메뉴 건너뛰기




Volumn 43, Issue 13, 2004, Pages 3956-3968

Biochemical and Spectroscopic Characterization of the Covalent Binding of Heme to Cytochrome b6

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BLOOD; HEMOGLOBIN; MUTAGENESIS; RAMAN SCATTERING; RESONANCE; SPECTROSCOPIC ANALYSIS;

EID: 1842538862     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036093p     Document Type: Article
Times cited : (37)

References (59)
  • 1
    • 0027241479 scopus 로고
    • The chloroplast cytochrome bf complex: A critical focus on function
    • Hope, A. B. (1993) The chloroplast cytochrome bf complex: a critical focus on function, Biochim. Biophys. Acta 1143, 1-22.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 1-22
    • Hope, A.B.1
  • 18
    • 0002565747 scopus 로고
    • 6 in an algal mutant lacking photosystem I centers
    • 6 in an algal mutant lacking photosystem I centers, Biochim. Biophys. Acta 725, 25-33.
    • (1983) Biochim. Biophys. Acta , vol.725 , pp. 25-33
    • Lavergne, J.1
  • 19
    • 0001695270 scopus 로고
    • The low-potential electron-transfer chain in the cytochrome bf complex
    • Joliot, P., and Joliot, A. (1988) The low-potential electron-transfer chain in the cytochrome bf complex, Biochim. Biophys. Acta 933, 319-333.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 319-333
    • Joliot, P.1    Joliot, A.2
  • 20
    • 0028360952 scopus 로고
    • 6f subunits. The Rieske iron-sulfur protein from Chlamydomonas reinhardtii is an extrinsic protein
    • 6f subunits. The Rieske iron-sulfur protein from Chlamydomonas reinhardtii is an extrinsic protein, J. Biol. Chem. 269, 7597-7602.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7597-7602
    • Breyton, C.1    De Vitry, C.2    Popot, J.-L.3
  • 23
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • Thomas, P. E., Ryan, D., and Levin, W. (1976) An improved staining procedure for the detection of peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels, Anal. Biochem. 75, 168-176.
    • (1976) Anal. Biochem. , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 24
    • 0028178516 scopus 로고
    • 6f complexes: An approach using genetic transformation of the green alga Chlamydomonas reinhardtii
    • 6f complexes: an approach using genetic transformation of the green alga Chlamydomonas reinhardtii, EMBO J. 13, 1019-1027.
    • (1994) EMBO J. , vol.13 , pp. 1019-1027
    • Kuras, R.1    Wollman, F.-A.2
  • 25
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection, Proc. Natl. Acad. Sci. U.S.A. 82, 488-492.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 26
    • 0025766849 scopus 로고
    • Transgenic expression of aminoglycoside adenine transferase in the chloroplast: A selectable marker of site-directed transformation of Chlamydomonas
    • Goldschmidt-Clermont, M. (1991) Transgenic expression of aminoglycoside adenine transferase in the chloroplast: a selectable marker of site-directed transformation of Chlamydomonas, Nucleic Acids Res. 19, 4083-4089.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4083-4089
    • Goldschmidt-Clermont, M.1
  • 29
    • 0027818118 scopus 로고
    • Complete assignment of cytochrome c resonance Raman spectra via enzymic reconstitution with isotopically labeled hemes
    • Hu, S., Morris, I. K., Singh, J. P., Smith, K. M., and Spiro, T. G. (1993) Complete assignment of cytochrome c resonance Raman spectra via enzymic reconstitution with isotopically labeled hemes, J. Am. Chem. Soc. 115, 12446-12458.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12446-12458
    • Hu, S.1    Morris, I.K.2    Singh, J.P.3    Smith, K.M.4    Spiro, T.G.5
  • 30
    • 0030467166 scopus 로고    scopus 로고
    • Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin
    • Hu, S., Smith, K. M., and Spiro, T. G. (1996) Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin, J. Am. Chem. Soc. 118, 12638-12646.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12638-12646
    • Hu, S.1    Smith, K.M.2    Spiro, T.G.3
  • 31
    • 0020803212 scopus 로고
    • Intermediate and stable redox states of cytochrome c studied by low-temperature resonance Raman spectroscopy
    • Cartling, B. (1983) Intermediate and stable redox states of cytochrome c studied by low-temperature resonance Raman spectroscopy, Biophys. J. 43, 191-205.
    • (1983) Biophys. J. , vol.43 , pp. 191-205
    • Cartling, B.1
  • 32
    • 0027961094 scopus 로고
    • Resonance Raman spectroscopy of c-type cytochromes
    • Desbois, A. (1994) Resonance Raman spectroscopy of c-type cytochromes, Biochimie 76, 693-707.
    • (1994) Biochimie , vol.76 , pp. 693-707
    • Desbois, A.1
  • 33
    • 0032987138 scopus 로고    scopus 로고
    • Investigation of some covalent and noncovalent complexes by matrix-assisted laser desorption/ionization time-of-flight and electrospray mass spectrometry
    • Bordini, E., and Hamdan, M. (1999) Investigation of some covalent and noncovalent complexes by matrix-assisted laser desorption/ionization time-of-flight and electrospray mass spectrometry, Mass Spectrom. 13, 1143-1151.
    • (1999) Mass Spectrom. , vol.13 , pp. 1143-1151
    • Bordini, E.1    Hamdan, M.2
  • 34
    • 0035563678 scopus 로고    scopus 로고
    • A study of peptide-peptide interaction by matrix-assisted laser desorption/ionization
    • Woods, A. S., and Huestis, M. A. (2001) A study of peptide-peptide interaction by matrix-assisted laser desorption/ionization, J. Am. Soc. Mass Spectrom. 12, 88-96.
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 88-96
    • Woods, A.S.1    Huestis, M.A.2
  • 35
    • 0028821421 scopus 로고
    • Primary structure and post-translational modification of ferredoxin-NADP reductase from Chlamydomonas reinhardtii
    • Decottignies, P., Le Maréchal, P., Jacquot, J.-P., Schmitter, J.-M., and Gadal, P. (1995) Primary structure and post-translational modification of ferredoxin-NADP reductase from Chlamydomonas reinhardtii, Arch. Biochem. Biophys. 316, 249-259.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 249-259
    • Decottignies, P.1    Le Maréchal, P.2    Jacquot, J.-P.3    Schmitter, J.-M.4    Gadal, P.5
  • 36
    • 0029866761 scopus 로고    scopus 로고
    • Characterisation of the heptameric poreforming complex of the Aeromonas toxin aerolysin using MALDI-TOF mass spectrometry
    • Moniatte, M., van der Goot, F. G., Buckley, J. T., Pattus, F., and van Dorsselaer, A. (1996) Characterisation of the heptameric poreforming complex of the Aeromonas toxin aerolysin using MALDI-TOF mass spectrometry, FEBS Lett. 384, 269-272.
    • (1996) FEBS Lett. , vol.384 , pp. 269-272
    • Moniatte, M.1    Van Der Goot, F.G.2    Buckley, J.T.3    Pattus, F.4    Van Dorsselaer, A.5
  • 37
    • 0032253727 scopus 로고    scopus 로고
    • Detection of non-covalent interaction of single and double stranded DNA with peptides by MALDI-TOF
    • Lin, S., Cotter, R. J., and Woods, A. S. (1998) Detection of non-covalent interaction of single and double stranded DNA with peptides by MALDI-TOF, Proteins Suppl. 2, 12-21.
    • (1998) Proteins , Issue.SUPPL. 2 , pp. 12-21
    • Lin, S.1    Cotter, R.J.2    Woods, A.S.3
  • 41
    • 1842546738 scopus 로고    scopus 로고
    • Identification of Three Previously Unknown in Vivo Protein Phosphorylation Sites in Thylakoid Membranes of Arabidopsis thaliana
    • Hansson, M., and Vener, A. V. (2003) Identification of Three Previously Unknown in Vivo Protein Phosphorylation Sites in Thylakoid Membranes of Arabidopsis thaliana, Mol. Cell. Proteomics 2, 550-559.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 550-559
    • Hansson, M.1    Vener, A.V.2
  • 42
    • 0026045166 scopus 로고
    • Photosystem II particles from Chlamydomonas reinhardtii. Purification, molecular weight, small subunit composition, and protein phosphorylation
    • de Vitry, C., Diner, B. A., and Popot, J.-L. (1991) Photosystem II particles from Chlamydomonas reinhardtii. Purification, molecular weight, small subunit composition, and protein phosphorylation, J. Biol. Chem. 266, 16614-16621.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16614-16621
    • De Vitry, C.1    Diner, B.A.2    Popot, J.-L.3
  • 43
    • 0032502756 scopus 로고    scopus 로고
    • Photosystem II particles from Chlamydomonas reinhardtii. Purification, molecular weight, small subunit composition, and protein phosphorylation
    • Yu, J., and Le Brun, N. E. (1998) Photosystem II particles from Chlamydomonas reinhardtii. Purification, molecular weight, small subunit composition, and protein phosphorylation, J. Biol. Chem. 273, 8860-8866.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8860-8866
    • Yu, J.1    Le Brun, N.E.2
  • 44
    • 0027424781 scopus 로고
    • A heme c-peptide model system for the resonance Raman study of c-type cytochromes: Characterization of the solvent-dependence of peptide-histidine-heme interactions
    • Othman, S., Le Lirzin, A., and Desbois, A. (1993) A heme c-peptide model system for the resonance Raman study of c-type cytochromes: characterization of the solvent-dependence of peptide-histidine-heme interactions, Biochemistry 32, 9781-9791.
    • (1993) Biochemistry , vol.32 , pp. 9781-9791
    • Othman, S.1    Le Lirzin, A.2    Desbois, A.3
  • 45
    • 0029942847 scopus 로고    scopus 로고
    • Evidence for a proximal histidine interaction in the structure of cytochromes c in solution: A resonance Raman study
    • Othman, S., Richaud, P., Verméglio, A., and Desbois, A. (1996) Evidence for a proximal histidine interaction in the structure of cytochromes c in solution: a resonance Raman study, Biochemistry 35, 9224-9234.
    • (1996) Biochemistry , vol.35 , pp. 9224-9234
    • Othman, S.1    Richaud, P.2    Verméglio, A.3    Desbois, A.4
  • 46
    • 1842494618 scopus 로고
    • On the properties and nature of dihydroxyl-haem
    • Keilin, J. (1949) On the properties and nature of dihydroxyl-haem, Biochem. J. 45, 448-455.
    • (1949) Biochem. J. , vol.45 , pp. 448-455
    • Keilin, J.1
  • 47
    • 0010104442 scopus 로고
    • Raman evidence for the formation of a monoaquo adduct of iron(II) tetrakis((N-tert-butylcarbamoyl)phenyl)porphyrin. A model for hemoproteins at low pH
    • Leondiadis, L., Momenteau, M., and Desbois, A. (1992) Raman evidence for the formation of a monoaquo adduct of iron(II) tetrakis((N-tert-butylcarbamoyl)phenyl)porphyrin. A model for hemoproteins at low pH, Inorg. Chem. 31, 4691-4696.
    • (1992) Inorg. Chem. , vol.31 , pp. 4691-4696
    • Leondiadis, L.1    Momenteau, M.2    Desbois, A.3
  • 48
    • 0037020614 scopus 로고    scopus 로고
    • Air-stable, electron-deficient Fe(II) catalytic porphyrins. Characterization and molecular structures of rare high spin Fe(II) hexacoordinated porphyrins
    • Barkigia, K. M., Palacio, M., Sun, Y., Nogues, M., Renner, M. W., Varret, F., Battioni, P., Mansuy, D., and Fajer, J. (2002) Air-stable, electron-deficient Fe(II) catalytic porphyrins. Characterization and molecular structures of rare high spin Fe(II) hexacoordinated porphyrins, Inorg. Chem. 41, 5647-5649.
    • (2002) Inorg. Chem. , vol.41 , pp. 5647-5649
    • Barkigia, K.M.1    Palacio, M.2    Sun, Y.3    Nogues, M.4    Renner, M.W.5    Varret, F.6    Battioni, P.7    Mansuy, D.8    Fajer, J.9
  • 51
    • 0028568237 scopus 로고
    • Resonance Raman investigation of imidazole and imidazolate complexes of microperoxidase: Characterization of the bis(histidine) axial ligation in c-type cytochrome
    • Othman, S., Le Lirzin, A., and Desbois, A. (1994) Resonance Raman investigation of imidazole and imidazolate complexes of microperoxidase: characterization of the bis(histidine) axial ligation in c-type cytochrome, Biochemistry 33, 15437-15488.
    • (1994) Biochemistry , vol.33 , pp. 15437-15488
    • Othman, S.1    Le Lirzin, A.2    Desbois, A.3
  • 52
    • 0032425991 scopus 로고    scopus 로고
    • Resonance Raman investigation of lysine and N-acetylmethionine complexes of ferric and ferrous microperoxidase. Influence of the axial ligation on the heme c structure
    • Othman, S., and Desbois, A. (1998) Resonance Raman investigation of lysine and N-acetylmethionine complexes of ferric and ferrous microperoxidase. Influence of the axial ligation on the heme c structure, Eur. Biophys. J. 28, 12-25.
    • (1998) Eur. Biophys. J. , vol.28 , pp. 12-25
    • Othman, S.1    Desbois, A.2
  • 54
    • 0001338654 scopus 로고
    • Photoreduction of heme proteins: Spectroscopic studies and cross-section measurements
    • Gu, Y., Li, P., Sage, J. T., and Champion, P. M. (1993) Photoreduction of heme proteins: spectroscopic studies and cross-section measurements, J. Am. Chem. Soc. 115, 4993-5004
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4993-5004
    • Gu, Y.1    Li, P.2    Sage, J.T.3    Champion, P.M.4
  • 55
    • 0141480147 scopus 로고    scopus 로고
    • Absorption and resonance Raman investigations of ligand rotation and nonplanar heme distortion in bis-base low-spin iron(II)-tetrakis(o-pivalamidophenyl)porphyrin complexes
    • Le Moigne, C., Picaud, T., Boussac, A., Loock, B., Momenteau, M., and Desbois, A. (2003) Absorption and resonance Raman investigations of ligand rotation and nonplanar heme distortion in bis-base low-spin iron(II)-tetrakis(o-pivalamidophenyl)porphyrin complexes, Inorg. Chem. 42, 6081-6088.
    • (2003) Inorg. Chem. , vol.42 , pp. 6081-6088
    • Le Moigne, C.1    Picaud, T.2    Boussac, A.3    Loock, B.4    Momenteau, M.5    Desbois, A.6
  • 56
    • 0036671471 scopus 로고    scopus 로고
    • Cytochrome c maturation: A complex pathway for a simple task?
    • Thony-Meyer, L. (2002) Cytochrome c maturation: a complex pathway for a simple task? Biochem. Soc. Trans. 30, 633-638.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 633-638
    • Thony-Meyer, L.1
  • 57
    • 0037462683 scopus 로고    scopus 로고
    • Functional analysis of a divergent system 11 protein, Ccs1, involved in c-type cytochrome biogenesis
    • Dreyfuss, B. W., Hamel, P. P., Nakamoto, S. S., and Merchant, S. (2003) Functional analysis of a divergent system 11 protein, Ccs1, involved in c-type cytochrome biogenesis, J. Biol. Chem. 278, 2604-2613.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2604-2613
    • Dreyfuss, B.W.1    Hamel, P.P.2    Nakamoto, S.S.3    Merchant, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.