메뉴 건너뛰기




Volumn 46, Issue 29, 2007, Pages 8647-8658

Axial ligation and stoichiometry of heme centers in adrenal cytochrome b561

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; ELECTRON SPIN RESONANCE SPECTROSCOPY; EMISSION SPECTROSCOPY; MUTAGENESIS; SPECTROSCOPIC ANALYSIS; STOICHIOMETRY;

EID: 34547105283     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700054g     Document Type: Article
Times cited : (22)

References (77)
  • 1
    • 27844441716 scopus 로고    scopus 로고
    • 561 protein family: Expanding roles and versatile transmembrane electron transfer abilities as predicted by a new classification system and protein sequence motif analyses
    • 561 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 1753, 174-190.
    • (2005) Biochim. Biophys. Acta , vol.1753 , pp. 174-190
    • Tsubaki, M.1    Takeuchi, F.2    Nakanishi, N.3
  • 4
    • 1442291188 scopus 로고    scopus 로고
    • 561 and potentially involved in catecholamine biochemistry in plants
    • 561 and potentially involved in catecholamine biochemistry in plants, J. Plant Physiol. 161, 175-181.
    • (2004) J. Plant Physiol , vol.161 , pp. 175-181
    • Verelst, W.1    Asard, H.2
  • 6
    • 33645637817 scopus 로고    scopus 로고
    • The copper-enzyme family of dopamine β-monooxygenase and peptidylglycine α-hydroxylating monooxygenase: Resolving the chemical pathway for substrate hydroxylation
    • Klinman, J. P. (2006) The copper-enzyme family of dopamine β-monooxygenase and peptidylglycine α-hydroxylating monooxygenase: Resolving the chemical pathway for substrate hydroxylation, J. Biol. Chem. 281, 3013-3016.
    • (2006) J. Biol. Chem , vol.281 , pp. 3013-3016
    • Klinman, J.P.1
  • 7
    • 0035880488 scopus 로고    scopus 로고
    • Domain homologues of dopamine β-hydroxylase and ferric reductase: Roles for iron methabolism in neurodegenerative disorders?
    • Ponting, C. P. (2001) Domain homologues of dopamine β-hydroxylase and ferric reductase: Roles for iron methabolism in neurodegenerative disorders? Hum. Mol. Genet. 10, 1853-1858.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1853-1858
    • Ponting, C.P.1
  • 10
    • 33947422966 scopus 로고    scopus 로고
    • 561 with trans-membrane ferrireductase capability
    • 561 with trans-membrane ferrireductase capability, FEBS Lett. 581, 1505-1508.
    • (2007) FEBS Lett , vol.581 , pp. 1505-1508
    • Berczi, A.1    Su, D.2    Asard, H.3
  • 13
    • 28844447007 scopus 로고    scopus 로고
    • The role of duodenal cytochrome b
    • intestinal iron absorption remains unclear, 4413 and author reply 4414
    • Frazer, D. M., Wilkins, S. J., Vulpe, C. D., and Anderson, G. J. (2005) The role of duodenal cytochrome b in intestinal iron absorption remains unclear, Blood 106, 4413 and author reply 4414.
    • (2005) Blood 106
    • Frazer, D.M.1    Wilkins, S.J.2    Vulpe, C.D.3    Anderson, G.J.4
  • 15
    • 33845979527 scopus 로고    scopus 로고
    • 561 that may be involved in extracellular ascorbate recycling
    • 561 that may be involved in extracellular ascorbate recycling, J. Biol. Chem. 281, 39852-39859.
    • (2006) J. Biol. Chem , vol.281 , pp. 39852-39859
    • Su, D.1    May, J.M.2    Koury, M.J.3    Asard, H.4
  • 16
    • 0036569946 scopus 로고    scopus 로고
    • Expression of several genes in the human chromosome 3p21.3 homozygous deletion region by an adenovirus vector results in tumor suppressor activities in vitro and in vivo
    • Ji, L., Nishizaki, M., Gao, B., Burbee, D., Kondo, M., Kamibayashi, C., Xu, K., Yen, N., Atkinson, E. N., Fang, B., Lerman, M. I., Roth, J. A., and Minna, J. D. (2002) Expression of several genes in the human chromosome 3p21.3 homozygous deletion region by an adenovirus vector results in tumor suppressor activities in vitro and in vivo, Cancer Res. 62, 2715-2720.
    • (2002) Cancer Res , vol.62 , pp. 2715-2720
    • Ji, L.1    Nishizaki, M.2    Gao, B.3    Burbee, D.4    Kondo, M.5    Kamibayashi, C.6    Xu, K.7    Yen, N.8    Atkinson, E.N.9    Fang, B.10    Lerman, M.I.11    Roth, J.A.12    Minna, J.D.13
  • 17
    • 34447128187 scopus 로고    scopus 로고
    • Tumor suppressor 101F6 and ascorbate synergistically and selectively inhibit non-small cell lung cancer growth by caspase-independent apoptosis and autophagy
    • in press
    • Ohtani, S., Ueda, K., Jayachandran, G., Xu, K., Minna, J. D., Roth, J., and Ji, L. (2007) Tumor suppressor 101F6 and ascorbate synergistically and selectively inhibit non-small cell lung cancer growth by caspase-independent apoptosis and autophagy. Cancer Res. 67, in press.
    • (2007) Cancer Res , vol.67
    • Ohtani, S.1    Ueda, K.2    Jayachandran, G.3    Xu, K.4    Minna, J.D.5    Roth, J.6    Ji, L.7
  • 18
    • 0001089191 scopus 로고    scopus 로고
    • Membrane and soluble proteins of adrenal chromaffin granules
    • Apps, D. K. (1997) Membrane and soluble proteins of adrenal chromaffin granules, Semin. Cell Dev. Biol. 8, 121-131.
    • (1997) Semin. Cell Dev. Biol , vol.8 , pp. 121-131
    • Apps, D.K.1
  • 23
    • 0018965590 scopus 로고
    • Direct spectrophotometric detection of ascorbate free radical formed by dopamine β-monooxygenase and by ascorbate oxidase
    • Skotland, T., and Ljones, T. (1980) Direct spectrophotometric detection of ascorbate free radical formed by dopamine β-monooxygenase and by ascorbate oxidase, Biochim. Biophys. Acta 630, 30-35.
    • (1980) Biochim. Biophys. Acta , vol.630 , pp. 30-35
    • Skotland, T.1    Ljones, T.2
  • 24
    • 0018395103 scopus 로고
    • The uptake of ascorbic acid and dehydroascorbic acid by chromaffin granules of the adrenal medulla
    • Tirrell, J. G., and Westhead, E. W. (1979) The uptake of ascorbic acid and dehydroascorbic acid by chromaffin granules of the adrenal medulla, Neuroscience 4, 181-186.
    • (1979) Neuroscience , vol.4 , pp. 181-186
    • Tirrell, J.G.1    Westhead, E.W.2
  • 26
    • 0022350362 scopus 로고
    • Enhancement of norepinephrine biosynthesis by ascorbic acid in cultured bovine chromaffin cells
    • Levine, M., Morita, K., and Pollard, H. (1985) Enhancement of norepinephrine biosynthesis by ascorbic acid in cultured bovine chromaffin cells, J. Biol. Chem. 260, 12942-12947.
    • (1985) J. Biol. Chem , vol.260 , pp. 12942-12947
    • Levine, M.1    Morita, K.2    Pollard, H.3
  • 27
    • 0019225842 scopus 로고
    • 561 is identical with chromomembrin B, a major polypeptide of chromaffin granule membranes
    • 561 is identical with chromomembrin B, a major polypeptide of chromaffin granule membranes, Neuroscience 5, 2279-2287.
    • (1980) Neuroscience , vol.5 , pp. 2279-2287
    • Apps, D.K.1    Pryde, J.G.2    Phillips, J.H.3
  • 28
    • 34547100616 scopus 로고
    • The chromaffin granule: Proton-cycling in the slow lane
    • Skulachev, V. P, and Hinkle, P. C, Eds, pp, Addison-Wesley Publishing Company, Inc, Reading, MA
    • Njus, D., Zallakian, M., and Knoth, J. (1981) The chromaffin granule: Proton-cycling in the slow lane, in Chemiosmotic Proton Circuits in Biological Membranes (Skulachev, V. P., and Hinkle, P. C., Eds.) pp 365-374, Addison-Wesley Publishing Company, Inc., Reading, MA.
    • (1981) Chemiosmotic Proton Circuits in Biological Membranes , pp. 365-374
    • Njus, D.1    Zallakian, M.2    Knoth, J.3
  • 29
    • 0023001148 scopus 로고
    • Electron transfer across the chromaffin granule membrane. Use of EPR to demonstrate reduction of intravesicular ascorbate radical by the extravesicular mitochondrial NADH:ascorbate radical oxidoreductase
    • Wakefield, L. M., Cass, A. E., and Radda, G. K. (1986) Electron transfer across the chromaffin granule membrane. Use of EPR to demonstrate reduction of intravesicular ascorbate radical by the extravesicular mitochondrial NADH:ascorbate radical oxidoreductase, J. Biol. Chem. 261, 9746-9752.
    • (1986) J. Biol. Chem , vol.261 , pp. 9746-9752
    • Wakefield, L.M.1    Cass, A.E.2    Radda, G.K.3
  • 30
    • 0022971533 scopus 로고
    • Functional coupling between enzymes of the chromaffin granule membrane
    • Wakefield, L. M., Cass, A. E., 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.2    Radda, G.K.3
  • 32
    • 0023009792 scopus 로고
    • Evidence for an ascorbate shuttle for the transfer of reducing equivalents across chromaffin granule membranes
    • Beers, M. F., Johnson, R. G., and Scarpa, A. (1986) Evidence for an ascorbate shuttle for the transfer of reducing equivalents across chromaffin granule membranes, J. Biol. Chem. 261, 2529-2535.
    • (1986) J. Biol. Chem , vol.261 , pp. 2529-2535
    • Beers, M.F.1    Johnson, R.G.2    Scarpa, A.3
  • 34
    • 0034724254 scopus 로고    scopus 로고
    • 561 from ascorbate but does not influence electron donation to monodehydroascorbate radical: Identification of the modification sites by mass spectrometric analysis
    • 561 from ascorbate but does not influence electron donation to monodehydroascorbate radical: identification of the modification sites by mass spectrometric analysis, 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
  • 37
    • 0016237981 scopus 로고
    • 561. An integral heme protein of the adrenal chromaffin granule membrane
    • 561. An integral heme protein of the adrenal chromaffin granule membrane, Biochim. Biophys. Acta 395, 257-266.
    • (1974) Biochim. Biophys. Acta , vol.395 , pp. 257-266
    • Silsand, T.1    Flatmark, T.2
  • 38
    • 0020479391 scopus 로고
    • 561 from bovine adrenal chromaffin granules
    • 561 from bovine adrenal chromaffin granules, J. Biol. Chem. 257, 8561-8564.
    • (1982) J. Biol. Chem , vol.257 , pp. 8561-8564
    • Duong, L.T.1    Fleming, P.J.2
  • 40
    • 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
  • 42
    • 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
  • 46
    • 0014077241 scopus 로고
    • Electronic spectrum of single crystals of ferricytochrome c
    • Eaton, W. A., and Hochstrasser, R. M. (1967) Electronic spectrum of single crystals of ferricytochrome c, J. Chem. Phys. 46, 2533-2539.
    • (1967) J. Chem. Phys , vol.46 , pp. 2533-2539
    • Eaton, W.A.1    Hochstrasser, R.M.2
  • 47
    • 0018199012 scopus 로고
    • 562 from E. coli: Conformational, configurational, and spin-state characterization
    • 562 from E. coli: Conformational, configurational, and spin-state characterization, Biochemistry 17, 3723-3729.
    • (1978) Biochemistry , vol.17 , pp. 3723-3729
    • Myer, Y.P.1    Bullock, P.A.2
  • 48
    • 0015733210 scopus 로고
    • Fine structure of the magnetooptical rotatory dispersion curves and the surroundings of heme in ferrocytochrome c and its model compounds
    • Arutyunyan, A. M., and Sharonov, Y. A. (1974) Fine structure of the magnetooptical rotatory dispersion curves and the surroundings of heme in ferrocytochrome c and its model compounds, Mol. Biol. 7, 478-484.
    • (1974) Mol. Biol , vol.7 , pp. 478-484
    • Arutyunyan, A.M.1    Sharonov, Y.A.2
  • 50
    • 0000187126 scopus 로고    scopus 로고
    • Electron paramagnetic resonance of metalloproteins
    • Que, L, Ed, pp, University Science Books, Sausalito, CA
    • Palmer, G. (2000) Electron paramagnetic resonance of metalloproteins, in Physical Methods in Bioinorganic Chemistry (Que, L., Ed.) pp 121 -186, University Science Books, Sausalito, CA.
    • (2000) Physical Methods in Bioinorganic Chemistry , pp. 121-186
    • Palmer, G.1
  • 51
    • 1042265206 scopus 로고    scopus 로고
    • Identification of Tyr504 as an alternative tyrosyl radical site in human prostaglandin H synthase-2
    • Rogge, C. E., Liu, W., Wu, G., Wang, L. H., Kulmacz, R. J., and Tsai, A. L. (2004) Identification of Tyr504 as an alternative tyrosyl radical site in human prostaglandin H synthase-2, Biochemistry 43, 1560-1568.
    • (2004) Biochemistry , vol.43 , pp. 1560-1568
    • Rogge, C.E.1    Liu, W.2    Wu, G.3    Wang, L.H.4    Kulmacz, R.J.5    Tsai, A.L.6
  • 52
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A., and Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra, Anal. Biochem. 161, 1-15.
    • (1987) Anal. Biochem , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 54
    • 0030824517 scopus 로고    scopus 로고
    • Carson, M. (1997) Ribbons, Methods Enzymol. 277, 493-505.
    • Carson, M. (1997) Ribbons, Methods Enzymol. 277, 493-505.
  • 55
    • 0015866513 scopus 로고
    • Rapid adiabatic passage EPR of ferricytochrome c: Signal enhancement and determination of the spin-lattice relaxation time
    • Mailer, C., and Taylor, C. P. (1973) Rapid adiabatic passage EPR of ferricytochrome c: Signal enhancement and determination of the spin-lattice relaxation time, Biochim. Biophys. Acta 322, 195-203.
    • (1973) Biochim. Biophys. Acta , vol.322 , pp. 195-203
    • Mailer, C.1    Taylor, C.P.2
  • 57
    • 0034713845 scopus 로고    scopus 로고
    • The distal heme center in Bacillus subtilis succinate:quinone reductase is crucial for electron transfer to menaquinone
    • Matsson, M., Tolstoy, D., Aasa, R., and Hederstedt, L. (2000) The distal heme center in Bacillus subtilis succinate:quinone reductase is crucial for electron transfer to menaquinone, Biochemistry 39, 8617-8624.
    • (2000) Biochemistry , vol.39 , pp. 8617-8624
    • Matsson, M.1    Tolstoy, D.2    Aasa, R.3    Hederstedt, L.4
  • 59
    • 0017579936 scopus 로고
    • Multiple low spin forms of the cytochrome c ferrihemochrome. EPR spectra of various eukaryotic and prokaryotic cytochromes c
    • Brautigan, D. L., Feinberg, B. A., Hoffman, B. M., Margoliash, E., Peisach, J., and Blumberg, W. E. (1977) Multiple low spin forms of the cytochrome c ferrihemochrome. EPR spectra of various eukaryotic and prokaryotic cytochromes c, J. Biol. Chem. 252, 574-582.
    • (1977) J. Biol. Chem , vol.252 , pp. 574-582
    • Brautigan, D.L.1    Feinberg, B.A.2    Hoffman, B.M.3    Margoliash, E.4    Peisach, J.5    Blumberg, W.E.6
  • 61
    • 0030845184 scopus 로고    scopus 로고
    • Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A
    • Magalon, A., Lemesle-Meunier, D., Rothery, R. A., Frixon, C., Weiner, J. H., and Blasco, F. (1997) Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A, J. Biol. Chem. 272, 25652-25658.
    • (1997) J. Biol. Chem , vol.272 , pp. 25652-25658
    • Magalon, A.1    Lemesle-Meunier, D.2    Rothery, R.A.3    Frixon, C.4    Weiner, J.H.5    Blasco, F.6
  • 63
    • 0021754858 scopus 로고
    • Crystal field of atypical low-spin ferriheme complexes
    • Salerno, J. C., and Leigh, J. S. (1984) Crystal field of atypical low-spin ferriheme complexes, J. Am. Chem. Soc. 106, 2156-2159.
    • (1984) J. Am. Chem. Soc , vol.106 , pp. 2156-2159
    • Salerno, J.C.1    Leigh, J.S.2
  • 65
    • 0029087762 scopus 로고
    • Trans effects on cysteine ligation in the proximal His93Cys variant of horse heart myoglobin
    • Hildebrand, D. P., Ferrer, J. C., Tang, H. L., Smith, M., and Mauk, A. G. (1995) Trans effects on cysteine ligation in the proximal His93Cys variant of horse heart myoglobin, Biochemistry 34, 11598-11605.
    • (1995) Biochemistry , vol.34 , pp. 11598-11605
    • Hildebrand, D.P.1    Ferrer, J.C.2    Tang, H.L.3    Smith, M.4    Mauk, A.G.5
  • 66
    • 0033600588 scopus 로고    scopus 로고
    • Engineering cytochrome c peroxidase into cytochrome P450: A proximal effect on heme-thiolate ligation
    • Sigman, J. A., Pond, A. E., Dawson, J. H., and Lu, Y. (1999) Engineering cytochrome c peroxidase into cytochrome P450: A proximal effect on heme-thiolate ligation, Biochemistry 38, 11122-11129.
    • (1999) Biochemistry , vol.38 , pp. 11122-11129
    • Sigman, J.A.1    Pond, A.E.2    Dawson, J.H.3    Lu, Y.4
  • 67
    • 0000675137 scopus 로고
    • Resonance Raman spectra and the active site structure of semisynthetic Met80Cys horse heart cytochrome c
    • Smulevich, G., Bjerrum, M. J., Gray, H. B., and Spiro, T. G. (1994) Resonance Raman spectra and the active site structure of semisynthetic Met80Cys horse heart cytochrome c, Inorg. Chem. 33, 4629-4634.
    • (1994) Inorg. Chem , vol.33 , pp. 4629-4634
    • Smulevich, G.1    Bjerrum, M.J.2    Gray, H.B.3    Spiro, T.G.4
  • 69
    • 0025302839 scopus 로고
    • Wolinella succinogenes fumarate reductase contains a dihaem cytochrome b
    • Kortner, C., Lauterbach, F., Tripier, D., Unden, G., and Kroger, A. (1990) Wolinella succinogenes fumarate reductase contains a dihaem cytochrome b, Mol. Microbiol. 4, 855-860.
    • (1990) Mol. Microbiol , vol.4 , pp. 855-860
    • Kortner, C.1    Lauterbach, F.2    Tripier, D.3    Unden, G.4    Kroger, A.5
  • 70
    • 0032518289 scopus 로고    scopus 로고
    • Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon
    • Simon, J., Gross, R., Ringel, M., Schmidt, E., and Kroger, A. (1998) Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon, Eur. J. Biochem. 251, 418-426.
    • (1998) Eur. J. Biochem , vol.251 , pp. 418-426
    • Simon, J.1    Gross, R.2    Ringel, M.3    Schmidt, E.4    Kroger, A.5
  • 71
    • 0343168085 scopus 로고    scopus 로고
    • Succinate:quinone oxidoreductases: New insights from X-ray crystal structures
    • Lancaster, C. R., and Kroger, A. (2000) Succinate:quinone oxidoreductases: New insights from X-ray crystal structures, Biochim. Biophys. Acta 1459, 422-431.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 422-431
    • Lancaster, C.R.1    Kroger, A.2
  • 72
    • 0029969718 scopus 로고    scopus 로고
    • Intramembrane bis-heme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase
    • Finegold, A. A., Shatwell, K. P., Segal, A. W., Klausner, R. D., and Dancis, A. (1996) Intramembrane bis-heme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase, J. Biol. Chem. 271, 31021-31024.
    • (1996) J. Biol. Chem , vol.271 , pp. 31021-31024
    • Finegold, A.A.1    Shatwell, K.P.2    Segal, A.W.3    Klausner, R.D.4    Dancis, A.5
  • 73
    • 0019797154 scopus 로고
    • Proton:substrate stoichiometries during active transport of biogenic amines in chromaffin ghosts
    • Johnson, R. G., Carty, S. E., and Scarpa, A. (1981) Proton:substrate stoichiometries during active transport of biogenic amines in chromaffin ghosts, J. Biol. Chem. 256, 5773-5780.
    • (1981) J. Biol. Chem , vol.256 , pp. 5773-5780
    • Johnson, R.G.1    Carty, S.E.2    Scarpa, A.3
  • 74
    • 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
  • 75
    • 0021993676 scopus 로고
    • Electron transfer across posterior pituitary neurosecretory vesicle membranes
    • Russell, J. T., Levine, M., and Njus, D. (1985) Electron transfer across posterior pituitary neurosecretory vesicle membranes, J Biol. Chem. 260, 226-231.
    • (1985) J Biol. Chem , vol.260 , pp. 226-231
    • Russell, J.T.1    Levine, M.2    Njus, D.3
  • 76
    • 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
  • 77
    • 1342283140 scopus 로고    scopus 로고
    • 561 in reconstituted vesicles catalyzes transmembrane electron transfer and supports extravesicular dopamine β-hydroxylase activity
    • 561 in reconstituted vesicles catalyzes transmembrane electron transfer and supports extravesicular dopamine β-hydroxylase activity, J. Biochem. (Tokyo) 134, 859-867.
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 859-867
    • Seike, Y.1    Takeuchi, F.2    Tsubaki, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.