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Volumn 45, Issue 41, 2006, Pages 12530-12538

Evaluating the roles of the heme a side chains in cytochrome c oxidase using designed heme proteins

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOSYNTHESIS; ELECTROCHEMISTRY; ENZYMES; PORPHYRINS; REDOX REACTIONS;

EID: 33750065106     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060565t     Document Type: Article
Times cited : (31)

References (54)
  • 2
    • 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
  • 5
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thöny-Meyer, L. (1997) Biogenesis of respiratory cytochromes in bacteria, Microbiol. Mol. Biol. Rev. 61, 337-376.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 337-376
    • Thöny-Meyer, L.1
  • 9
    • 2542483466 scopus 로고    scopus 로고
    • Structural elements involved in electron-coupled proton transfer in cytochrome c oxidase
    • Namslauer, A., and Brzezinski, P. (2004) Structural elements involved in electron-coupled proton transfer in cytochrome c oxidase, FEBS Lett. 567, 103-110.
    • (2004) FEBS Lett. , vol.567 , pp. 103-110
    • Namslauer, A.1    Brzezinski, P.2
  • 10
    • 0028290824 scopus 로고
    • Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation
    • Trumpower, B. L., and Gennis, R. B. (1994) Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation, Annu. Rev. Biochem. 63, 675-716.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 675-716
    • Trumpower, B.L.1    Gennis, R.B.2
  • 11
    • 0038518286 scopus 로고    scopus 로고
    • Assembly of cytochrome c oxidase within the mitochondrion
    • Carr, H. S., and Winge, D. R. (2003) Assembly of cytochrome c oxidase within the mitochondrion, Acc. Chem. Res. 36, 309-316.
    • (2003) Acc. Chem. Res. , vol.36 , pp. 309-316
    • Carr, H.S.1    Winge, D.R.2
  • 12
    • 0028038276 scopus 로고
    • Isolation of a human cDNA for heme a:farnesyltransferase by functional complementation of a yeast COX10 mutant
    • Glerum, D. M., and Tzagoloff, A. (1994) Isolation of a human cDNA for heme a:farnesyltransferase by functional complementation of a yeast COX10 mutant, Proc. Natl. Acad. Sci. U.S.A. 91, 8452-8456.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 8452-8456
    • Glerum, D.M.1    Tzagoloff, A.2
  • 13
    • 0025917055 scopus 로고
    • The heme groups of cytochrome o from Escherichia coli
    • Puustinen, A., and Wikström, M. (1991) The heme groups of cytochrome o from Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 88, 6122-6126,
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 6122-6126
    • Puustinen, A.1    Wikström, M.2
  • 14
    • 0027442655 scopus 로고
    • In vitro heme o synthesis by the cyoE gene product from Escherichia coli
    • Saiki, K., Mogi, T., Ogura, K., and Ankaru, Y. (1993) In vitro heme o synthesis by the cyoE gene product from Escherichia coli, J. Biol. Chem. 268, 26041-26045.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26041-26045
    • Saiki, K.1    Mogi, T.2    Ogura, K.3    Ankaru, Y.4
  • 15
    • 3042706379 scopus 로고    scopus 로고
    • Biosynthesis and role of heme o and heme a
    • (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.), Academic Press, Amsterdam
    • Mogi, T. (2003) Biosynthesis and role of heme o and heme a, in The Iron and Cobalt Pigments: Biosynthesis, Structure, and Degradation (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.) pp 157-181, Academic Press, Amsterdam.
    • (2003) The Iron and Cobalt Pigments: Biosynthesis, Structure, and Degradation , pp. 157-181
    • Mogi, T.1
  • 16
    • 0035831217 scopus 로고    scopus 로고
    • Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of heme o
    • Barros, M. H., Carlson, C. G., Glerum, D. M., and Tzagoloff, A. (2001) Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of heme o, FEBS Lett. 492, 133-138.
    • (2001) FEBS Lett. , vol.492 , pp. 133-138
    • Barros, M.H.1    Carlson, C.G.2    Glerum, D.M.3    Tzagoloff, A.4
  • 17
    • 0032617222 scopus 로고    scopus 로고
    • Cloning of Bacillus stearothemophilus ctaA and heme a synthesis with the CtaA protein produced in Escherichia coli
    • Sakamoto, J., Hayakawa, A., Uehara, T., Noguchi, S., and Sone, N. (1999) Cloning of Bacillus stearothemophilus ctaA and heme a synthesis with the CtaA protein produced in Escherichia coli, Biosci. Biotechnol. Biochem. 63, 96-103.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 96-103
    • Sakamoto, J.1    Hayakawa, A.2    Uehara, T.3    Noguchi, S.4    Sone, N.5
  • 18
    • 0027527547 scopus 로고
    • Bacillus subtilis CtaA and CtaB function in haem a biosynthesis
    • Svensson, B., Lübben, M., and Hederstedt, L. (1993) Bacillus subtilis CtaA and CtaB function in haem a biosynthesis, Mol. Microbiol. 10, 193-201.
    • (1993) Mol. Microbiol. , vol.10 , pp. 193-201
    • Svensson, B.1    Lübben, M.2    Hederstedt, L.3
  • 19
    • 3042774125 scopus 로고    scopus 로고
    • Heme a synthase does not incorporate molecular oxygen into the formyl group of heme a
    • Brown, K. R., Brown, B. M., Hoagland, E., Manye, C. L., and Hegg, E. L. (2004) Heme a synthase does not incorporate molecular oxygen into the formyl group of heme a, Biochemistry 43, 8616-8624.
    • (2004) Biochemistry , vol.43 , pp. 8616-8624
    • Brown, K.R.1    Brown, B.M.2    Hoagland, E.3    Manye, C.L.4    Hegg, E.L.5
  • 20
    • 0036713124 scopus 로고    scopus 로고
    • Identification of novel hemes generated by heme a synthase: Evidence for two successive monooxygenase reactions
    • Brown, K. R., Allan, B. M., Do, P., and Hegg, E. L. (2002) Identification of novel hemes generated by heme a synthase: Evidence for two successive monooxygenase reactions, Biochemistry 41, 10906-10913.
    • (2002) Biochemistry , vol.41 , pp. 10906-10913
    • Brown, K.R.1    Allan, B.M.2    Do, P.3    Hegg, E.L.4
  • 22
    • 0037424025 scopus 로고    scopus 로고
    • Thermodynamic characterization of ferric and ferrous haem binding to a designed four-α-helix protein
    • Reedy, C. J., Kennedy, M. L., and Gibney, B. R. (2003) Thermodynamic characterization of ferric and ferrous haem binding to a designed four-α-helix protein, Chem. Commun., 570-571.
    • (2003) Chem. Commun. , pp. 570-571
    • Reedy, C.J.1    Kennedy, M.L.2    Gibney, B.R.3
  • 24
    • 11144288653 scopus 로고    scopus 로고
    • Design of a five-coordinate heme protein maquette: A spectroscopic model of deoxyMyoglobin
    • Zhuang, J., Amoroso, J. H., Kinloch, R., Dawson, J. H., Baldwin, M. J., and Gibney, B. R. (2004) Design of a five-coordinate heme protein maquette: A spectroscopic model of deoxyMyoglobin, Inorg. Chem. 43, 8218-8220.
    • (2004) Inorg. Chem. , vol.43 , pp. 8218-8220
    • Zhuang, J.1    Amoroso, J.H.2    Kinloch, R.3    Dawson, J.H.4    Baldwin, M.J.5    Gibney, B.R.6
  • 25
    • 33745684585 scopus 로고    scopus 로고
    • Evaluation of electron-withdrawing group effects on heme binding in a designed protein: Implications for heme a in cytochrome c oxidase
    • Zhuang, J., Amoroso, J. H., Kinloch, R., Dawson, J. H., Baldwin, M. J., and Gibney, B. R. (2006) Evaluation of electron-withdrawing group effects on heme binding in a designed protein: Implications for heme a in cytochrome c oxidase, Inorg. Chem. 45, 4685-4694.
    • (2006) Inorg. Chem. , vol.45 , pp. 4685-4694
    • Zhuang, J.1    Amoroso, J.H.2    Kinloch, R.3    Dawson, J.H.4    Baldwin, M.J.5    Gibney, B.R.6
  • 26
    • 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
  • 29
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A., and Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra, Anal. Blochem. 161, 1-15.
    • (1987) Anal. Blochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 31
    • 0018115502 scopus 로고
    • Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems
    • Dutton, P. L. (1978) Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems, Methods Enzymol. 54, 411-435.
    • (1978) Methods Enzymol. , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 32
    • 0001295932 scopus 로고    scopus 로고
    • Models of the cytochromes. Redox properties and thermodynamic stabilities of complexes of "hindered" iron(III) and iron(II) tetraphenylporphyrinates with substituted pyridines and imidazoles
    • Nesset, M. J. M., Shokhirev, N. V., Enemark, P. D., Jacobson, S. E., and Walker, F. A. (1996) Models of the cytochromes. Redox properties and thermodynamic stabilities of complexes of "hindered" iron(III) and iron(II) tetraphenylporphyrinates with substituted pyridines and imidazoles, Inorg. Chem. 35, 5188-5200.
    • (1996) Inorg. Chem. , vol.35 , pp. 5188-5200
    • Nesset, M.J.M.1    Shokhirev, N.V.2    Enemark, P.D.3    Jacobson, S.E.4    Walker, F.A.5
  • 33
    • 1542274547 scopus 로고    scopus 로고
    • Heme protein assemblies
    • Reedy, C. J., and Gibney, B. R. (2004) Heme protein assemblies, Chem. Rev. 104, 589-604.
    • (2004) Chem. Rev. , vol.104 , pp. 589-604
    • Reedy, C.J.1    Gibney, B.R.2
  • 35
    • 0035471139 scopus 로고    scopus 로고
    • Peptide-based heme protein models
    • Lombardi, A., Nastri, F., and Pavone, V. (2001) Peptide-based heme protein models, Chem. Rev. 101, 3165-3190.
    • (2001) Chem. Rev. , vol.101 , pp. 3165-3190
    • Lombardi, A.1    Nastri, F.2    Pavone, V.3
  • 36
    • 0035471138 scopus 로고    scopus 로고
    • Engineering novel metalloproteins: Design of metal-binding sites into native protein scaffolds
    • Lu, Y., Berry, S. M., and Pfister, T. D. (2001) Engineering novel metalloproteins: Design of metal-binding sites into native protein scaffolds, Chem. Rev. 101, 3047-3080.
    • (2001) Chem. Rev. , vol.101 , pp. 3047-3080
    • Lu, Y.1    Berry, S.M.2    Pfister, T.D.3
  • 37
    • 0035104068 scopus 로고    scopus 로고
    • Design, synthesis and characterization of a novel hemoprotein
    • Xu, Z., and Farid, R. S. (2001) Design, synthesis and characterization of a novel hemoprotein, Protein Sci. 10, 236-249.
    • (2001) Protein Sci. , vol.10 , pp. 236-249
    • Xu, Z.1    Farid, R.S.2
  • 38
    • 0029737895 scopus 로고    scopus 로고
    • The association rate constant for heme binding to globin is independent of protein structure
    • Hargrove, M. S., Barrick, D., and Olson, J. S. (1996) The association rate constant for heme binding to globin is independent of protein structure, Biochemistry 35, 11293-11299.
    • (1996) Biochemistry , vol.35 , pp. 11293-11299
    • Hargrove, M.S.1    Barrick, D.2    Olson, J.S.3
  • 41
    • 0034641675 scopus 로고    scopus 로고
    • Self-assembly of heme a and heme b in a designed four-helix bundle. Implications for a cytochrome c oxidase maquette
    • Gibney, B. R., Isogai, Y., Reddy, K. S., Rabanal, F., Grosset, A. M., Moser, C. C., and Dutton, P. L. (2000) Self-assembly of heme a and heme b in a designed four-helix bundle. Implications for a cytochrome c oxidase maquette, Biochemistry 39, 11041-11049.
    • (2000) Biochemistry , vol.39 , pp. 11041-11049
    • Gibney, B.R.1    Isogai, Y.2    Reddy, K.S.3    Rabanal, F.4    Grosset, A.M.5    Moser, C.C.6    Dutton, P.L.7
  • 42
    • 0001536888 scopus 로고
    • Studies on cytochrome oxidase. III. Improved preparation and some properties
    • Yonetani, T. (1961) Studies on cytochrome oxidase. III. Improved preparation and some properties, J. Biol. Chem. 236, 1850-1856.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1850-1856
    • Yonetani, T.1
  • 43
    • 0034610349 scopus 로고    scopus 로고
    • Heme redox potential control in de novo designed four-α-helix bundle proteins
    • Shifman, J. M., Gibney, B. R., Sharp, R. E., and Dutton, P. L. (2000) Heme redox potential control in de novo designed four-α-helix bundle proteins, Biochemistry 39, 14813-14821.
    • (2000) Biochemistry , vol.39 , pp. 14813-14821
    • Shifman, J.M.1    Gibney, B.R.2    Sharp, R.E.3    Dutton, P.L.4
  • 45
    • 0028356367 scopus 로고
    • Influence of hydrocarbon tail structure on quinone binding and electron-transfer at the QA and QB sites in the photosynthetic reaction center protein
    • Warncke, K., Gunner, M. R., Braun, B. S., Gu, L., Yu, C.-A., Bruce, J. M., and Dutton, P. L. (1994) Influence of hydrocarbon tail structure on quinone binding and electron-transfer at the QA and QB sites in the photosynthetic reaction center protein, Biochemistry 33, 7830-7841.
    • (1994) Biochemistry , vol.33 , pp. 7830-7841
    • Warncke, K.1    Gunner, M.R.2    Braun, B.S.3    Gu, L.4    Yu, C.-A.5    Bruce, J.M.6    Dutton, P.L.7
  • 46
    • 0015086335 scopus 로고
    • The oxidation-reduction potentials of the hemes and copper of cytochrome oxidase from beef heart
    • Tsudzuki, T., and Wilson, D. F. (1971) The oxidation-reduction potentials of the hemes and copper of cytochrome oxidase from beef heart, Arch. Biochem. Biophys. 145, 149-154.
    • (1971) Arch. Biochem. Biophys. , vol.145 , pp. 149-154
    • Tsudzuki, T.1    Wilson, D.F.2
  • 47
    • 0018801573 scopus 로고
    • Horse heart cytochrome c. The oxidation-reduction potential and protein structures
    • Myer, Y. P., Saturno, A. F., Verma, B. C., and Pande, A. (1979) Horse heart cytochrome c. The oxidation-reduction potential and protein structures, J. Biol. Chem. 254, 11202-11207.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11202-11207
    • Myer, Y.P.1    Saturno, A.F.2    Verma, B.C.3    Pande, A.4
  • 50
    • 1842412487 scopus 로고    scopus 로고
    • Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme
    • Williams, P. A., Fülöp, V., Garman, E. F., Saunders, N. F. W., Ferguson, S. J., and Hajdu, J. (1997) Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme, Nature 389, 406-412.
    • (1997) Nature , vol.389 , pp. 406-412
    • Williams, P.A.1    Fülöp, V.2    Garman, E.F.3    Saunders, N.F.W.4    Ferguson, S.J.5    Hajdu, J.6
  • 51
    • 1042299967 scopus 로고    scopus 로고
    • A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide
    • Cowley, A. B., Lukat-Rodgers, G. S., Rodgers, K. R., and Benson, D. R. (2004) A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide, Biochemistry 43, 1656-1666.
    • (2004) Biochemistry , vol.43 , pp. 1656-1666
    • Cowley, A.B.1    Lukat-Rodgers, G.S.2    Rodgers, K.R.3    Benson, D.R.4
  • 52
    • 28444470538 scopus 로고    scopus 로고
    • Role of heme types in heme-copper oxidases: Effects of replacing a heme b with a heme o mimic in an engineered heme-copper center in myoglobin
    • Wang, N., Zhao, X., and Lu, Y. (2005) Role of heme types in heme-copper oxidases: Effects of replacing a heme b with a heme o mimic in an engineered heme-copper center in myoglobin, J. Am. Chem. Soc. 127, 16541-16547.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 16541-16547
    • Wang, N.1    Zhao, X.2    Lu, Y.3
  • 53
    • 84941518128 scopus 로고
    • Cytohemin from the heart muscle
    • Warburg, O., and Gewitz, H. S. (1951) Cytohemin from the heart muscle, Z. Physiol. Chem. 288, 1-4.
    • (1951) Z. Physiol. Chem. , vol.288 , pp. 1-4
    • Warburg, O.1    Gewitz, H.S.2
  • 54
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


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