메뉴 건너뛰기




Volumn 4, Issue , 2004, Pages

Synthesis of chlorophyll b: Localization of chlorophyllide a oxygenase and discovery of a stable radical in the catalytic subunit

Author keywords

[No Author keywords available]

Indexed keywords

ALGAE; ARABIDOPSIS; CHLAMYDOMONAS; CHLAMYDOMONAS REINHARDTII; CHLOROPHYTA; PISUM SATIVUM;

EID: 2942557179     PISSN: 14712229     EISSN: 14712229     Source Type: Journal    
DOI: 10.1186/1471-2229-4-5     Document Type: Article
Times cited : (57)

References (64)
  • 1
    • 0033427835 scopus 로고    scopus 로고
    • Assembly of light-harvesting complex II and biogenesis of thylakoid membranes in chloroplasts
    • Hoober JK, Eggink LL: Assembly of light-harvesting complex II and biogenesis of thylakoid membranes in chloroplasts. Photosynth Res 1999, 61:197-215.
    • (1999) Photosynth Res , vol.61 , pp. 197-215
    • Hoober, J.K.1    Eggink, L.L.2
  • 2
    • 0035852295 scopus 로고    scopus 로고
    • Biogenesis and origin of thylakoid membranes
    • Vothknecht UC, Westhoff P: Biogenesis and origin of thylakoid membranes. Biochim Biophys Acta 2001, 1541:91-101.
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 91-101
    • Vothknecht, U.C.1    Westhoff, P.2
  • 3
    • 0033012091 scopus 로고    scopus 로고
    • A guide to the Lhc genes and their relatives in Arabidopsis
    • Jansson S: A guide to the Lhc genes and their relatives in Arabidopsis. Trends Plant Sci 1999, 4:236-240.
    • (1999) Trends Plant Sci , vol.4 , pp. 236-240
    • Jansson, S.1
  • 4
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt W, Wang DN, Fujiyoshi Y: Atomic model of plant light-harvesting complex by electron crystallography. Nature 1994, 367:614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 5
    • 0033569933 scopus 로고    scopus 로고
    • Carotenoid-binding sites of the major light-harvesting complex II of higher plants
    • Croce R, Weiss S, Bassi R: Carotenoid-binding sites of the major light-harvesting complex II of higher plants. J Biol Chem 1999, 274:29613-29623.
    • (1999) J Biol Chem , vol.274 , pp. 29613-29623
    • Croce, R.1    Weiss, S.2    Bassi, R.3
  • 6
    • 0037195240 scopus 로고    scopus 로고
    • Pigment compositions, spectral properties, and energy transfer efficiencies between the xanthophylls and chlorophylls in the major and minor pigment-protein complexes of photosystem II
    • Das SK, Frank HA: Pigment compositions, spectral properties, and energy transfer efficiencies between the xanthophylls and chlorophylls in the major and minor pigment-protein complexes of photosystem II. Biochemistry 2002, 41:13087-13095.
    • (2002) Biochemistry , vol.41 , pp. 13087-13095
    • Das, S.K.1    Frank, H.A.2
  • 7
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution
    • Liu Z, Yan H, Wang K, Kuang T, Zhang J, Gui L, An X, Chang W: Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution. Nature 2004, 428:287-292.
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Wang, K.3    Kuang, T.4    Zhang, J.5    Gui, L.6    An, X.7    Chang, W.8
  • 8
    • 0028089099 scopus 로고
    • The derivation of the formyl-group of chlorophyll b in higher plants from molecular oxygen
    • Porra RJ, Schäfer W, Cmiel E, Katheder I, Scheer H: The derivation of the formyl-group of chlorophyll b in higher plants from molecular oxygen. Eur J Biochem 1994, 219:671-679.
    • (1994) Eur J Biochem , vol.219 , pp. 671-679
    • Porra, R.J.1    Schäfer, W.2    Cmiel, E.3    Katheder, I.4    Scheer, H.5
  • 9
    • 0029257523 scopus 로고
    • Chlorophyll a/b-binding proteins, pigment conversions, and early light-induced proteins in a chlorophyll b-less barley mutant
    • Król M, Spangfort MD, Huner NPA, Öquist G, Gustafsson P, Jansson S: Chlorophyll a/b-binding proteins, pigment conversions, and early light-induced proteins in a chlorophyll b-less barley mutant. Plant Physiol 1995, 107:873-883.
    • (1995) Plant Physiol , vol.107 , pp. 873-883
    • Król, M.1    Spangfort, M.D.2    Huner, N.P.A.3    Öquist, G.4    Gustafsson, P.5    Jansson, S.6
  • 10
    • 0032989822 scopus 로고    scopus 로고
    • Protease-stable integration of Lhcb1 in thylakoid membranes is dependent on chlorophyll b in allelic chlorina-f2 mutants of barley (Hordeum vulgare L.)
    • Bossmann B, Grimme LH, Knoetzel J: Protease-stable integration of Lhcb1 in thylakoid membranes is dependent on chlorophyll b in allelic chlorina-f2 mutants of barley (Hordeum vulgare L.). Planta 1999, 207:551-558.
    • (1999) Planta , vol.207 , pp. 551-558
    • Bossmann, B.1    Grimme, L.H.2    Knoetzel, J.3
  • 11
    • 0033621182 scopus 로고    scopus 로고
    • The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyll b synthesis in Arabidopsis thaliana
    • Espineda CE, Linford AS, Devine D, Brusslan JA: The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyll b synthesis in Arabidopsis thaliana. Proc Natl Acad Sci USA 1999, 96:10507-10511.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10507-10511
    • Espineda, C.E.1    Linford, A.S.2    Devine, D.3    Brusslan, J.A.4
  • 12
    • 0034943675 scopus 로고    scopus 로고
    • Overexpression of chlorophyllide a oxygenase (CAO) enlarges the antenna size of photosystem II in Arabidopsis thaliana
    • Tanaka R, Koshino Y, Sawa S, Ishiguro S, Okada K, Tanaka A: Overexpression of chlorophyllide a oxygenase (CAO) enlarges the antenna size of photosystem II in Arabidopsis thaliana. Plant J 2001, 26:365-373.
    • (2001) Plant J , vol.26 , pp. 365-373
    • Tanaka, R.1    Koshino, Y.2    Sawa, S.3    Ishiguro, S.4    Okada, K.5    Tanaka, A.6
  • 13
    • 3042547200 scopus 로고    scopus 로고
    • The role of chlorophyll b in photosynthesis: Hypothesis
    • Eggink LL, Park H, Hoober JK: The role of chlorophyll b in photosynthesis: hypothesis. BMC Plant Biology 2001, 1:2.
    • (2001) BMC Plant Biology , vol.1 , pp. 2
    • Eggink, L.L.1    Park, H.2    Hoober, J.K.3
  • 14
    • 0032514698 scopus 로고    scopus 로고
    • Chlorophyll a oxygenase (CAO) is involved in chlorophyll b formation from chlorophyll a
    • Tanaka A, Ito H, Tanaka R, Tanaka NK, Yoshida K, Okada K: Chlorophyll a oxygenase (CAO) is involved in chlorophyll b formation from chlorophyll a. Proc Natl Acad Sci USA 1998, 95:12719-12723.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12719-12723
    • Tanaka, A.1    Ito, H.2    Tanaka, R.3    Tanaka, N.K.4    Yoshida, K.5    Okada, K.6
  • 15
    • 0033536171 scopus 로고    scopus 로고
    • Chlorophyll b and phycobilins in the common ancestor of cyanobacteria and chloroplasts
    • Tomitani A, Okada K, Miyashita H, Matthijs HCP, Ohno T, Tanaka A: Chlorophyll b and phycobilins in the common ancestor of cyanobacteria and chloroplasts. Nature 1999, 400:159-162.
    • (1999) Nature , vol.400 , pp. 159-162
    • Tomitani, A.1    Okada, K.2    Miyashita, H.3    Matthijs, H.C.P.4    Ohno, T.5    Tanaka, A.6
  • 16
    • 0001755262 scopus 로고
    • Chlorophyll b- and loroxanthin-deficient mutants of Chlamydomonas reinhardtii
    • Chunaev AS, Mirnaya ON, Maslov VG, Boschetti A: Chlorophyll b- and loroxanthin-deficient mutants of Chlamydomonas reinhardtii. Photosynthetica 1991, 25:291-301.
    • (1991) Photosynthetica , vol.25 , pp. 291-301
    • Chunaev, A.S.1    Mirnaya, O.N.2    Maslov, V.G.3    Boschetti, A.4
  • 17
    • 0036914512 scopus 로고    scopus 로고
    • Light-dependent death of maize lls1 cells is mediated by mature chloroplasts
    • Gray J, Janick-Buckner D, Buckner B, Close PS, Johal GS: Light-dependent death of maize lls1 cells is mediated by mature chloroplasts. Plant Physiol 2002, 130:1894-1907.
    • (2002) Plant Physiol , vol.130 , pp. 1894-1907
    • Gray, J.1    Janick-Buckner, D.2    Buckner, B.3    Close, P.S.4    Johal, G.S.5
  • 18
    • 1842764848 scopus 로고    scopus 로고
    • Genetic analysis of revertants of chlorophyll b -deficient mutants of Chlamydomonas reinhardtii
    • Nikoulina KV, Chekunova EM, Rüdiger W, Chunayev AS: Genetic analysis of revertants of chlorophyll b -deficient mutants of Chlamydomonas reinhardtii. Russian J Genet 1997, 33:474-479.
    • (1997) Russian J Genet , vol.33 , pp. 474-479
    • Nikoulina, K.V.1    Chekunova, E.M.2    Rüdiger, W.3    Chunayev, A.S.4
  • 19
    • 0021100246 scopus 로고
    • Preparation and characterization of membrane fractions enriched in outer and inner envelope membranes from spinach chloroplasts. II. Biochemical characterization
    • Block MA, Dorne A-J, Joyard J, Douce R: Preparation and characterization of membrane fractions enriched in outer and inner envelope membranes from spinach chloroplasts. II. Biochemical characterization. J Biol Chem 1983, 258:13281-13286.
    • (1983) J Biol Chem , vol.258 , pp. 13281-13286
    • Block, M.A.1    Dorne, A.-J.2    Joyard, J.3    Douce, R.4
  • 20
    • 0343948350 scopus 로고    scopus 로고
    • The role of the envelope in assembly of light-harvesting complexes in the chloroplast: Distribution of LHCP between chloroplast and vacuoles during chloroplast development in Chlamydomonas reinhardtii
    • Edited by: Argyroudi-Akoyunoglou JH, Senger H. Dordrecht: Kluwer
    • Eggink LL, Park H, Hoober JK: The role of the envelope in assembly of light-harvesting complexes in the chloroplast: distribution of LHCP between chloroplast and vacuoles during chloroplast development in Chlamydomonas reinhardtii. In The Chloroplast: From Molecular Biology to Biotechnology Edited by: Argyroudi-Akoyunoglou JH, Senger H. Dordrecht: Kluwer; 1999:161-166.
    • (1999) The Chloroplast: From Molecular Biology to Biotechnology , pp. 161-166
    • Eggink, L.L.1    Park, H.2    Hoober, J.K.3
  • 21
    • 0029812767 scopus 로고    scopus 로고
    • Localization of light-harvesting complex apoproteins in the chloroplast and cytoplasm during greening of Chlamydomonas reinhardtii at 38°C
    • White RA, Wolfe GR, Komine Y, Hoober JK: Localization of light-harvesting complex apoproteins in the chloroplast and cytoplasm during greening of Chlamydomonas reinhardtii at 38°C. Photosynth Res 1996, 47:267-280.
    • (1996) Photosynth Res , vol.47 , pp. 267-280
    • White, R.A.1    Wolfe, G.R.2    Komine, Y.3    Hoober, J.K.4
  • 22
    • 0029139732 scopus 로고
    • The 26- and 14-kDa phosphoproteins associated with spinach chloroplast envelope membranes are distinct membrane-bound poosl of the light-harvesting complex of photosystem II and of the small subunit of the ribulose-1,5- bisphosphate carboxylase-oxygenase
    • Bovet L, Müller MO, Siegenthaler PA: The 26- and 14-kDa phosphoproteins associated with spinach chloroplast envelope membranes are distinct membrane-bound poosl of the light-harvesting complex of photosystem II and of the small subunit of the ribulose-1,5-bisphosphate carboxylase-oxygenase. Planta 1995, 195:563-569.
    • (1995) Planta , vol.195 , pp. 563-569
    • Bovet, L.1    Müller, M.O.2    Siegenthaler, P.A.3
  • 23
    • 0030810571 scopus 로고    scopus 로고
    • In vitro and in organello phosphorylation of envelope proteins and phosphoglucomutase in spinach chloroplasts
    • Bovet L, L'Eplattenier B, Siegenthaler PA: In vitro and in organello phosphorylation of envelope proteins and phosphoglucomutase in spinach chloroplasts. Plant Sci 1997, 128:169-180.
    • (1997) Plant Sci , vol.128 , pp. 169-180
    • Bovet, L.1    L'Eplattenier, B.2    Siegenthaler, P.A.3
  • 24
    • 34447331528 scopus 로고    scopus 로고
    • Production of recombinant proteins
    • Edited by: Coligan JE, Dunn BM, Speicher DW, Wingfield PT, Ploegh HL. New York: John Wiley & Sons
    • Wingfield PT: Production of recombinant proteins. In Current Protocols in Protein Science Volume 1. Edited by: Coligan JE, Dunn BM, Speicher DW, Wingfield PT, Ploegh HL. New York: John Wiley & Sons; 2000:5.0.1-5.3.18.
    • (2000) Current Protocols in Protein Science Volume 1 , vol.1 , pp. 501-5318
    • Wingfield, P.T.1
  • 25
    • 0030956053 scopus 로고    scopus 로고
    • Expression of the Solfolobus acidocaldarius Rieske iron sulfur protein II (SOXF) with the correctly inserted [2Fe-2S] cluster in Escherichia coli
    • Schmidt CL, Hatzfeld OM, Petersen A, Link TA, Schäfer G: Expression of the Solfolobus acidocaldarius Rieske iron sulfur protein II (SOXF) with the correctly inserted [2Fe-2S] cluster in Escherichia coli. Biochem Biophys Res Commun 1997, 234:283-287.
    • (1997) Biochem Biophys Res Commun , vol.234 , pp. 283-287
    • Schmidt, C.L.1    Hatzfeld, O.M.2    Petersen, A.3    Link, T.A.4    Schäfer, G.5
  • 26
    • 2542510506 scopus 로고    scopus 로고
    • An Escherichia coli mutant quinol:fumarate reductase contains an EPR-detectable semiquinone stabilized at the proximal quinone-binding site
    • Hägerhäll C, Magnitsky S, Sled VD, Schröder I, Gunsalus RP, Cecchini G, Ohnishi T: An Escherichia coli mutant quinol:fumarate reductase contains an EPR-detectable semiquinone stabilized at the proximal quinone-binding site. J Biol Chem 1999, 274:26157-26164.
    • (1999) J Biol Chem , vol.274 , pp. 26157-26164
    • Hägerhäll, C.1    Magnitsky, S.2    Sled, V.D.3    Schröder, I.4    Gunsalus, R.P.5    Cecchini, G.6    Ohnishi, T.7
  • 27
    • 0348087046 scopus 로고    scopus 로고
    • The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein
    • Basu P, Katterle B, Andersson KK, Dalton H: The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein. Biochem J 2003, 369:417-427.
    • (2003) Biochem J , vol.369 , pp. 417-427
    • Basu, P.1    Katterle, B.2    Andersson, K.K.3    Dalton, H.4
  • 29
    • 7744231498 scopus 로고    scopus 로고
    • Mechanisms whereby mononuclear copper proteins functionalize organic substrates
    • Klinman JP: Mechanisms whereby mononuclear copper proteins functionalize organic substrates. Chem Rev 1996, 96:2541-2561.
    • (1996) Chem Rev , vol.96 , pp. 2541-2561
    • Klinman, J.P.1
  • 32
    • 0001312469 scopus 로고
    • Identification of the photochemically iodinated amino-acid residue on D1-protein in the photosystem II core complex by peptide mapping analysis
    • Takahashi Y, Satoh K: Identification of the photochemically iodinated amino-acid residue on D1-protein in the photosystem II core complex by peptide mapping analysis. Biochim Biophys Acta 1989, 973:138-146.
    • (1989) Biochim Biophys Acta , vol.973 , pp. 138-146
    • Takahashi, Y.1    Satoh, K.2
  • 34
    • 0001322788 scopus 로고
    • Origin of thylakoid membranes in Chlamydomonas reinhardtii y-1 at 38°C
    • Hoober JK, Boyd CO, Paavola LG: Origin of thylakoid membranes in Chlamydomonas reinhardtii y-1 at 38°C. Plant Physiol 1991, 96:1321-1328.
    • (1991) Plant Physiol , vol.96 , pp. 1321-1328
    • Hoober, J.K.1    Boyd, C.O.2    Paavola, L.G.3
  • 35
    • 0000083078 scopus 로고
    • Kinetics of chlorophyll accumulation and formation of chlorophyll-protein complexes during greening of Chlamydomonas reinhardtii y-1 at 38°C
    • Maloney MA, Hoober JK, Marks DB: Kinetics of chlorophyll accumulation and formation of chlorophyll-protein complexes during greening of Chlamydomonas reinhardtii y-1 at 38°C. Plant Physiol 1989, 91:1100-1106.
    • (1989) Plant Physiol , vol.91 , pp. 1100-1106
    • Maloney, M.A.1    Hoober, J.K.2    Marks, D.B.3
  • 37
    • 0001310408 scopus 로고
    • Stromal low temperature compartment derived from the inner membrane of the chloroplast envelope
    • Morré DJ, Selldén G, Sundqvist C, Sandelius AS: Stromal low temperature compartment derived from the inner membrane of the chloroplast envelope. Plant Physiol 1991, 97:1558-1564.
    • (1991) Plant Physiol , vol.97 , pp. 1558-1564
    • Morré, D.J.1    Selldén, G.2    Sundqvist, C.3    Sandelius, A.S.4
  • 39
    • 0035850922 scopus 로고    scopus 로고
    • A vesicle transport system inside chloroplasts
    • Westphal S, Soll J, Vothknecht UC: A vesicle transport system inside chloroplasts. FEBS Lett 2001, 506:257-261.
    • (2001) FEBS Lett , vol.506 , pp. 257-261
    • Westphal, S.1    Soll, J.2    Vothknecht, U.C.3
  • 40
    • 0031398089 scopus 로고    scopus 로고
    • Chlorophyll synthesis modulates retention of apoproteins of light-harvesting complex II by the chloroplast in Chlamydomonas reinhardtii
    • Park H, Hoober JK: Chlorophyll synthesis modulates retention of apoproteins of light-harvesting complex II by the chloroplast in Chlamydomonas reinhardtii. Physiol Plant 1997, 101:135-142.
    • (1997) Physiol Plant , vol.101 , pp. 135-142
    • Park, H.1    Hoober, J.K.2
  • 41
    • 0028109712 scopus 로고
    • Isolation of components of the chloroplast protein import machinery
    • Schnell DJ, Kessler F, Blobel G: Isolation of components of the chloroplast protein import machinery. Science 1994, 266:1007-1012.
    • (1994) Science , vol.266 , pp. 1007-1012
    • Schnell, D.J.1    Kessler, F.2    Blobel, G.3
  • 42
    • 0037428511 scopus 로고    scopus 로고
    • In vitro reconstitution of light-harvesting POR-protochlorophyllide complex with protochlorophyllides a and b
    • Reinbothe C, Buhr F, Pollmann S, Reinbothe S: In vitro reconstitution of light-harvesting POR-protochlorophyllide complex with protochlorophyllides a and b. J Biol Chem 2003, 278:807-815.
    • (2003) J Biol Chem , vol.278 , pp. 807-815
    • Reinbothe, C.1    Buhr, F.2    Pollmann, S.3    Reinbothe, S.4
  • 43
    • 0031019820 scopus 로고    scopus 로고
    • Redox chains in chloroplast envelope membranes: Spectroscopic evidence for the presence of electron carriers, including iron-sulfur centers
    • Jäger-Vottero P, Dorne A-J, Jordanov J, Douce R, Joyard J: Redox chains in chloroplast envelope membranes: spectroscopic evidence for the presence of electron carriers, including iron-sulfur centers. Proc Natl Acad Sci USA 1997, 94:1597-1602.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1597-1602
    • Jäger-Vottero, P.1    Dorne, A.-J.2    Jordanov, J.3    Douce, R.4    Joyard, J.5
  • 44
    • 0031463305 scopus 로고    scopus 로고
    • The chloroplastic protein import machinery contains a Rieske-type iron-sulfur cluster and a mononuclear iron-binding protein
    • Caliebe A, Grimm R, Kaiser G, Lübeck J, Soll J, Heins L: The chloroplastic protein import machinery contains a Rieske-type iron-sulfur cluster and a mononuclear iron-binding protein. EMBO J 1997, 16:7342-7350.
    • (1997) EMBO J , vol.16 , pp. 7342-7350
    • Caliebe, A.1    Grimm, R.2    Kaiser, G.3    Lübeck, J.4    Soll, J.5    Heins, L.6
  • 45
    • 0037112789 scopus 로고    scopus 로고
    • Protein import into chloroplasts involves redox-rgulated proteins
    • Küchler M, Decker S, Hörmann F, Soll J, Heins L: Protein import into chloroplasts involves redox-rgulated proteins. EMBO J 2002, 21:6136-6145.
    • (2002) EMBO J , vol.21 , pp. 6136-6145
    • Küchler, M.1    Decker, S.2    Hörmann, F.3    Soll, J.4    Heins, L.5
  • 47
    • 0036153918 scopus 로고    scopus 로고
    • The plant S-adenosyl-L-methionine:MG-protoporphyrin IX methyltransferase is located in both envelope and thylakoid chloroplast membranes
    • Block MA, Tewari AK, Albrieux C, Maréchal E, Joyard J: The plant S-adenosyl-L-methionine:MG-protoporphyrin IX methyltransferase is located in both envelope and thylakoid chloroplast membranes. Eur J Biochem 2002, 269:240-248.
    • (2002) Eur J Biochem , vol.269 , pp. 240-248
    • Block, M.A.1    Tewari, A.K.2    Albrieux, C.3    Maréchal, E.4    Joyard, J.5
  • 48
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • Stubbe J, van der Donk W: Protein radicals in enzyme catalysis. Chem Rev 1998, 98:705-762.
    • (1998) Chem Rev , vol.98 , pp. 705-762
    • Stubbe, J.1    Van Der Donk, W.2
  • 51
    • 0028002754 scopus 로고
    • Reconstitution of iron-sulfur center B of photosystem I damaged by mercuric chloride
    • He WZ, Malkin R: Reconstitution of iron-sulfur center B of photosystem I damaged by mercuric chloride. Photosynth Res 1994, 41:381-388.
    • (1994) Photosynth Res , vol.41 , pp. 381-388
    • He, W.Z.1    Malkin, R.2
  • 52
    • 0001709828 scopus 로고
    • + photoreduction in Hg-treated photosystem I complexes from Synechococcus sp. PCC6301
    • + photoreduction in Hg-treated photosystem I complexes from Synechococcus sp. PCC6301. Photosynth Res 1995, 46:249-255.
    • (1995) Photosynth Res , vol.46 , pp. 249-255
    • Jung, Y.S.1    Yu, L.2    Golbeck, J.H.3
  • 53
    • 0005914814 scopus 로고
    • Synthesis of chlorophyllide b from protochlorophyllide in Chlamydomonas reinhardtii y-1
    • Bednarik DP, Hoober JK: Synthesis of chlorophyllide b from protochlorophyllide in Chlamydomonas reinhardtii y-1. Science 1985, 230:450-453.
    • (1985) Science , vol.230 , pp. 450-453
    • Bednarik, D.P.1    Hoober, J.K.2
  • 54
    • 0026050851 scopus 로고
    • Chloroplast biogenesis: Detection of monovinyl protochlorophyll(ide) b in plants
    • Shedbalkar VP, Ioannides IM, Rebeiz CA: Chloroplast biogenesis: detection of monovinyl protochlorophyll(ide) b in plants. J Biol Chem 1991, 266:17151-17157.
    • (1991) J Biol Chem , vol.266 , pp. 17151-17157
    • Shedbalkar, V.P.1    Ioannides, I.M.2    Rebeiz, C.A.3
  • 55
    • 0037428509 scopus 로고    scopus 로고
    • In situ conversion of protochlorophyllide b to protochlorophyllide a in barley
    • Reinbothe S, Pollmann S, Reinbothe C: In situ conversion of protochlorophyllide b to protochlorophyllide a in barley. J Biol Chem 2003, 278:800-806.
    • (2003) J Biol Chem , vol.278 , pp. 800-806
    • Reinbothe, S.1    Pollmann, S.2    Reinbothe, C.3
  • 56
    • 0037044761 scopus 로고    scopus 로고
    • The presence of chlorophyll b in Synechocystis sp. PCC 6803 disturbs tetrapyrrole biosynthesis and enhances chlorophyll degradation
    • Xu H, Vavilin D, Vermaas W: The presence of chlorophyll b in Synechocystis sp. PCC 6803 disturbs tetrapyrrole biosynthesis and enhances chlorophyll degradation. J Biol Chem 2002, 277:42726-42732.
    • (2002) J Biol Chem , vol.277 , pp. 42726-42732
    • Xu, H.1    Vavilin, D.2    Vermaas, W.3
  • 57
    • 0034058987 scopus 로고    scopus 로고
    • Cloning and functional expression of the gene encoding the key enzyme for chlorophyll b biosynthesis (CAO) from Arabidopsis thaliana
    • Oster U, Tanaka R, Tanaka A, Rüdiger W: Cloning and functional expression of the gene encoding the key enzyme for chlorophyll b biosynthesis (CAO) from Arabidopsis thaliana. Plant J 2000, 21:305-310.
    • (2000) Plant J , vol.21 , pp. 305-310
    • Oster, U.1    Tanaka, R.2    Tanaka, A.3    Rüdiger, W.4
  • 58
    • 84961985438 scopus 로고    scopus 로고
    • Monooxygenation mechanism by cytochrome P-450
    • Hata M, Hirano Y, Hoshino T, Tsuda M: Monooxygenation mechanism by cytochrome P-450. J Am Chem Soc 2001, 123:6410-6416.
    • (2001) J Am Chem Soc , vol.123 , pp. 6410-6416
    • Hata, M.1    Hirano, Y.2    Hoshino, T.3    Tsuda, M.4
  • 59
    • 0002514628 scopus 로고
    • Electrochemistry of chlorophylls
    • Edited by: Scheer H. Boca Raton: CRC Press
    • Watanabe T, Kobayashi M: Electrochemistry of chlorophylls. In Chlorophylls Edited by: Scheer H. Boca Raton: CRC Press; 1991:287-315.
    • (1991) Chlorophylls , pp. 287-315
    • Watanabe, T.1    Kobayashi, M.2
  • 60
    • 0029942829 scopus 로고    scopus 로고
    • Recombinant toluene-4-monooxygenase: Catalytic and Mössbauer studies of the purified diiron and Rieske components of a four-protein complex
    • Pikus JD, Studts JM, Achim C, Kauffmann KE, Münck E, Steffan RJ, McClay K, Fox BG: Recombinant toluene-4-monooxygenase: catalytic and Mössbauer studies of the purified diiron and Rieske components of a four-protein complex. Biochemistry 1996, 35:9106-9119.
    • (1996) Biochemistry , vol.35 , pp. 9106-9119
    • Pikus, J.D.1    Studts, J.M.2    Achim, C.3    Kauffmann, K.E.4    Münck, E.5    Steffan, R.J.6    McClay, K.7    Fox, B.G.8
  • 61
    • 0033613246 scopus 로고    scopus 로고
    • Component interactions in the soluble methane monooxygenase system from Methylococcus capsulatus (Bath)
    • Gassner GT, Lippard SJ: Component interactions in the soluble methane monooxygenase system from Methylococcus capsulatus (Bath). Biochemistry 1999, 38:12768-12785.
    • (1999) Biochemistry , vol.38 , pp. 12768-12785
    • Gassner, G.T.1    Lippard, S.J.2
  • 62
    • 0037022829 scopus 로고    scopus 로고
    • Combined participation of hydroxylase active site residues and effector protein binding in a para to ortho modulation of toluene 4-monooxygenase regiospecificity
    • Mitchell KH, Studts JM, Fox BG: Combined participation of hydroxylase active site residues and effector protein binding in a para to ortho modulation of toluene 4-monooxygenase regiospecificity. Biochemistry 2002, 41:3176-3188.
    • (2002) Biochemistry , vol.41 , pp. 3176-3188
    • Mitchell, K.H.1    Studts, J.M.2    Fox, B.G.3
  • 63
    • 0030799267 scopus 로고    scopus 로고
    • Light-harvesting complex apoproteins in cytoplasmic vacuoles in Chlamydomonas reinhardtii (Chlorophyta)
    • Wolfe GR, Park H, Sharp WP, Hoober JK: Light-harvesting complex apoproteins in cytoplasmic vacuoles in Chlamydomonas reinhardtii (Chlorophyta). J Phycol 1997, 33:377-386.
    • (1997) J Phycol , vol.33 , pp. 377-386
    • Wolfe, G.R.1    Park, H.2    Sharp, W.P.3    Hoober, J.K.4
  • 64
    • 0019294814 scopus 로고
    • Structural similarities between the major polypeptides of thylakoid membranes from Chlamydomonas reinhardtii
    • Hoober JK, Millington RH, D'Angelo LP: Structural similarities between the major polypeptides of thylakoid membranes from Chlamydomonas reinhardtii. Arch Biochem Biophys 1980, 202:221-234.
    • (1980) Arch Biochem Biophys , vol.202 , pp. 221-234
    • Hoober, J.K.1    Millington, R.H.2    D'Angelo, L.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.