메뉴 건너뛰기




Volumn 134, Issue 6, 2003, Pages 859-867

Reversely-Oriented Cytochrome b561 in Reconstituted Vesicles Catalyzes Transmembrane Electron Transfer and Supports Extravesicular Dopamine β-Hydroxylase Activity

Author keywords

Ascorbate; Cytochrome b561; Dopamine hydroxylase; Reconstituted vesicle; Transmembrane electron transfer

Indexed keywords

CHOLESTEROL; CYTOCHROME B; CYTOCHROME B561; CYTOCHROME C; DETERGENT; DIETHYL PYROCARBONATE; DOPAMINE BETA MONOOXYGENASE; FERRICYANIDE; HEME B; HEME DERIVATIVE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL; THIAZOLE BLUE; THIAZOLE DERIVATIVE; TRYPSIN; TYRAMINE; UNCLASSIFIED DRUG;

EID: 1342283140     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvg212     Document Type: Article
Times cited : (15)

References (37)
  • 1
    • 0020803454 scopus 로고
    • Identification in pituitary tissue of a peptide α-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic acid
    • Eipper, B.A., Mains, R.E., and Glembotski, C.C. (1983) Identification in pituitary tissue of a peptide α-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic acid. Proc. Natl Acad. Sci. USA 80, 5144-5148
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5144-5148
    • Eipper, B.A.1    Mains, R.E.2    Glembotski, C.C.3
  • 2
    • 0023655324 scopus 로고
    • 561 catalyzes transmembrane electron transfer for dopamine β-hydroxylase and peptidyl glycine α-amidating monooxygenase activities in reconstituted systems
    • 561 catalyzes transmembrane electron transfer for dopamine β-hydroxylase and peptidyl glycine α-amidating monooxygenase activities in reconstituted systems. J. Biol. Chem. 262, 8174-8178
    • (1987) J. Biol. Chem. , vol.262 , pp. 8174-8178
    • Kent, U.M.1    Fleming, P.J.2
  • 3
    • 0025850585 scopus 로고
    • Semidehydroascorbic acid as an intermediate in norepinephrine biosynthesis in chromaffin granules
    • Dhariwal, K.R., Black, C.D.V., and Lavine, M. (1991) Semidehydroascorbic acid as an intermediate in norepinephrine biosynthesis in chromaffin granules. J. Biol. Chem. 266, 12908-12914
    • (1991) J. Biol. Chem. , vol.266 , pp. 12908-12914
    • Dhariwal, K.R.1    Black, C.D.V.2    Lavine, M.3
  • 4
    • 0020657388 scopus 로고
    • Electron transfer across the chromaffin granule membrane
    • Njus, D., Knoth, J., Cook, C., and Kelley, P.M. (1983) Electron transfer across the chromaffin granule membrane. J. Biol. Chem. 258, 27-30
    • (1983) J. Biol. Chem. , vol.258 , pp. 27-30
    • Njus, D.1    Knoth, J.2    Cook, C.3    Kelley, P.M.4
  • 6
    • 0022971533 scopus 로고
    • Functional coupling between enzymes of the chromaffin granule membrane
    • Wakefield, L.M., Cass, A.E.G., and Radda, G.K. (1986) Functional coupling between enzymes of the chromaffin granule membrane. J. Biol. Chem. 261, 9739-9745
    • (1986) J. Biol. Chem. , vol.261 , pp. 9739-9745
    • Wakefield, L.M.1    Cass, A.E.G.2    Radda, G.K.3
  • 7
    • 0029013274 scopus 로고
    • 5 reductase gene results in immunologically undetectable enzyme and impaired NADH-dependent ascorbate regeneration in cultured fibroblasts of a patient with type II hereditary methemoglobinemia
    • 5 reductase gene results in immunologically undetectable enzyme and impaired NADH-dependent ascorbate regeneration in cultured fibroblasts of a patient with type II hereditary methemoglobinemia. Amer. J. Hum. Genet. 57, 302-310
    • (1995) Amer. J. Hum. Genet. , vol.57 , pp. 302-310
    • Shirabe, K.1    Landi, M.T.2    Takeshita, M.3    Uziel, G.4    Fedrizzi, E.5    Borgese, N.6
  • 8
    • 0025028991 scopus 로고
    • 5-Methylphenazinium methylsufate mediates cyclic electron flow and proton gradient dissipation in chromaffin-vesicle membranes
    • Harnadek, G., Ries, E.A., Farhat, A., and Njus, D. (1990) 5-Methylphenazinium methylsufate mediates cyclic electron flow and proton gradient dissipation in chromaffin-vesicle membranes. J. Biol. Chem. 265, 18135-18141
    • (1990) J. Biol. Chem. , vol.265 , pp. 18135-18141
    • Harnadek, G.1    Ries, E.A.2    Farhat, A.3    Njus, D.4
  • 9
    • 0022931515 scopus 로고
    • 561 spectral changes associated with electron transfer in chromaffin-vesicle ghosts
    • 561 spectral changes associated with electron transfer in chromaffin-vesicle ghosts. J. Biol. Chem. 261, 6429-6432
    • (1986) J. Biol. Chem. , vol.261 , pp. 6429-6432
    • Kelley, P.M.1    Njus, D.2
  • 11
    • 0030817141 scopus 로고    scopus 로고
    • 561 from bovine adrenal chromaffin vesicles as revealed by a new purification procedure and EPR spectroscopy
    • 561 from bovine adrenal chromaffin vesicles as revealed by a new purification procedure and EPR spectroscopy. J. Biol. Chem. 272, 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
  • 12
    • 0035936858 scopus 로고    scopus 로고
    • Chromaffin granule membranes contain at least three heme centers: Direct evidence from EPR and absorption spectroscopy
    • Kamensky, Y.A. and Palmer, G. (2001) Chromaffin granule membranes contain at least three heme centers: direct evidence from EPR and absorption spectroscopy. FEBS Lett. 491, 119-122
    • (2001) FEBS Lett. , vol.491 , pp. 119-122
    • Kamensky, Y.A.1    Palmer, G.2
  • 13
    • 0028172069 scopus 로고
    • 561: A revised hypothesis for conformation in membranes which reconciles sequence and functional information
    • 561: A revised hypothesis for conformation in membranes which reconciles sequence and functional information. Biochem. J. 303, 915-921
    • (1994) Biochem. J. , vol.303 , pp. 915-921
    • Srivastava, M.1    Gibson, K.R.2    Pollard, H.B.3    Fleming, P.J.4
  • 17
    • 0032568938 scopus 로고    scopus 로고
    • 561 from bovine adrenal chromaffin vesicles as revealed by pulse radiolysis
    • 561 from bovine adrenal chromaffin vesicles as revealed by pulse radiolysis. J. Biol. Chem. 273, 16038-16042
    • (1998) J. Biol. Chem. , vol.273 , pp. 16038-16042
    • Kobayashi, K.1    Tsubaki, M.2    Tagawa, S.3
  • 18
    • 0034724254 scopus 로고    scopus 로고
    • 561 from ascorbate but does not influence on electron donation to monodehydroascorbate radical: Distinct roles of two heme centers for electron transfer across the chromaffin vesicle membranes
    • 561 from ascorbate but does not influence on electron donation to monodehydroascorbate radical: Distinct roles of two heme centers for electron transfer across the chromaffin vesicle membranes. Biochemistry 39, 3276-3284
    • (2000) Biochemistry , vol.39 , pp. 3276-3284
    • Tsubaki, M.1    Kobayashi, K.2    Ichise, T.3    Takeuchi, F.4    Tagawa, S.5
  • 21
    • 0021289369 scopus 로고
    • An identical cytochrome b561 is present in bovine adrenal chromaffin vesicles and posterior pituitary neurosecretory vesicles
    • Duong, L.T., Fleming, P.J., and Russell, J.T. (1984) An identical cytochrome b561 is present in bovine adrenal chromaffin vesicles and posterior pituitary neurosecretory vesicles. J. Biol. Chem. 259, 4885-4889
    • (1984) J. Biol. Chem. , vol.259 , pp. 4885-4889
    • Duong, L.T.1    Fleming, P.J.2    Russell, J.T.3
  • 22
    • 0023161655 scopus 로고
    • 561 can be detected in many neuroendocrine tissues using a specific monoclonal antibody
    • 561 can be detected in many neuroendocrine tissues using a specific monoclonal antibody. Neuroscience 22, 149-157
    • (1987) Neuroscience , vol.22 , pp. 149-157
    • Pruss, R.M.1    Shepard, E.A.2
  • 23
    • 0035880488 scopus 로고    scopus 로고
    • Domain homologues of dopamine β-hydroxylase and ferric reductase: Roles for iron metabolism in neurodegenerative disorders?
    • Ponting, C.P. (2001) Domain homologues of dopamine β-hydroxylase and ferric reductase: roles for iron metabolism in neurodegenerative disorders? Hum. Mol. Genet. 10, 1853-1858
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1853-1858
    • Ponting, C.P.1
  • 26
    • 0017252387 scopus 로고
    • Purification and characterization of dopamine β-hydroxylase from bovine adrenal medulla
    • Ljones, T., Skotland, T., and Flatmark, T. (1976) Purification and characterization of dopamine β-hydroxylase from bovine adrenal medulla. Eur. J. Biochem. 61, 525-533
    • (1976) Eur. J. Biochem. , vol.61 , pp. 525-533
    • Ljones, T.1    Skotland, T.2    Flatmark, T.3
  • 29
    • 0024077919 scopus 로고
    • The structure of cytochrome b561, a secretory vesicle-specific electron transport protein
    • Perin, M.S., Fried, V.A., Slaughter, C.A., and Südhof, T.C. (1988) The structure of cytochrome b561, a secretory vesicle-specific electron transport protein. EMBO J. 7, 2697-2703
    • (1988) EMBO J. , vol.7 , pp. 2697-2703
    • Perin, M.S.1    Fried, V.A.2    Slaughter, C.A.3    Südhof, T.C.4
  • 30
    • 0038687193 scopus 로고    scopus 로고
    • 561 is not fatty acylated but acetylated at the amino terminus in the chromaffin vesicle membranes: An approach for identification of the posttranslational modification of transmembrane proteins
    • 561 is not fatty acylated but acetylated at the amino terminus in the chromaffin vesicle membranes: An approach for identification of the posttranslational modification of transmembrane proteins. Protoplasma 221, 41-46
    • (2003) Protoplasma , vol.221 , pp. 41-46
    • Nakamura, M.1    Takeuchi, F.2    Tsubaki, M.3
  • 32
    • 0029666227 scopus 로고    scopus 로고
    • Physical properties of hemoglobin vesicles as red cell substitutes
    • Sakai, H., Hamada, K., Takeoka, S., Nishide, H., and Tsuchida, E. (1996) Physical properties of hemoglobin vesicles as red cell substitutes. Biotechnol. Prog. 12, 119-125
    • (1996) Biotechnol. Prog. , vol.12 , pp. 119-125
    • Sakai, H.1    Hamada, K.2    Takeoka, S.3    Nishide, H.4    Tsuchida, E.5
  • 34
    • 0021923851 scopus 로고
    • An electron transfer dependent membrane potential in chromaffin-vesicle ghosts
    • Harnadek, G.J., Callahan, R.E., Barone, A.R., and Njus, D. (1985) An electron transfer dependent membrane potential in chromaffin-vesicle ghosts. Biochemistry 24, 384-389
    • (1985) Biochemistry , vol.24 , pp. 384-389
    • Harnadek, G.J.1    Callahan, R.E.2    Barone, A.R.3    Njus, D.4
  • 35
    • 0018827418 scopus 로고
    • Subcellular distribution of ascorbate in bovine adrenal medulla Evidence for accumulation in chromaffin granules against a concentration gradient
    • Ingebretsen, O.C., Terland, O., and Flatmark, T. (1980) Subcellular distribution of ascorbate in bovine adrenal medulla Evidence for accumulation in chromaffin granules against a concentration gradient. Biochim. Biophys. Acta 628, 182-189
    • (1980) Biochim. Biophys. Acta , vol.628 , pp. 182-189
    • Ingebretsen, O.C.1    Terland, O.2    Flatmark, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.