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Volumn 585, Issue 3, 2011, Pages 545-548

Axial ligation of the high-potential heme center in an Arabidopsis cytochrome b561

Author keywords

Cytochrome b561; Double mutant; EPR; Optical absorption spectroscopy; Resonance Raman spectroscopy

Indexed keywords

ARABIDOPSIS PROTEIN; CYTOCHROME B561; HEME; HISTIDINE; UNCLASSIFIED DRUG;

EID: 79551485549     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.01.006     Document Type: Article
Times cited : (12)

References (21)
  • 1
    • 27844441716 scopus 로고    scopus 로고
    • Cytochrome b561 protein family: Expanding roles and versatile transmembrane electron transfer abilities as predicted by a new classification system and protein sequence motif analyses
    • M. Tsubaki, F. Takeuchi, and N. Nakanishi Cytochrome b561 protein family: expanding roles and versatile transmembrane electron transfer abilities as predicted by a new classification system and protein sequence motif analyses Biochim. Biophys. Acta 1763 2005 174 200
    • (2005) Biochim. Biophys. Acta , vol.1763 , pp. 174-200
    • Tsubaki, M.1    Takeuchi, F.2    Nakanishi, N.3
  • 3
    • 1342308497 scopus 로고    scopus 로고
    • Localization of an ascorbate-reducible cytochrome b561 in the plant tonoplast
    • D. Griesen, D. Su, A. Bérczi, and H. Asard Localization of an ascorbate-reducible cytochrome b561 in the plant tonoplast Plant Physiol. 134 2004 726 734
    • (2004) Plant Physiol. , vol.134 , pp. 726-734
    • Griesen, D.1    Su, D.2    Bérczi, A.3    Asard, H.4
  • 4
    • 33947422966 scopus 로고    scopus 로고
    • An Arabidopsis cytochrome b561 with trans-membrane ferrireductase capability
    • A. Bérczi, D. Su, and H. Asard An Arabidopsis cytochrome b561 with trans-membrane ferrireductase capability FEBS Lett. 581 2007 1505 1508
    • (2007) FEBS Lett. , vol.581 , pp. 1505-1508
    • Bérczi, A.1    Su, D.2    Asard, H.3
  • 5
    • 0015214389 scopus 로고
    • Cytochrome b561 of the bovine adrenal chromaffin granules. A high potential b-type cytochrome
    • T. Flatmark, and O. Terland Cytochrome b561 of the bovine adrenal chromaffin granules. A high potential b-type cytochrome Biochim. Biophys. Acta 253 1971 487 491
    • (1971) Biochim. Biophys. Acta , vol.253 , pp. 487-491
    • Flatmark, T.1    Terland, O.2
  • 6
    • 0019882456 scopus 로고
    • Cytochrome b-561 of the bovine adrenal chromaffin granules. Molecular weight and hydrodynamic properties in micellar solutions of Triton X-100
    • T. Flatmark, and M. Grønberg Cytochrome b-561 of the bovine adrenal chromaffin granules. Molecular weight and hydrodynamic properties in micellar solutions of Triton X-100 Biochem. Biophys. Res. Commun. 99 1981 292 301
    • (1981) Biochem. Biophys. Res. Commun. , vol.99 , pp. 292-301
    • Flatmark, T.1    Grønberg, M.2
  • 7
    • 0035799318 scopus 로고    scopus 로고
    • Ascorbate inhibits the carbethoxylation of two histidyl and one tyrosyl residues indispensable for the trans-membrane electron transfer reaction of cytochrome b561
    • F. Takeuchi, K. Kobayashi, S. Tagawa, and M. Tsubaki Ascorbate inhibits the carbethoxylation of two histidyl and one tyrosyl residues indispensable for the trans-membrane electron transfer reaction of cytochrome b561 Biochemistry 40 2001 4067 4076
    • (2001) Biochemistry , vol.40 , pp. 4067-4076
    • Takeuchi, F.1    Kobayashi, K.2    Tagawa, S.3    Tsubaki, M.4
  • 8
    • 0030817141 scopus 로고    scopus 로고
    • Existence of two heme B centers in cytochrome b561 from bovine adrenal chromaffin vesicles as revealed by a new purification procedure and EPR spectroscopy
    • M. Tsubaki, M. Nakayama, E. Okuyama, Y. Ichikawa, and H. Hori Existence of two heme B centers in cytochrome b561 from bovine adrenal chromaffin vesicles as revealed by a new purification procedure and EPR spectroscopy J. Biol. Chem. 272 1997 23206 23210
    • (1997) J. Biol. Chem. , vol.272 , pp. 23206-23210
    • Tsubaki, M.1    Nakayama, M.2    Okuyama, E.3    Ichikawa, Y.4    Hori, H.5
  • 9
    • 14844321947 scopus 로고    scopus 로고
    • Purification and characterization of bovine adrenal cytochrome b561 expressed in insect and yeast cell systems
    • W. Liu, Y. Kamensky, R. Kakkar, E. Foley, R.J. Kulmacz, and G. Palmer Purification and characterization of bovine adrenal cytochrome b561 expressed in insect and yeast cell systems Protein Expr. Purif. 40 2005 429 439
    • (2005) Protein Expr. Purif. , vol.40 , pp. 429-439
    • Liu, W.1    Kamensky, Y.2    Kakkar, R.3    Foley, E.4    Kulmacz, R.J.5    Palmer, G.6
  • 10
    • 1642504227 scopus 로고    scopus 로고
    • Properties of two distinct centers of cytochrome b561 from bovine chromaffin vesicles studied by EPR, resonance Raman and ascorbate reduction assay
    • F. Takeuchi, H. Hori, E. Obayashi, Y. Shiro, and M. Tsubaki Properties of two distinct centers of cytochrome b561 from bovine chromaffin vesicles studied by EPR, resonance Raman and ascorbate reduction assay J. Biochem. 135 2004 53 64
    • (2004) J. Biochem. , vol.135 , pp. 53-64
    • Takeuchi, F.1    Hori, H.2    Obayashi, E.3    Shiro, Y.4    Tsubaki, M.5
  • 11
    • 34547105283 scopus 로고    scopus 로고
    • Axial ligation and stoichiometry of heme centers in adrenal cytochrome b561
    • Y. Kamensky, W. Liu, A.-L. Tsai, R.J. Kulmacz, and G. Palmer Axial ligation and stoichiometry of heme centers in adrenal cytochrome b561 Biochemistry 46 2007 8647 8658
    • (2007) Biochemistry , vol.46 , pp. 8647-8658
    • Kamensky, Y.1    Liu, W.2    Tsai, A.-L.3    Kulmacz, R.J.4    Palmer, G.5
  • 13
    • 77955654011 scopus 로고    scopus 로고
    • Spectral characterization of the recombinant mouse tumor suppressor 101F6 protein
    • A. Bérczi, F. Desmet, S. Van Doorslaer, and H. Asard Spectral characterization of the recombinant mouse tumor suppressor 101F6 protein Eur. Biophys. J. 39 2010 1129 1142
    • (2010) Eur. Biophys. J. , vol.39 , pp. 1129-1142
    • Bérczi, A.1    Desmet, F.2    Van Doorslaer, S.3    Asard, H.4
  • 14
    • 33846435157 scopus 로고    scopus 로고
    • Characterization of an ascorbate-reducible cytochrome b561 by site-directed mutagenesis
    • A. Bérczi, and H. Asard Characterization of an ascorbate-reducible cytochrome b561 by site-directed mutagenesis Acta Biol. Szeged. 50 2006 55 59
    • (2006) Acta Biol. Szeged. , vol.50 , pp. 55-59
    • Bérczi, A.1    Asard, H.2
  • 15
    • 27644494426 scopus 로고    scopus 로고
    • Heterologous expression and site-directed mutagenesis of an ascorbate-reducible cytochrome b561
    • A. Bérczi, D. Su, M. Lakshminarasimhan, A.S. Vargas, and H. Asard Heterologous expression and site-directed mutagenesis of an ascorbate-reducible cytochrome b561 Arch. Biochem. Biophys. 443 2005 82 92
    • (2005) Arch. Biochem. Biophys. , vol.443 , pp. 82-92
    • Bérczi, A.1    Su, D.2    Lakshminarasimhan, M.3    Vargas, A.S.4    Asard, H.5
  • 16
    • 0026633609 scopus 로고
    • Singular value decomposition - Application to analysis of experimental data
    • E.R. Henry, and J. Hofrichter Singular value decomposition - application to analysis of experimental data Methods Enzymol. 210 1992 129 192
    • (1992) Methods Enzymol. , vol.210 , pp. 129-192
    • Henry, E.R.1    Hofrichter, J.2
  • 17
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • S. Stoll, and A. Schweiger EasySpin, a comprehensive software package for spectral simulation and analysis in EPR J. Magn. Reson. 178 2006 42 55
    • (2006) J. Magn. Reson. , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 18
    • 32944470699 scopus 로고    scopus 로고
    • Selective perturbation of the intravesicular heme center of cytochrome b561 by cysteinyl modification with 4, 4-dithiodipyridine
    • F. Takeuchi, H. Hori, and M. Tsubaki Selective perturbation of the intravesicular heme center of cytochrome b561 by cysteinyl modification with 4, 4-dithiodipyridine J. Biochem. 138 2005 751 762
    • (2005) J. Biochem. , vol.138 , pp. 751-762
    • Takeuchi, F.1    Hori, H.2    Tsubaki, M.3
  • 19
    • 0000740326 scopus 로고    scopus 로고
    • Theoretical and physical characterization
    • J.R. Kincaid Theoretical and physical characterization K.M. Kadish, K.M. Smith, R. Guilard, The Porphyrin Handbook vol. 7 2000 Academic Press New York, NY 225 289
    • (2000) The Porphyrin Handbook , vol.7 , pp. 225-289
    • Kincaid, J.R.1
  • 20
    • 0030467166 scopus 로고    scopus 로고
    • Assignment of protoheme resonance Raman spectra by heme labeling in myoglobin
    • S. Hu, K.M. Smith, and T.G. Spiro Assignment of protoheme resonance Raman spectra by heme labeling in myoglobin J. Am. Chem. Soc. 118 1996 12638 12646
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12638-12646
    • Hu, S.1    Smith, K.M.2    Spiro, T.G.3
  • 21
    • 2842546487 scopus 로고
    • Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins
    • S. Choi, T.G. Spiro, K.C. Langny, K.M. Smith, D.L. Budd, and G.N. La Mar Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins J. Am. Chem. Soc. 104 1982 4345 4351
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4345-4351
    • Choi, S.1    Spiro, T.G.2    Langny, K.C.3    Smith, K.M.4    Budd, D.L.5    La Mar, G.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.