메뉴 건너뛰기




Volumn 173, Issue 1, 2000, Pages 29-34

Primary structure of cytochrome c' of Methylococcus capsulatus Bath: Evidence of a phylogenetic link between P460 and c'-type cytochromes

Author keywords

Cytochrome c' Methylococcus capsulatus Bath; Hydroxylamine oxidation; Methanotroph; Methylotroph; Peptide mapping

Indexed keywords

BACTERIAL PROTEIN; CYTOCHROME C OXIDASE; HYDROXYLAMINE; PROTEIN P460; UNCLASSIFIED DRUG;

EID: 0033972007     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050004     Document Type: Article
Times cited : (14)

References (33)
  • 3
    • 0030833664 scopus 로고    scopus 로고
    • Evidence for a crosslink between heme-c and a lsyine residue in cytochrome P460 of Nitrosomonas europaea
    • Arciero DM, Hooper AB (1997) Evidence for a crosslink between heme-c and a lsyine residue in cytochrome P460 of Nitrosomonas europaea. FEBS Lett 410:457-460
    • (1997) FEBS Lett , vol.410 , pp. 457-460
    • Arciero, D.M.1    Hooper, A.B.2
  • 4
    • 0028046264 scopus 로고
    • The primary structure of cytochrome P460 of Nitrosomonas europaea: The presence of a heme-c binding motif
    • Bergmann DJ, Hooper AB (1994) The primary structure of cytochrome P460 of Nitrosomonas europaea: the presence of a heme-c binding motif. FEBS Lett 353:324-326
    • (1994) FEBS Lett , vol.353 , pp. 324-326
    • Bergmann, D.J.1    Hooper, A.B.2
  • 5
    • 0032431903 scopus 로고    scopus 로고
    • Cytochrome P460 genes from the methanotroph Methylococcus capsulatus Bath
    • Bergman DJ, Zahn JA, Hooper AB, DiSpirito AA (1998) Cytochrome P460 genes from the methanotroph Methylococcus capsulatus Bath. J Bacteriol 180 : 6440-6445
    • (1998) J Bacteriol , vol.180 , pp. 6440-6445
    • Bergman, D.J.1    Zahn, J.A.2    Hooper, A.B.3    DiSpirito, A.A.4
  • 6
    • 0025007137 scopus 로고
    • Soluble cytochromes c from Methylomonas A4
    • DiSpirito AA (1990) Soluble cytochromes c from Methylomonas A4. Methods Enzymol 188: 289-297
    • (1990) Methods Enzymol , vol.188 , pp. 289-297
    • DiSpirito, A.A.1
  • 7
    • 0021832269 scopus 로고
    • Carbon monoxide binding to Rhodobacter capsulatus cytochrome c′
    • Doyle ML, Weber PC, Gill SJ (1985) Carbon monoxide binding to Rhodobacter capsulatus cytochrome c′. Biochemistry 24 : 1987-1991
    • (1985) Biochemistry , vol.24 , pp. 1987-1991
    • Doyle, M.L.1    Weber, P.C.2    Gill, S.J.3
  • 8
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction enzyme fragments to high specific activity
    • Feinburg AP, Volgelstein B (1983) A technique for radiolabeling DNA restriction enzyme fragments to high specific activity. Anal Biochem 132 : 6-13
    • (1983) Anal Biochem , vol.132 , pp. 6-13
    • Feinburg, A.P.1    Volgelstein, B.2
  • 9
    • 0022419653 scopus 로고
    • Structure of ferricytochrome c′ from Rhodospirillum molischianum at 1.6 Å resolution
    • Finzel BC, Weber PC, Hardman KD, Salemme FR (1985) Structure of ferricytochrome c′ from Rhodospirillum molischianum at 1.6 Å resolution. J Mol Biol 186 : 627-643
    • (1985) J Mol Biol , vol.186 , pp. 627-643
    • Finzel, B.C.1    Weber, P.C.2    Hardman, K.D.3    Salemme, F.R.4
  • 12
    • 0025903765 scopus 로고
    • Ligand binding properties of cytochrome c′
    • Kassner RJ (1970) Ligand binding properties of cytochrome c′ Biochim Biophys Acta 1058 : 8-12
    • (1970) Biochim Biophys Acta , vol.1058 , pp. 8-12
    • Kassner, R.J.1
  • 13
    • 0019904249 scopus 로고
    • Wide host range cloning vectors: Cosmid clone bank of Agrobacterium Ti plasmids
    • Knauf CV, Nester EW (1982) Wide host range cloning vectors: cosmid clone bank of Agrobacterium Ti plasmids. Plasmid 8 : 45-54
    • (1982) Plasmid , vol.8 , pp. 45-54
    • Knauf, C.V.1    Nester, E.W.2
  • 14
    • 0017129914 scopus 로고
    • The spin 3/2 state and quantum spin mixtures in haeme proteins
    • Maltempo MM, Moss TH (1976) The spin 3/2 state and quantum spin mixtures in haeme proteins. Q Rev Biophys 9 : 181-215
    • (1976) Q Rev Biophys , vol.9 , pp. 181-215
    • Maltempo, M.M.1    Moss, T.H.2
  • 15
    • 0019631649 scopus 로고
    • Detection of cytochrome f, a c-class cytochrome, with diaminobenzidine in polyacrylamide gels
    • McDonnel A, Staehelin LA (1981) Detection of cytochrome f, a c-class cytochrome, with diaminobenzidine in polyacrylamide gels. Anal Biochem 117 : 40-44
    • (1981) Anal Biochem , vol.117 , pp. 40-44
    • McDonnel, A.1    Staehelin, L.A.2
  • 16
    • 0025237588 scopus 로고
    • Crystallization and characterization of Chromatium vinosum cytochrome c′
    • McRee DA, Redford SM, Meyer TE, Cusanovich MA (1990) Crystallization and characterization of Chromatium vinosum cytochrome c′. J Biol Chem 265:5364-5365
    • (1990) J Biol Chem , vol.265 , pp. 5364-5365
    • McRee, D.A.1    Redford, S.M.2    Meyer, T.E.3    Cusanovich, M.A.4
  • 17
    • 0020453669 scopus 로고
    • New perspectives on c-type cytochromes
    • Meyer TE, Kamen MD (1982) New perspectives on c-type cytochromes. Adv Prot Chem 35:105-212
    • (1982) Adv Prot Chem , vol.35 , pp. 105-212
    • Meyer, T.E.1    Kamen, M.D.2
  • 20
    • 0029884241 scopus 로고    scopus 로고
    • Regulation of bacterial methane oxidation: Transcription of the soluble methane monooxygenase operon of Methylococcus capsulatus (Bath) is repressed by copper ions
    • Nielsen AK, Gerdes K, Degn H, Murrell JC (1996) Regulation of bacterial methane oxidation: transcription of the soluble methane monooxygenase operon of Methylococcus capsulatus (Bath) is repressed by copper ions. Microbiology 142 : 1289-1296
    • (1996) Microbiology , vol.142 , pp. 1289-1296
    • Nielsen, A.K.1    Gerdes, K.2    Degn, H.3    Murrell, J.C.4
  • 21
    • 0027380310 scopus 로고
    • Atomic structure of a cytochrome c′ with and unusual ligand-controlled dimer dissociation at 1.8 Å resolution
    • Ren Z, Meyer T, McRee DE (1993) Atomic structure of a cytochrome c′ with and unusual ligand-controlled dimer dissociation at 1.8 Å resolution. J Mol Biol 234 : 433-445
    • (1993) J Mol Biol , vol.234 , pp. 433-445
    • Ren, Z.1    Meyer, T.2    McRee, D.E.3
  • 23
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range 1-100 kD
    • Schagger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range 1-100 kD. Ann Biochem 166 : 368-379
    • (1987) Ann Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 24
    • 0025119754 scopus 로고
    • Spectral characterization of c-type cytochromes purified from Beggiatoa alba
    • Schmidt TM, DiSpirito AA (1990) Spectral characterization of c-type cytochromes purified from Beggiatoa alba. Arch Microbiol 154 : 453-458
    • (1990) Arch Microbiol , vol.154 , pp. 453-458
    • Schmidt, T.M.1    DiSpirito, A.A.2
  • 25
    • 0017828994 scopus 로고
    • Cytochrome c from Schizosaccharomyces pombe. 2. Amino acid sequence
    • Simon-Becam AM, Claisse M, Eederer F (1978) Cytochrome c from Schizosaccharomyces pombe. 2. Amino acid sequence. Eur J Biochem 86 : 407-416
    • (1978) Eur J Biochem , vol.86 , pp. 407-416
    • Simon-Becam, A.M.1    Claisse, M.2    Eederer, F.3
  • 26
    • 0001740731 scopus 로고
    • Spectral properties of carbon monoxide or cyanide complexes of cytochrome c′ from denitrifying bacteria
    • Suzuki S, Nakahara A, Yoshimura T, Iwasaki H, Shidara S, Matsubara T (1988) Spectral properties of carbon monoxide or cyanide complexes of cytochrome c′ from denitrifying bacteria. Inorg Chim Acta 153 : 227-233
    • (1988) Inorg Chim Acta , vol.153 , pp. 227-233
    • Suzuki, S.1    Nakahara, A.2    Yoshimura, T.3    Iwasaki, H.4    Shidara, S.5    Matsubara, T.6
  • 27
    • 0029940242 scopus 로고    scopus 로고
    • High resolution crystal structure of two polymorphs of cytochrome c′ from the purple phototrophic bacterium Rhodobacter capsulatus
    • Tahirov TH, Misaki S, Meyer TE, Cusanovitch MA, Higuchi Y, Yasuoka N (1996) High resolution crystal structure of two polymorphs of cytochrome c′ from the purple phototrophic bacterium Rhodobacter capsulatus. J Mol Biol 259 : 467-479
    • (1996) J Mol Biol , vol.259 , pp. 467-479
    • Tahirov, T.H.1    Misaki, S.2    Meyer, T.E.3    Cusanovitch, M.A.4    Higuchi, Y.5    Yasuoka, N.6
  • 28
    • 0019873792 scopus 로고
    • Crystallographic structure of rhodospirillum molischianum ferricytochrome c′ at 2.5 Å resolution
    • Weber PC, Howard A, Xuong NH, Salemme FR (1981) Crystallographic structure of Rhodospirillum molischianum ferricytochrome c′ at 2.5 Å resolution. J Mol Biol 153:399-424
    • (1981) J Mol Biol , vol.153 , pp. 399-424
    • Weber, P.C.1    Howard, A.2    Xuong, N.H.3    Salemme, F.R.4
  • 29
    • 0021766171 scopus 로고
    • Bacterial proteins with CO-binding b or c-type haem functions and absorption spectroscopy
    • Wood PM (1984) Bacterial proteins with CO-binding b or c-type haem functions and absorption spectroscopy. Biochim Biophys Acta 768 : 293-317
    • (1984) Biochim Biophys Acta , vol.768 , pp. 293-317
    • Wood, P.M.1
  • 30
    • 0026598140 scopus 로고
    • Three dimensional structure of ferricytochrome c′ from Rhodospirillum rubrum at 2.8 Å resolution
    • Yasui M, Harada S, Kai Y, Kasai N, Kusanoki M, Matsuura Y (1992) Three dimensional structure of ferricytochrome c′ from Rhodospirillum rubrum at 2.8 Å resolution. J Biochem 111 : 317-324
    • (1992) J Biochem , vol.111 , pp. 317-324
    • Yasui, M.1    Harada, S.2    Kai, Y.3    Kasai, N.4    Kusanoki, M.5    Matsuura, Y.6
  • 31
    • 0028131263 scopus 로고
    • Oxidation of hydroxylamine by cytochrome P-460 of the obligate methylotroph Methylococcus capsulatus Bath
    • Zahn JA, Duncan C, DiSpirito AA (1994) Oxidation of hydroxylamine by cytochrome P-460 of the obligate methylotroph Methylococcus capsulatus Bath. J Bacteriol 176:5879-5887
    • (1994) J Bacteriol , vol.176 , pp. 5879-5887
    • Zahn, J.A.1    Duncan, C.2    DiSpirito, A.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.