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Volumn 85, Issue 5, 2003, Pages 3367-3374

Role of the Aromatic Ring of Tyr43 in Tetraheme Cytochrome c3 from Desulfovibrio vulgaris Miyazaki F

Author keywords

[No Author keywords available]

Indexed keywords

5 DEAZAFLAVINE DERIVATIVE; AROMATIC COMPOUND; CYTOCHROME C3; HEME DERIVATIVE; HISTIDINE; LEUCINE; RIBOFLAVIN DERIVATIVE; SEMIQUINONE; TETRAHEME; TYROSINE; UNCLASSIFIED DRUG;

EID: 0242322433     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74756-0     Document Type: Article
Times cited : (25)

References (32)
  • 2
    • 0002172471 scopus 로고
    • A. B. Robinson, and N. O. Kaplan, editors. Academic Press, London
    • Ambler, R. P. 1980. From Cyclotrons to Cytochromes. A. B. Robinson, and N. O. Kaplan, editors. Academic Press, London. 263-279.
    • (1980) From Cyclotrons to Cytochromes , pp. 263-279
    • Ambler, R.P.1
  • 4
    • 0028671818 scopus 로고
    • 3 (Mr 26,000) isolated from sulfate-reducing bacteria and its relationships to other polyheme cytochromes from Desulfovibrio
    • 3 (Mr 26,000) isolated from sulfate-reducing bacteria and its relationships to other polyheme cytochromes from Desulfovibrio. Methods Enzymol. 243:140-155.
    • (1994) Methods Enzymol , vol.243 , pp. 140-155
    • Bruschi, M.1
  • 5
    • 0028103275 scopus 로고
    • CCP4 - A suite of programs for protein crystallography
    • Collaborative Computational Project, Number 4, SERC Darebury Laboratory. 1994. CCP4 - a suite of programs for protein crystallography. Acta Cryst. D50:760-763.
    • (1994) Acta Cryst. , vol.D50 , pp. 760-763
  • 7
    • 0028007253 scopus 로고
    • Molecular and structural basis of electron transfer in tetra- and octa-heme cytochromes
    • Czjzek, M., F. Payan, and R. Haser. 1994. Molecular and structural basis of electron transfer in tetra- and octa-heme cytochromes. Biochimie. 76:546-553.
    • (1994) Biochimie , vol.76 , pp. 546-553
    • Czjzek, M.1    Payan, F.2    Haser, R.3
  • 11
    • 0025249781 scopus 로고
    • 3 of Desulfovibrio vulgaris Miyazaki F and partial assignments of heme groups
    • 3 of Desulfovibrio vulgaris Miyazaki F and partial assignments of heme groups. Biochemistry. 29:2257-2263.
    • (1990) Biochemistry , vol.29 , pp. 2257-2263
    • Fan, K.1    Akutsu, H.2    Kyogoku, Y.3    Niki, K.4
  • 13
    • 0028947904 scopus 로고
    • An oligodeoxyribonucleotide-directed dual amber method for site-directed mutagenesis
    • Hashimoto-Gotoh, T., T. Mizuno, Y. Ogasahara, and M. Nakagawa. 1995. An oligodeoxyribonucleotide-directed dual amber method for site-directed mutagenesis. Gene. 152:271-275.
    • (1995) Gene , vol.152 , pp. 271-275
    • Hashimoto-Gotoh, T.1    Mizuno, T.2    Ogasahara, Y.3    Nakagawa, M.4
  • 15
    • 0000526158 scopus 로고
    • 3 from Desulfovibrio vulgaris (Miyazaki F) as determined by nucleotide sequencing of its gene and partial amino acid sequencing
    • 3 from Desulfovibrio vulgaris (Miyazaki F) as determined by nucleotide sequencing of its gene and partial amino acid sequencing. Protein Seq. Data Anal. 5:193-196.
    • (1993) Protein Seq. Data Anal. , vol.5 , pp. 193-196
    • Kitamura, M.1    Ozawa, K.2    Kojima, S.3    Kumagai, I.4    Akutsu, H.5    Miura, K.6
  • 16
    • 0242367024 scopus 로고
    • MOSFILM Vers. 5.41, MRC Laboratory of Molecular Biology
    • Oxford University Press, Oxford, UK
    • Leslie, A. G. W. 1990. MOSFILM Vers. 5.41, MRC Laboratory of Molecular Biology. In Crystallographic Computing. Oxford University Press, Oxford, UK.
    • (1990) Crystallographic Computing
    • Leslie, A.G.W.1
  • 17
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati, V. 1952. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallogr. 5:802-810.
    • (1952) Acta Crystallogr. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 18
    • 0021902977 scopus 로고
    • The structure, function and evolution of cytochromes
    • Mathews, F. S. 1985. The structure, function and evolution of cytochromes. Prog. Biophys. Mol. Biol. 45:1-56.
    • (1985) Prog. Biophys. Mol. Biol. , vol.45 , pp. 1-56
    • Mathews, F.S.1
  • 19
    • 0037033048 scopus 로고    scopus 로고
    • Sulfate respiration in Desulfovibrio vulgaris Hildenborough: Structure of the 16-heme Cytochrome c HmcA at 2.5 Å resolution and a view of its role in transmembrane electron transfer
    • Matias, P. M., A. V. Coelho, F. M. A. Valente, D. Plaido, J. LeGall, A. V. Xavier, I. A. C. Pereira, and M. A. Carrondo. 2002. Sulfate respiration in Desulfovibrio vulgaris Hildenborough: structure of the 16-heme Cytochrome c HmcA at 2.5 Å resolution and a view of its role in transmembrane electron transfer. J. Biol. Chem. 277:47907-47916.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47907-47916
    • Matias, P.M.1    Coelho, A.V.2    Valente, F.M.A.3    Plaido, D.4    LeGall, J.5    Xavier, A.V.6    Pereira, I.A.C.7    Carrondo, M.A.8
  • 24
    • 0035229710 scopus 로고    scopus 로고
    • A simple, rapid, highly efficient gene expression system for multiheme cytochrome c
    • Ozawa, K., F. Yasukawa, Y. Fujiwara, and H. Akutsu. 2001. A simple, rapid, highly efficient gene expression system for multiheme cytochrome c. Biosci. Biotechnol. Biochem. 65:185-189.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 185-189
    • Ozawa, K.1    Yasukawa, F.2    Fujiwara, Y.3    Akutsu, H.4
  • 26
    • 0026084295 scopus 로고
    • Cloning, sequencing, and expression of the gene encoding the high-molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough
    • Pollock, W. B. R., M. Loutfi, M. Bruschi, B. J. Rapp-Giles, J. D. Wall, and G. Voordouw. 1991. Cloning, sequencing, and expression of the gene encoding the high-molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough. J. Bacteriol. 173:220-228.
    • (1991) J. Bacteriol. , vol.173 , pp. 220-228
    • Pollock, W.B.R.1    Loutfi, M.2    Bruschi, M.3    Rapp-Giles, B.J.4    Wall, J.D.5    Voordouw, G.6
  • 28
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • Sheldrick, G. M., and T. R. Schneider. 1997. SHELXL: high-resolution refinement. Methods Enzymol. 277:319-343.
    • (1997) Methods Enzymol. , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 29
    • 0023006777 scopus 로고
    • Elucidation of the factors which determine reaction-rate constants and biological specificity for electron-transfer proteins
    • Tollin, G., T. E. Meyer, and M. A. Cusanovich, 1986. Elucidation of the factors which determine reaction-rate constants and biological specificity for electron-transfer proteins. Biochim. Biophys. Acta. 853:29-41.
    • (1986) Biochim. Biophys. Acta , vol.853 , pp. 29-41
    • Tollin, G.1    Meyer, T.E.2    Cusanovich, M.A.3
  • 31
    • 0025398721 scopus 로고
    • Quality control of protein models: Directional atomic contact analysis
    • Vriend, G. 1990. Quality control of protein models: directional atomic contact analysis. J. Mol. Graph. 8:52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.