P450: Stepwise and effectively conderted pathways and their reactivity patterns
    • Ogliaro, F., Harris, N., Cohen, S., Filatov, M., deVisser, D. P., and Shaik, S. (2000) A model "rebound" mechanism of hydroxylation by cytochrome P450: Stepwise and effectively conderted pathways and their reactivity patterns, J. Am. Chem. Soc. 122, 8977-8989.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8977-8989
    • Ogliaro, F.1    Harris, N.2    Cohen, S.3    Filatov, M.4    DeVisser, D.P.5    Shaik, S.6
  • 49
    • 84962377244 scopus 로고    scopus 로고
    • A theoretical study on the mechanism of camphor hydroxylation by compound I of cytochrome P450
    • Kamachi, T., and Yoshizawa, K. (2003) A theoretical study on the mechanism of camphor hydroxylation by compound I of cytochrome P450, J. Am. Chem. Soc. 125, 4652-4661.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4652-4661
    • Kamachi, T.1    Yoshizawa, K.2
  • 50
    • 0038472409 scopus 로고    scopus 로고
    • Peripheral heme substituents control the hydrogen-atom abstraction chemistry in cytochromes P450
    • Guallar, V., Baik, M. H., Lippard, S. J., and Friesner, R. A. (2003) Peripheral heme substituents control the hydrogen-atom abstraction chemistry in cytochromes P450, Proc. Natl. Acad. Sci. U.S.A. 100, 6998-7002.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6998-7002
    • Guallar, V.1    Baik, M.H.2    Lippard, S.J.3    Friesner, R.A.4
  • 51
    • 12144287949 scopus 로고    scopus 로고
    • Quantum mechanical/molecular mechanical investigation of the mechanism of C-H hydroxylation of camphor by cytochrome P450cam: Theory supports a two-state rebound mechanism
    • Schoneboom, J. C., Cohen, S., Lin, H., Shaik, S., and Thiel, W. (2004) Quantum mechanical/molecular mechanical investigation of the mechanism of C-H hydroxylation of camphor by cytochrome P450cam: theory supports a two-state rebound mechanism, J. Am. Chem. Soc. 126, 4017-4034.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4017-4034
    • Schoneboom, J.C.1    Cohen, S.2    Lin, H.3    Shaik, S.4    Thiel, W.5
  • 53
    • 18844479874 scopus 로고    scopus 로고
    • Water-hydroxide exchange reactions at the catalytic site of heme-copper oxidases
    • Branden, M., Namslauer, A., Hansson, O., Aasa, R., and Brzezinski, P. (2003) Water-hydroxide exchange reactions at the catalytic site of heme-copper oxidases, Biochemistry 42, 13178-13184.
    • (2003) Biochemistry , vol.42 , pp. 13178-13184
    • Branden, M.1    Namslauer, A.2    Hansson, O.3    Aasa, R.4    Brzezinski, P.5
  • 55
    • 0030945495 scopus 로고    scopus 로고
    • Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties
    • Alexov, E. G., and Gunner, M. R. (1997) Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties, Biophys. J. 72, 2075-2093.
    • (1997) Biophys. J. , vol.72 , pp. 2075-2093
    • Alexov, E.G.1    Gunner, M.R.2
  • 57
    • 33749189483 scopus 로고    scopus 로고
    • Factors influencing energetics of electron and proton transfers in proteins. What can be learned from calculations
    • in press
    • Gunner, M. R., Mao, J., Song, Y., and Kim, J. (2006) Factors influencing energetics of electron and proton transfers in proteins. What can be learned from calculations, Biochim. Biophys. Acta (in press).
    • (2006) Biochim. Biophys. Acta
    • Gunner, M.R.1    Mao, J.2    Song, Y.3    Kim, J.4
  • 58
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls, A., and Honig, B. (1991) A rapid finite difference algorithm utilizing successive over-relaxation to solve the Poisson-Boltzmann equation, J. Comput. Chem. 12, 435-445.
    • (1991) J. Comput. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2
  • 59
    • 84986452939 scopus 로고
    • The fast multipole boundary element method for molecular electrostatics: An optimal approach for large systems
    • Bharadwaj, R., Windemuth, A., Sridharan, S., Honig, B., and Nicholls, A. (1995) The fast multipole boundary element method for molecular electrostatics: An optimal approach for large systems, J. Comput. Chem. 16, 898-913.
    • (1995) J. Comput. Chem. , vol.16 , pp. 898-913
    • Bharadwaj, R.1    Windemuth, A.2    Sridharan, S.3    Honig, B.4    Nicholls, A.5
  • 60
    • 0035913537 scopus 로고    scopus 로고
    • Extending the applicability of the nonlinear Poisson-Boltzmann equation: Multiple dielectric constants and multivalent ions
    • Rocchia, W., Alexov, E., and Honig, B. (2001) Extending the applicability of the nonlinear Poisson-Boltzmann equation: multiple dielectric constants and multivalent ions, J. Phys. Chem. B 105, 6507-6514.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6507-6514
    • Rocchia, W.1    Alexov, E.2    Honig, B.3
  • 61
    • 0023779259 scopus 로고
    • Calculation of the total electrostatic energy of a macromolecular system: Solvation energies, binding energies, and conformational analysis
    • Gilson, M. K., and Honig, B. (1988) Calculation of the total electrostatic energy of a macromolecular system: solvation energies, binding energies, and conformational analysis, Proteins: Struct., Funct., Genet. 4, 7-18.
    • (1988) Proteins: Struct., Funct., Genet. , vol.4 , pp. 7-18
    • Gilson, M.K.1    Honig, B.2
  • 62
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • Sitkoff, D., Sharp, K. A., and Honig, B. (1994) Accurate calculation of hydration free energies using macroscopic solvent models, J. Phys. Chem. 98, 1978-1988.
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 63
    • 0041471589 scopus 로고    scopus 로고
    • Calculation of proton transfers in bacteriorhodopsin bR and M intermediates
    • Song, Y., Mao, J., and Gunner, M. R. (2003) Calculation of proton transfers in bacteriorhodopsin bR and M intermediates, Biochemistry 42, 9875-9888.
    • (2003) Biochemistry , vol.42 , pp. 9875-9888
    • Song, Y.1    Mao, J.2    Gunner, M.R.3
  • 66
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. 3. The role of exact exchange
    • Becke, A. D. (1993) Density-Functional Thermochemistry. 3. The role of exact exchange, J. Chem. Phys. 98, 5648-5652.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 68
    • 0018118592 scopus 로고
    • Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • Richarz, R., and Wüthrich, K. (1975) Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH, Biopolymers 17, 2133-2141.
    • (1975) Biopolymers , vol.17 , pp. 2133-2141
    • Richarz, R.1    Wüthrich, K.2
  • 70
    • 0001645795 scopus 로고    scopus 로고
    • Heme-peptide models for hemoproteins. 1. Solution chemistry of N-acetylmicroperoxidase-8
    • Munro, O. Q., and Marques, H. M. (1996) Heme-peptide models for hemoproteins. 1. solution chemistry of N-acetylmicroperoxidase-8, Inorg. Chem. 35, 3752-3767.
    • (1996) Inorg. Chem. , vol.35 , pp. 3752-3767
    • Munro, O.Q.1    Marques, H.M.2
  • 72
    • 0002270409 scopus 로고    scopus 로고
    • Coordination of weak field ligands by N-acetylmicroperoxidase-8 (NAcMPS), a ferric haempeptide from cytochrome c, and the influence of the axial ligand on the reduction potential of complexes of NAcMPS
    • Marques, H. M., Cukrowski, I., and Vashi, P. R. (2000) Coordination of weak field ligands by N-acetylmicroperoxidase-8 (NAcMPS), a ferric haempeptide from cytochrome c, and the influence of the axial ligand on the reduction potential of complexes of NAcMPS, J. Chem. Soc. 2000, 1335-1342.
    • (2000) J. Chem. Soc. , vol.2000 , pp. 1335-1342
    • Marques, H.M.1    Cukrowski, I.2    Vashi, P.R.3
  • 73
    • 33845278074 scopus 로고
    • Direct electrochemistry of the undacapeptide from cytochrome c (microperoxidase) at a glassy carbon electrode
    • Santucci, R., Reinhard, H., and Brunori, M. (1988) Direct electrochemistry of the undacapeptide from cytochrome c (microperoxidase) at a glassy carbon electrode, J. Am. Chem. Soc. 110, 8536-8357.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8536-18357
    • Santucci, R.1    Reinhard, H.2    Brunori, M.3
  • 74
    • 0001354839 scopus 로고
    • Reductive alteration of heme a hemochromes
    • Vanderkooi, G., and Stotz, E. (1965) Reductive alteration of heme a hemochromes, J. Biol. Chem. 240, 3418-3424.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3418-3424
    • Vanderkooi, G.1    Stotz, E.2
  • 75
    • 0014027839 scopus 로고
    • Oxidation-reduction potentials of heme a hemochromes
    • Vanderkooi, G., and Stotz, E. (1966) Oxidation-reduction potentials of heme a hemochromes, J. Biol. Chem. 241, 3316-3323.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3316-3323
    • Vanderkooi, G.1    Stotz, E.2
  • 76
    • 0026095641 scopus 로고
    • Protonation of interacting residues in a protein by a Monte Carlo method: Application to Lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides
    • Beroza, P., Fredkin, D. R., Okamura, M. Y., and Feher, G. (1991) Protonation of interacting residues in a protein by a Monte Carlo method: application to Lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides, Proc. Natl. Acad. Sci. U.S.A. 88, 5804-5808.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 5804-5808
    • Beroza, P.1    Fredkin, D.R.2    Okamura, M.Y.3    Feher, G.4
  • 77
    • 11844302809 scopus 로고    scopus 로고
    • Energetics of quinone-dependent electron and proton transfers in Rhodobacter sphaeroides photosynthetic reaction centers
    • Zhu, Z., and Gunner, M. R. (2005) Energetics of quinone-dependent electron and proton transfers in Rhodobacter sphaeroides photosynthetic reaction centers, Biochemistry 44, 82-96.
    • (2005) Biochemistry , vol.44 , pp. 82-96
    • Zhu, Z.1    Gunner, M.R.2
  • 78
    • 33745770836 scopus 로고
    • Ab initio effective core potentials for molecular calculations. Potentials for the transition metal atoms Sc to Hg
    • Hay, P. J., and Wadt, W. R. (1985) Ab initio effective core potentials for molecular calculations. Potentials for the transition metal atoms Sc to Hg, J. Chem. Phys. 82, 270-283.
    • (1985) J. Chem. Phys. , vol.82 , pp. 270-283
    • Hay, P.J.1    Wadt, W.R.2
  • 79
    • 0023806074 scopus 로고
    • Resonance Raman spectroscopic evidence for heme iron-hydroxide ligation in peroxidase alkaline forms
    • Sitter, A. J., Shifflett, J. R., and Terner, J. (1988) Resonance Raman spectroscopic evidence for heme iron-hydroxide ligation in peroxidase alkaline forms, J. Biol. Chem. 263, 13032-13038.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13032-13038
    • Sitter, A.J.1    Shifflett, J.R.2    Terner, J.3
  • 80
    • 0015239511 scopus 로고
    • The effects of protein conformation on the heme symmetry in high spin ferric heme proteins as studied by electron paramagnetic resonance
    • Peisach, J., Blumberg, W. E., Ogawa, S., Rachmilewitz, E. A., and Oltzik, R. (1971) The effects of protein conformation on the heme symmetry in high spin ferric heme proteins as studied by electron paramagnetic resonance, J. Biol. Chem. 246, 3342-3355.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3342-3355
    • Peisach, J.1    Blumberg, W.E.2    Ogawa, S.3    Rachmilewitz, E.A.4    Oltzik, R.5
  • 81
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B., and Nicholls, A. (1995) Classical electrostatics in biology and chemistry, Science 268, 1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 82
    • 0034091669 scopus 로고    scopus 로고
    • Backbone dipoles generate positive potentials in all proteins: Origins and implications of the effect
    • Gunner, M. R., Salen, M. A., Cross, E., ud-Doula, A., and Wise, M. (2000) Backbone dipoles generate positive potentials in all proteins: origins and implications of the effect, Biophys. J. 78, 1126-1144.
    • (2000) Biophys. J. , vol.78 , pp. 1126-1144
    • Gunner, M.R.1    Salen, M.A.2    Cross, E.3    Ud-Doula, A.4    Wise, M.5
  • 83
    • 0025167226 scopus 로고
    • Hemoglobins of the Lucina pectinata/bacteria symbiosis. II. An electron paramagnetic resonance and optical spectral study of the ferric proteins
    • Kraus, D. W., Wittenberg, J. B., Lu, J. F., and Peisach, J. (1990) Hemoglobins of the Lucina pectinata/bacteria symbiosis. II. An electron paramagnetic resonance and optical spectral study of the ferric proteins, J. Biol. Chem. 265, 16054-16059.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16054-16059
    • Kraus, D.W.1    Wittenberg, J.B.2    Lu, J.F.3    Peisach, J.4
  • 84
    • 0027717068 scopus 로고
    • Resonance Raman and EPR spectroscopic studies on heme-heme oxygenase complexes
    • Sun, J., Wilks, A., Ortiz de Montellano, P. R., and Loehr, T. M. (1993) Resonance Raman and EPR spectroscopic studies on heme-heme oxygenase complexes, Biochemistry 32, 14151-14157.
    • (1993) Biochemistry , vol.32 , pp. 14151-14157
    • Sun, J.1    Wilks, A.2    Ortiz De Montellano, P.R.3    Loehr, T.M.4
  • 85
    • 0028057463 scopus 로고
    • Heme-heme oxygenase complex. Structure of the catalytic site and its implication for oxygen activation
    • Takahashi, S., Wang, J., Rousseau, D. L., Ishikawa, K., Yoshida, T., Host, J. R., and Ikeda-Saito, M. (1994) Heme-heme oxygenase complex. Structure of the catalytic site and its implication for oxygen activation, J. Biol. Chem. 269, 1010-1014.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1010-1014
    • Takahashi, S.1    Wang, J.2    Rousseau, D.L.3    Ishikawa, K.4    Yoshida, T.5    Host, J.R.6    Ikeda-Saito, M.7
  • 86
    • 0019765035 scopus 로고
    • Measurement of the oxidation-reduction equilibria of hemoglobin and myoglobin
    • Taylor, J. F. (1981) Measurement of the oxidation-reduction equilibria of hemoglobin and myoglobin, Methods Enzymol. 76, 577-582.
    • (1981) Methods Enzymol. , vol.76 , pp. 577-582
    • Taylor, J.F.1
  • 87
    • 0025026382 scopus 로고
    • Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands
    • Kraus, D. W., and Wittenberg, J. B. (1990) Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands, J. Biol. Chem. 265, 16043-16053.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16043-16053
    • Kraus, D.W.1    Wittenberg, J.B.2
  • 88
    • 0016682440 scopus 로고
    • Effects of 2,4-substituents of deuteropheme upon redox potentials of horseradish peroxidases
    • Yamada, H., Makino, R., and Yamazaki, I. (1975) Effects of 2,4-substituents of deuteropheme upon redox potentials of horseradish peroxidases, Arch. Biochem. Biophys. 169, 344-353.
    • (1975) Arch. Biochem. Biophys. , vol.169 , pp. 344-353
    • Yamada, H.1    Makino, R.2    Yamazaki, I.3
  • 89
    • 0001233062 scopus 로고
    • Oxidation-reduction potentials of horseradish peroxidase
    • Harbury, H. A. (1957) Oxidation-reduction potentials of horseradish peroxidase, J. Biol. Chem. 225, 1009-1024.
    • (1957) J. Biol. Chem. , vol.225 , pp. 1009-1024
    • Harbury, H.A.1


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