메뉴 건너뛰기




Volumn 54, Issue , 2003, Pages 497-517

Membrane-Bound Diiron Carboxylate Proteins

Author keywords

Carotenoid biosynthesis; Chlorophyll biosynthesis; Chlororespiration; Interfacial membrane binding; Nonheme iron protein; Plant respiration; Ubiquinone biosynthesis

Indexed keywords

CARBOXYLIC ACID; HYDROLASE; IRON CARBONYL COMPOUNDS; ORGANOMETALLIC COMPOUND; OXIDOREDUCTASE; VEGETABLE PROTEIN;

EID: 0141661868     PISSN: 15435008     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.arplant.54.031902.134915     Document Type: Review
Times cited : (114)

References (101)
  • 1
    • 0037116611 scopus 로고    scopus 로고
    • Exploring the molecular nature of alternative oxidase regulation and catalysis
    • Affourtit C, Albury MS, Crichton PG, Moore AL. 2002. Exploring the molecular nature of alternative oxidase regulation and catalysis. FEBS Lett. 510:121-26
    • (2002) FEBS Lett. , vol.510 , pp. 121-126
    • Affourtit, C.1    Albury, M.S.2    Crichton, P.G.3    Moore, A.L.4
  • 2
    • 0034049080 scopus 로고    scopus 로고
    • The active site of the plant alternative oxidase: Structural and mechanistic considerations
    • Affourtit C, Albury MS, Whitehouse DG, Moore AL. 2000. The active site of the plant alternative oxidase: structural and mechanistic considerations. Pest Manag. Sci. 56:31-38
    • (2000) Pest Manag. Sci. , vol.56 , pp. 31-38
    • Affourtit, C.1    Albury, M.S.2    Whitehouse, D.G.3    Moore, A.L.4
  • 3
    • 0037040961 scopus 로고    scopus 로고
    • Site-directed mutagenesis reveals the essentiality of the conserved residues in the putative diiron active site of the trypansome alternative oxidase
    • Ajayi W, Chaudhuri M, Hill GC. 2002. Site-directed mutagenesis reveals the essentiality of the conserved residues in the putative diiron active site of the trypansome alternative oxidase. J. Biol. Chem. 277:8187-93
    • (2002) J. Biol. Chem. , vol.277 , pp. 8187-8193
    • Ajayi, W.1    Chaudhuri, M.2    Hill, G.C.3
  • 4
    • 0037059747 scopus 로고    scopus 로고
    • Structure of the plant alternative oxidase: Site-directed mutagenesis provides new information on the active site and membrane topology
    • Albury MS, Affourtit C, Crichton PG, Moore AL. 2002. Structure of the plant alternative oxidase: Site-directed mutagenesis provides new information on the active site and membrane topology. J. Biol. Chem. 277:1190-94
    • (2002) J. Biol. Chem. , vol.277 , pp. 1190-1194
    • Albury, M.S.1    Affourtit, C.2    Crichton, P.G.3    Moore, A.L.4
  • 5
    • 0032934819 scopus 로고    scopus 로고
    • A revised model of the active site of the alternative oxidase
    • Andersson ME, Nordlund P. 1999. A revised model of the active site of the alternative oxidase. FEBS Lett. 449:17-22
    • (1999) FEBS Lett. , vol.449 , pp. 17-22
    • Andersson, M.E.1    Nordlund, P.2
  • 6
    • 0032817545 scopus 로고    scopus 로고
    • Enzymes of chlorophyll biosynthesis
    • Beale SI. 1999. Enzymes of chlorophyll biosynthesis. Photosynth. Res. 60:43-73
    • (1999) Photosynth. Res. , vol.60 , pp. 43-73
    • Beale, S.I.1
  • 7
    • 0032516058 scopus 로고    scopus 로고
    • Isolation of mutants of the Arabidopsis thaliana alternative oxidase (ubiquinol: oxygen oxidoreductase) resistant to salicylhydroxamic acid
    • Berthold DA. 1998. Isolation of mutants of the Arabidopsis thaliana alternative oxidase (ubiquinol: oxygen oxidoreductase) resistant to salicylhydroxamic acid. Biochim. Biophys. Acta 1364:73-83
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 73-83
    • Berthold, D.A.1
  • 8
    • 0034693765 scopus 로고    scopus 로고
    • New insight into the structure and function of the alternative oxidase
    • Berthold DA, Andersson ME, Nordlund P. 2000. New insight into the structure and function of the alternative oxidase. Biochim. Biophys. Acta 1460:241-54
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 241-254
    • Berthold, D.A.1    Andersson, M.E.2    Nordlund, P.3
  • 9
    • 0037215266 scopus 로고    scopus 로고
    • Screening for functional expression and overexpression of a family of diiron-containing interfacial membrane proteins using the univector recombination system
    • Berthold DA, Stenmark P, Nordlund P. 2003. Screening for functional expression and overexpression of a family of diiron-containing interfacial membrane proteins using the univector recombination system. Protein Sci. 12:124-34
    • (2003) Protein Sci. , vol.12 , pp. 124-134
    • Berthold, D.A.1    Stenmark, P.2    Nordlund, P.3
  • 10
    • 0037113986 scopus 로고    scopus 로고
    • EPR studies of the mitochondrial alternative oxidase. Evidence for a diiron carboxylate center
    • Berthold DA, Voevodskaya N, Stenmark P, Gräslund A, Nordlund P. 2002. EPR studies of the mitochondrial alternative oxidase. Evidence for a diiron carboxylate center. J. Biol. Chem. 277:43608-14
    • (2002) J. Biol. Chem. , vol.277 , pp. 43608-43614
    • Berthold, D.A.1    Voevodskaya, N.2    Stenmark, P.3    Gräslund, A.4    Nordlund, P.5
  • 11
    • 0024728612 scopus 로고
    • Molecular oxygen and the state of geometric isomerism of intermediates are essential in the carotene desaturation and cyclization reactions in daffodil chromoplasts
    • Beyer P, Mayer M, Kleinig H. 1989. Molecular oxygen and the state of geometric isomerism of intermediates are essential in the carotene desaturation and cyclization reactions in daffodil chromoplasts. Eur. J. Biochem. 184:141-50
    • (1989) Eur. J. Biochem. , vol.184 , pp. 141-150
    • Beyer, P.1    Mayer, M.2    Kleinig, H.3
  • 12
    • 0029132620 scopus 로고
    • Formation of the isocyclic ring of chlorophyll by isolated Chlamydomonas reinhardtii chloroplasts
    • Bollivar DW, Beale SI. 1995. Formation of the isocyclic ring of chlorophyll by isolated Chlamydomonas reinhardtii chloroplasts. Photosynth. Res. 43:113-24
    • (1995) Photosynth. Res. , vol.43 , pp. 113-124
    • Bollivar, D.W.1    Beale, S.I.2
  • 13
    • 0029914197 scopus 로고    scopus 로고
    • The chlorophyll biosynthetic enzyme Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase
    • Bollivar DW, Beale SI. 1996. The chlorophyll biosynthetic enzyme Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase. Plant Physiol. 112:105-14
    • (1996) Plant Physiol. , vol.112 , pp. 105-114
    • Bollivar, D.W.1    Beale, S.I.2
  • 14
    • 0035211544 scopus 로고    scopus 로고
    • A plastid terminal oxidase comes to light: Implications for carotenoid biosynthesis and chlororespiration
    • Carol P, Kuntz M. 2001. A plastid terminal oxidase comes to light: implications for carotenoid biosynthesis and chlororespiration. Trends Plant Sci. 6:31-36
    • (2001) Trends Plant Sci. , vol.6 , pp. 31-36
    • Carol, P.1    Kuntz, M.2
  • 15
    • 0032697005 scopus 로고    scopus 로고
    • Mutations in the Arabidopsis gene IMMUTANS cause a variegated phenotype by inactivating a chloroplast terminal oxidase associated with phytoene desaturation
    • Carol P, Stevenson D, Bisanz C, Breitenbach J, Sandmann G, et al. 1999. Mutations in the Arabidopsis gene IMMUTANS cause a variegated phenotype by inactivating a chloroplast terminal oxidase associated with phytoene desaturation. Plant Cell 11:57-68
    • (1999) Plant Cell , vol.11 , pp. 57-68
    • Carol, P.1    Stevenson, D.2    Bisanz, C.3    Breitenbach, J.4    Sandmann, G.5
  • 17
    • 0033815884 scopus 로고    scopus 로고
    • New advances in coenzyme Q biosynthesis
    • Clarke C. 2000. New advances in coenzyme Q biosynthesis. Protoplasma 213:134-47
    • (2000) Protoplasma , vol.213 , pp. 134-147
    • Clarke, C.1
  • 18
    • 0035476428 scopus 로고    scopus 로고
    • A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: Catalytic electron transfer to rubrerythrin and two-iron superoxide reductase
    • Coulter ED, Kurtz DM. 2001. A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: catalytic electron transfer to rubrerythrin and two-iron superoxide reductase. Arch. Biochem. Biophys. 394:76-86
    • (2001) Arch. Biochem. Biophys. , vol.394 , pp. 76-86
    • Coulter, E.D.1    Kurtz, D.M.2
  • 19
    • 0034730965 scopus 로고    scopus 로고
    • Flexibility in photosynthetic electron transport: A newly identified chloroplast oxidase involved in chlororespiration
    • Cournac L, Josse E-M, Joët T, Rumeau D, Redding K, et al. 2000. Flexibility in photosynthetic electron transport: a newly identified chloroplast oxidase involved in chlororespiration. Philos. Trans. R. Soc. London Ser. B 355:1447-54
    • (2000) Philos. Trans. R. Soc. London Ser. B , vol.355 , pp. 1447-1454
    • Cournac, L.1    Josse, E.-M.2    Joët, T.3    Rumeau, D.4    Redding, K.5
  • 20
    • 0034625412 scopus 로고    scopus 로고
    • Electron flow between photosystem II and oxygen in chloroplasts of photosystem I-deficient algae is mediated by a quinol oxidase involved in chlororespiration
    • Cournac L, Redding K, Ravenel J, Rumeau D, Josse E-M, et al. 2000. Electron flow between photosystem II and oxygen in chloroplasts of photosystem I-deficient algae is mediated by a quinol oxidase involved in chlororespiration. J. Biol. Chem. 275:17256-62
    • (2000) J. Biol. Chem. , vol.275 , pp. 17256-17262
    • Cournac, L.1    Redding, K.2    Ravenel, J.3    Rumeau, D.4    Josse, E.-M.5
  • 21
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano WL, Ultsch MH, de Vos AM, Wells JA. 2000. Convergent solutions to binding at a protein-protein interface. Science 287:1279-83
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 22
    • 0032974375 scopus 로고    scopus 로고
    • A single amino acid change in the plant alternative oxidase alters the specificity of organic acid activation
    • Djajanegara I, Holtzapffel R, Finnegan PM, Hoefnagel MHN, Berthold DA, et al. 1999. A single amino acid change in the plant alternative oxidase alters the specificity of organic acid activation. FEBS Lett. 454:220-24
    • (1999) FEBS Lett. , vol.454 , pp. 220-224
    • Djajanegara, I.1    Holtzapffel, R.2    Finnegan, P.M.3    Hoefnagel, M.H.N.4    Berthold, D.A.5
  • 24
    • 0001335087 scopus 로고
    • Monoclonal antibodies to the alternative oxidase of higher plant mitochondria
    • Elthon TE, Nickels RL, McIntosh L. 1989. Monoclonal antibodies to the alternative oxidase of higher plant mitochondria. Plant Physiol. 89:1311-17
    • (1989) Plant Physiol. , vol.89 , pp. 1311-1317
    • Elthon, T.E.1    Nickels, R.L.2    McIntosh, L.3
  • 25
    • 0031030678 scopus 로고    scopus 로고
    • Structural and functional conservation of the Caenorhabditis elegans timing gene clk-1
    • Ewbank JJ, Barnes TM, Lakowski B, Lussier M, Bussey H, Hekimi S. 1997. Structural and functional conservation of the Caenorhabditis elegans timing gene clk-1. Science 275:980-83
    • (1997) Science , vol.275 , pp. 980-983
    • Ewbank, J.J.1    Barnes, T.M.2    Lakowski, B.3    Lussier, M.4    Bussey, H.5    Hekimi, S.6
  • 26
    • 0002883704 scopus 로고    scopus 로고
    • Catalysis by non-heme iron-containing enzymes
    • ed. M Sinnott, London: Academic
    • Fox BG. 1998. Catalysis by non-heme iron-containing enzymes. In Comprehensive Biological Catalysis, ed. M Sinnott, pp. 261-348. London: Academic
    • (1998) Comprehensive Biological Catalysis , pp. 261-348
    • Fox, B.G.1
  • 27
    • 0025291817 scopus 로고
    • Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: Mechanistic and environmental implications
    • Fox BG, Borneman JG, Wackett LP, Lipscomb JD. 1990. Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: mechanistic and environmental implications. Biochemistry 29:6419-27
    • (1990) Biochemistry , vol.29 , pp. 6419-6427
    • Fox, B.G.1    Borneman, J.G.2    Wackett, L.P.3    Lipscomb, J.D.4
  • 29
    • 0033603005 scopus 로고    scopus 로고
    • Global conformational changes control the reactivity of methane monooxygenase
    • Gallagher SC, Callaghan AJ, Zhao J, Dalton H, Trewhella J. 1999. Global conformational changes control the reactivity of methane monooxygenase. Biochemistry 38:6752-60
    • (1999) Biochemistry , vol.38 , pp. 6752-6760
    • Gallagher, S.C.1    Callaghan, A.J.2    Zhao, J.3    Dalton, H.4    Trewhella, J.5
  • 30
    • 0037051963 scopus 로고    scopus 로고
    • CLK-1 protein has DNA binding activity specific to O(L) region of mitochondrial DNA
    • Gorbunova V, Seluanov A. 2002. CLK-1 protein has DNA binding activity specific to O(L) region of mitochondrial DNA. FEBS Lett. 516:279-84
    • (2002) FEBS Lett. , vol.516 , pp. 279-284
    • Gorbunova, V.1    Seluanov, A.2
  • 31
    • 0034612350 scopus 로고    scopus 로고
    • Anaerobic chlorophyll isocyclic ring formation in Rhodobacter capsulatus requires a cobalamin cofactor
    • Gough SP, Petersen BO, Duus JØ. 2000. Anaerobic chlorophyll isocyclic ring formation in Rhodobacter capsulatus requires a cobalamin cofactor. Proc. Natl. Acad. Sci. USA 97:6908-13
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6908-6913
    • Gough, S.P.1    Petersen, B.O.2    Duus, J.Ø.3
  • 32
    • 0016431422 scopus 로고
    • Cyanide-insensitive respiration. An alternative mitochondrial pathway
    • Henry MF, Nyns EJ. 1975. Cyanide-insensitive respiration. An alternative mitochondrial pathway. Sub-Cell. Biochem. 4:1-65
    • (1975) Sub-Cell. Biochem. , vol.4 , pp. 1-65
    • Henry, M.F.1    Nyns, E.J.2
  • 33
    • 0031403406 scopus 로고    scopus 로고
    • Substrate kinetics of the plant mitochondrial alternative oxidase and the effects of pyruvate
    • Hoefnagel MHN, Rich PR, Zhang Q, Wiskich JT. 1997. Substrate kinetics of the plant mitochondrial alternative oxidase and the effects of pyruvate. Plant Physiol. 115:1145-53
    • (1997) Plant Physiol. , vol.115 , pp. 1145-1153
    • Hoefnagel, M.H.N.1    Rich, P.R.2    Zhang, Q.3    Wiskich, J.T.4
  • 35
    • 0034630103 scopus 로고    scopus 로고
    • Genetic evidence for a multi-subunit complex in the O-methyltransferase steps of coenzyme Q biosynthesis
    • Hsu AY, Do TQ, Lee PT, Clarke CF. 2000. Genetic evidence for a multi-subunit complex in the O-methyltransferase steps of coenzyme Q biosynthesis. Biochim. Biophys. Acta 1484:287-97
    • (2000) Biochim. Biophys. Acta , vol.1484 , pp. 287-297
    • Hsu, A.Y.1    Do, T.Q.2    Lee, P.T.3    Clarke, C.F.4
  • 36
    • 0026697885 scopus 로고
    • Characterization and molecular cloning of a flavoprotein catalyzing the synthesis of phytofluene and ζ-carotene in Capsicum chromoplasts
    • Hugueney P, Römer S, Kuntz M, Camara B. 1992. Characterization and molecular cloning of a flavoprotein catalyzing the synthesis of phytofluene and ζ-carotene in Capsicum chromoplasts. Eur. J. Biochem. 209:399-407
    • (1992) Eur. J. Biochem. , vol.209 , pp. 399-407
    • Hugueney, P.1    Römer, S.2    Kuntz, M.3    Camara, B.4
  • 37
    • 0035800788 scopus 로고    scopus 로고
    • Mouse CLK-1 is imported into mitochondria by an unusual process that requires a leader sequence but no membrane potential
    • Jiang N, Levavasseur F, McCright B, Shoubridge EA, Hekimi S. 2001. Mouse CLK-1 is imported into mitochondria by an unusual process that requires a leader sequence but no membrane potential. J. Biol. Chem. 276:29,218-25
    • (2001) J. Biol. Chem. , vol.276 , pp. 29218-29225
    • Jiang, N.1    Levavasseur, F.2    McCright, B.3    Shoubridge, E.A.4    Hekimi, S.5
  • 38
    • 0034795985 scopus 로고    scopus 로고
    • Desaturation reactions catalyzed by soluble methane monooxygenase
    • Jin Y, Lipscomb JD. 2001. Desaturation reactions catalyzed by soluble methane monooxygenase. J. Biol. Inorg. Chem. 6:717-25
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 717-725
    • Jin, Y.1    Lipscomb, J.D.2
  • 39
    • 0037199963 scopus 로고    scopus 로고
    • Involvement of a plastid terminal oxidase in plastoquinone oxidation as evidenced by expression of the Arabidopsis thaliana enzyme in tobacco
    • Joët T, Gentry B, Josse E-M, Kuntz M, Cournac L, Peltier G. 2002. Involvement of a plastid terminal oxidase in plastoquinone oxidation as evidenced by expression of the Arabidopsis thaliana enzyme in tobacco. J. Biol. Chem. 211:31623-30
    • (2002) J. Biol. Chem. , vol.211 , pp. 31623-31630
    • Joët, T.1    Gentry, B.2    Josse, E.-M.3    Kuntz, M.4    Cournac, L.5    Peltier, G.6
  • 40
    • 0035895199 scopus 로고    scopus 로고
    • A dietary source of coenzyme Q is essential for growth of long-lived Caenorhabditis elegans clk-1 mutants
    • Jonassen T, Larsen PL, Clarke CF. 2001. A dietary source of coenzyme Q is essential for growth of long-lived Caenorhabditis elegans clk-1 mutants. Proc. Natl. Acad. Sci. USA 98:421-26
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 421-426
    • Jonassen, T.1    Larsen, P.L.2    Clarke, C.F.3
  • 41
    • 0032488838 scopus 로고    scopus 로고
    • Yeast clk-1 homologue (Coq7/Cat5) is a mitochondrial protein in coenzyme Q synthesis
    • Jonassen T, Proft M, Randez-Gil F, Schultz JR, Marbois BN, et al. 1998. Yeast clk-1 homologue (Coq7/Cat5) is a mitochondrial protein in coenzyme Q synthesis. J. Biol. Chem. 273:3351-57
    • (1998) J. Biol. Chem. , vol.273 , pp. 3351-3357
    • Jonassen, T.1    Proft, M.2    Randez-Gil, F.3    Schultz, J.R.4    Marbois, B.N.5
  • 42
    • 0033841024 scopus 로고    scopus 로고
    • A plastid terminal oxidase associated with carotenoid desaturation during chromoplast differentiation
    • Josse EM, Simkin AJ, Gaffé J, Labouré A-M, Kuntz M, Carol P. 2000. A plastid terminal oxidase associated with carotenoid desaturation during chromoplast differentiation. Plant Physiol. 123:1427-36
    • (2000) Plant Physiol. , vol.123 , pp. 1427-1436
    • Josse, E.M.1    Simkin, A.J.2    Gaffé, J.3    Labouré, A.-M.4    Kuntz, M.5    Carol, P.6
  • 43
    • 0022081301 scopus 로고
    • Solubilization of the alternative oxidase of cuckoo-pint (Arum maculatum) mitochondria. Stimulation by high concentrations of ions and effects of specific inhibitors
    • Kay CJ, Palmer JM. 1985. Solubilization of the alternative oxidase of cuckoo-pint (Arum maculatum) mitochondria. Stimulation by high concentrations of ions and effects of specific inhibitors. Biochem. J. 228:309-18
    • (1985) Biochem. J. , vol.228 , pp. 309-318
    • Kay, C.J.1    Palmer, J.M.2
  • 44
    • 0034840430 scopus 로고    scopus 로고
    • Life as aerobes: Are there simple rules for activation of dioxygen by enzymes?
    • Kinman JP. 2001. Life as aerobes: are there simple rules for activation of dioxygen by enzymes? J. Biol. Inorg. Chem. 6:1-13
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 1-13
    • Kinman, J.P.1
  • 45
    • 12644273812 scopus 로고    scopus 로고
    • Structural similarity and functional diversity in diiron-oxo proteins
    • Kurtz DM. 1997. Structural similarity and functional diversity in diiron-oxo proteins. J. Biol. Inorg. Chem. 2:159-67
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 159-167
    • Kurtz, D.M.1
  • 46
    • 0037016442 scopus 로고    scopus 로고
    • Extension of life-span in Caenorhabditis elegans by a diet lacking coenzyme Q
    • Larsen PL, Clarke CF. 2002. Extension of life-span in Caenorhabditis elegans by a diet lacking coenzyme Q. Science 295:120-23
    • (2002) Science , vol.295 , pp. 120-123
    • Larsen, P.L.1    Clarke, C.F.2
  • 47
    • 0000283657 scopus 로고
    • The cyanide-resistant, alternative path in higher plant respiration
    • Laties GG. 1982. The cyanide-resistant, alternative path in higher plant respiration. Annu. Rev. Plant Physiol. 33:519-55
    • (1982) Annu. Rev. Plant Physiol. , vol.33 , pp. 519-555
    • Laties, G.G.1
  • 48
    • 0030063759 scopus 로고    scopus 로고
    • The COQ7 gene encodes a protein in Saccharomyces cerevisiae necessary for ubiquinone biosynthesis
    • Marbois BN, Clarke CF. 1996. The COQ7 gene encodes a protein in Saccharomyces cerevisiae necessary for ubiquinone biosynthesis. J. Biol. Chem. 271:2995-3004
    • (1996) J. Biol. Chem. , vol.271 , pp. 2995-3004
    • Marbois, B.N.1    Clarke, C.F.2
  • 49
    • 0033529335 scopus 로고    scopus 로고
    • The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells
    • Maxwell DP, Wang Y, McIntosh L. 1999. The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells. Proc. Natl. Acad. Sci. USA 96:8271-76
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8271-8276
    • Maxwell, D.P.1    Wang, Y.2    McIntosh, L.3
  • 50
    • 0025325851 scopus 로고
    • Quinone compounds are able to replace molecular oxygen as terminal electron acceptor in phytoene desaturation in chromoplasts of Narcissus pseudonarcissus L.
    • Mayer MP. 1990. Quinone compounds are able to replace molecular oxygen as terminal electron acceptor in phytoene desaturation in chromoplasts of Narcissus pseudonarcissus L. Eur. J. Biochem. 191:359-63
    • (1990) Eur. J. Biochem. , vol.191 , pp. 359-363
    • Mayer, M.P.1
  • 51
    • 0035219809 scopus 로고    scopus 로고
    • 2) and ubiquinone (coenzyme Q): A perspective on enzymatic mechanisms
    • 2) and ubiquinone (coenzyme Q): a perspective on enzymatic mechanisms. Vitam. Horm. 61:173-218
    • (2001) Vitam. Horm. , vol.61 , pp. 173-218
    • Meganathan, R.1
  • 52
    • 0035800409 scopus 로고    scopus 로고
    • Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: A tale of two irons and three proteins
    • Merkx M, Kopp DA, Sazinsky MH, Blazyk JL, Müller J, Lippard SJ. 2001. Dioxygen activation and methane hydroxylation by soluble methane monooxygenase: a tale of two irons and three proteins. Angew. Chem. Int. Ed. 40:2782-807
    • (2001) Angew. Chem. Int. Ed. , vol.40 , pp. 2782-2807
    • Merkx, M.1    Kopp, D.A.2    Sazinsky, M.H.3    Blazyk, J.L.4    Müller, J.5    Lippard, S.J.6
  • 53
    • 0000249448 scopus 로고    scopus 로고
    • Specificity of the organic acid activation of alternative oxidase in plant mitochondria
    • Millar AH, Hoefnagel MHN, Day DA, Wiskich JT. 1996. Specificity of the organic acid activation of alternative oxidase in plant mitochondria. Plant Physiol. 111:613-18
    • (1996) Plant Physiol. , vol.111 , pp. 613-618
    • Millar, A.H.1    Hoefnagel, M.H.N.2    Day, D.A.3    Wiskich, J.T.4
  • 54
    • 0025371012 scopus 로고
    • Essential role of ferrous iron in cyanide-resistant respiration in Hansenula anomala
    • Minagawa N, Sakajo S, Komiyama T, Yoshimoto A. 1990. Essential role of ferrous iron in cyanide-resistant respiration in Hansenula anomala. FEBS Lett. 267:114-16
    • (1990) FEBS Lett. , vol.267 , pp. 114-116
    • Minagawa, N.1    Sakajo, S.2    Komiyama, T.3    Yoshimoto, A.4
  • 55
    • 0035896557 scopus 로고    scopus 로고
    • Altered quinone biosynthesis in the long-lived clk-1 mutants of Caenorhabditis elegans
    • Miyadera H, Amino H, Hiraishi A, Taka H, Murayama K, et al. 2001. Altered quinone biosynthesis in the long-lived clk-1 mutants of Caenorhabditis elegans. J. Biol. Chem. 276:7713-16
    • (2001) J. Biol. Chem. , vol.276 , pp. 7713-7716
    • Miyadera, H.1    Amino, H.2    Hiraishi, A.3    Taka, H.4    Murayama, K.5
  • 56
    • 0034658505 scopus 로고    scopus 로고
    • The Crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii
    • Moseley J, Quinn J, Eriksson M, Merchant S. 2000. The Crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii. EMBO J. 19:2139-51
    • (2000) EMBO J. , vol.19 , pp. 2139-2151
    • Moseley, J.1    Quinn, J.2    Eriksson, M.3    Merchant, S.4
  • 57
    • 0036010573 scopus 로고    scopus 로고
    • Reciprocal expression of two candidate di-iron enzymes affecting photosystem I and light-harvesting complex accumulation
    • Moseley JL, Page MD, Alder NP, Eriksson M, Quinn J, et al. 2002. Reciprocal expression of two candidate di-iron enzymes affecting photosystem I and light-harvesting complex accumulation. Plant Cell 14:673-88
    • (2002) Plant Cell , vol.14 , pp. 673-688
    • Moseley, J.L.1    Page, M.D.2    Alder, N.P.3    Eriksson, M.4    Quinn, J.5
  • 58
    • 0023320838 scopus 로고
    • The use of continuous assays to characterize the oxidative cyclase that synthesizes the chlorophyll isocyclic ring
    • Nasrulhaq-Boyce A, Griffiths WT, Jones OT. 1987. The use of continuous assays to characterize the oxidative cyclase that synthesizes the chlorophyll isocyclic ring. Biochem. J. 243:23-29
    • (1987) Biochem. J. , vol.243 , pp. 23-29
    • Nasrulhaq-Boyce, A.1    Griffiths, W.T.2    Jones, O.T.3
  • 60
    • 0002439105 scopus 로고    scopus 로고
    • Structure-function of non-heme iron proteins with oxygen- and nitrogen-dominated coordination
    • ed. I Bertini, A Sigel, H Sigel, New York: Marcel Dekker
    • Nordlund P. 2001. Structure-function of non-heme iron proteins with oxygen- and nitrogen-dominated coordination. In Handbook of Metalloproteins, ed. I Bertini, A Sigel, H Sigel, pp. 461-570. New York: Marcel Dekker
    • (2001) Handbook of Metalloproteins , pp. 461-570
    • Nordlund, P.1
  • 62
    • 0029556712 scopus 로고
    • Genetic dissection of carotenoid synthesis in Arabidopsis defines plastoquinone as an essential component of phytoene desaturation
    • Norris SR, Barrette TR, DellaPenna D. 1995. Genetic dissection of carotenoid synthesis in Arabidopsis defines plastoquinone as an essential component of phytoene desaturation. Plant Cell 7:2139-49
    • (1995) Plant Cell , vol.7 , pp. 2139-2149
    • Norris, S.R.1    Barrette, T.R.2    DellaPenna, D.3
  • 65
    • 0036178443 scopus 로고    scopus 로고
    • Rubrivivax gelatinosus acsF (previously orf358) codes for a conserved, putative binuclear-iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethylester
    • Pinta V, Picaud M, Reiss-Husson F, Astier C. 2002. Rubrivivax gelatinosus acsF (previously orf358) codes for a conserved, putative binuclear-iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethylester. J. Bacteriol. 184:746-53
    • (2002) J. Bacteriol. , vol.184 , pp. 746-753
    • Pinta, V.1    Picaud, M.2    Reiss-Husson, F.3    Astier, C.4
  • 66
    • 0029161931 scopus 로고
    • 1-oxo and 3-acetyl groups of bacteriochlorophyll a from water in Rhodobacter sphaeroides cells adapting from respiratory to photosynthetic conditions: Evidence for ananaerobicpathway for the formation of isocyclic ring E
    • 1-oxo and 3-acetyl groups of bacteriochlorophyll a from water in Rhodobacter sphaeroides cells adapting from respiratory to photosynthetic conditions: evidence for ananaerobicpathway for the formation of isocyclic ring E. FEBS Lett. 371:21-24
    • (1995) FEBS Lett. , vol.371 , pp. 21-24
    • Porra, R.J.1    Schäfer, W.2    Katheder, I.3    Scheer, H.4
  • 67
    • 0029610003 scopus 로고
    • CAT5, a new gene necessary for derepression of gluconeogenic enzymes in Saccharomyces cerevisiae
    • Proft M, Kotter P, Hedges D, Bojunga N, Entian KD. 1995. CAT5, a new gene necessary for derepression of gluconeogenic enzymes in Saccharomyces cerevisiae. EMBO J. 14:6116-26
    • (1995) EMBO J. , vol.14 , pp. 6116-6126
    • Proft, M.1    Kotter, P.2    Hedges, D.3    Bojunga, N.4    Entian, K.D.5
  • 68
    • 0001503269 scopus 로고
    • Monodentate carboxylate complexes and the carboxylate shift: Implications for poly-metalloprotein structure and function
    • Rardin RL, Tolman WB, Lippard SJ. 1991. Monodentate carboxylate complexes and the carboxylate shift: implications for poly-metalloprotein structure and function. New J. Chem. 15:417-30
    • (1991) New J. Chem. , vol.15 , pp. 417-430
    • Rardin, R.L.1    Tolman, W.B.2    Lippard, S.J.3
  • 69
    • 0025968150 scopus 로고
    • Isolation and characterization of a complementary DNA clone encoding an alternative oxidase protein of Sauromatum guttatum (Schott)
    • Rhoads DM, McIntosh L. 1991. Isolation and characterization of a complementary DNA clone encoding an alternative oxidase protein of Sauromatum guttatum (Schott). Proc. Natl. Acad. Sci. USA 88:2122-26
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2122-2126
    • Rhoads, D.M.1    McIntosh, L.2
  • 70
    • 0032514922 scopus 로고    scopus 로고
    • Regulation of the cyanide-resistant alternative oxidase of plant mitochondria. Identification of the cysteine residue involved in α-keto acid stimulation and intersubunit disulfide bond formation
    • Rhoads DM, Umbach AL, Sweet CR, Lennon AM, Rauch GS, Siedow JN. 1998. Regulation of the cyanide-resistant alternative oxidase of plant mitochondria. Identification of the cysteine residue involved in α-keto acid stimulation and intersubunit disulfide bond formation. J. Biol. Chem. 273:30750-56
    • (1998) J. Biol. Chem. , vol.273 , pp. 30750-30756
    • Rhoads, D.M.1    Umbach, A.L.2    Sweet, C.R.3    Lennon, A.M.4    Rauch, G.S.5    Siedow, J.N.6
  • 71
    • 58149367966 scopus 로고
    • Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states
    • Rosenzweig AC, Nordlund P, Takahara PM, Frederick CA, Lippard SJ. 1995. Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states. Chem. Biol. 2:409-18
    • (1995) Chem. Biol. , vol.2 , pp. 409-418
    • Rosenzweig, A.C.1    Nordlund, P.2    Takahara, P.M.3    Frederick, C.A.4    Lippard, S.J.5
  • 72
    • 0031080495 scopus 로고    scopus 로고
    • Effects of nucleotides on cyanide-resistant respiratory activity in mitochondria isolated from antimycin A-treated yeast Hansenula anomala
    • Sakajo S, Minagawa N, Yoshimoto A. 1997. Effects of nucleotides on cyanide-resistant respiratory activity in mitochondria isolated from antimycin A-treated yeast Hansenula anomala. Biosci. Biotechol. Biochem. 61:396-99
    • (1997) Biosci. Biotechol. Biochem. , vol.61 , pp. 396-399
    • Sakajo, S.1    Minagawa, N.2    Yoshimoto, A.3
  • 73
    • 0014984252 scopus 로고
    • Specific inhibition of the cyanide-insensitive respiratory pathway in plant mitochondria by hydroxamic acids
    • Schonbaum GR, Bonner WD Jr, Storey BT, Bahr JT. 1971. Specific inhibition of the cyanide-insensitive respiratory pathway in plant mitochondria by hydroxamic acids. Plant Physiol. 47:124-28
    • (1971) Plant Physiol. , vol.47 , pp. 124-128
    • Schonbaum, G.R.1    Bonner Jr., W.D.2    Storey, B.T.3    Bahr, J.T.4
  • 74
    • 0028089687 scopus 로고
    • Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-Coa desaturase, and are conserved in alkane hydroyxlase and xylene monooxygenase
    • Shanklin J, Whittle E, Fox BG. 1994. Eight histidine residues are catalytically essential in a membrane-associated iron enzyme, stearoyl-CoA desaturase, and are conserved in alkane hydroyxlase and xylene monooxygenase. Biochemistry 33:12,787-94
    • (1994) Biochemistry , vol.33 , pp. 12787-12794
    • Shanklin, J.1    Whittle, E.2    Fox, B.G.3
  • 75
    • 0001628738 scopus 로고
    • Alternative respiratory pathway. Its role in seed respiration and its inhibition by propyl gallate
    • Siedow JN, Girvin ME. 1980. Alternative respiratory pathway. Its role in seed respiration and its inhibition by propyl gallate. Plant Physiol. 65:669-74
    • (1980) Plant Physiol. , vol.65 , pp. 669-674
    • Siedow, J.N.1    Girvin, M.E.2
  • 76
    • 0034663499 scopus 로고    scopus 로고
    • The mitochondrial cyanide-resistant oxidase: Structural conservation amid regulatory diversity
    • Siedow JN, Umbach AL. 2000. The mitochondrial cyanide-resistant oxidase: structural conservation amid regulatory diversity. Biochim. Biophys. Acta 1459:432-39
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 432-439
    • Siedow, J.N.1    Umbach, A.L.2
  • 77
    • 0028904496 scopus 로고
    • The active site of the cyanide-resistant oxidase from plant mitochondria contains a binuclear iron center
    • Siedow JN, Umbach AL, Moore AL. 1995. The active site of the cyanide-resistant oxidase from plant mitochondria contains a binuclear iron center. FEBS Lett. 362:10-14
    • (1995) FEBS Lett. , vol.362 , pp. 10-14
    • Siedow, J.N.1    Umbach, A.L.2    Moore, A.L.3
  • 78
    • 0000208617 scopus 로고    scopus 로고
    • Geometric and electronic structure/function correlations in non-heme iron enzymes
    • Solomon EI, Brunold TC, Davis MI, Kemsley JN, Lee S-K, et al. 2000. Geometric and electronic structure/function correlations in non-heme iron enzymes. Chem. Rev. 100:235-349
    • (2000) Chem. Rev. , vol.100 , pp. 235-349
    • Solomon, E.I.1    Brunold, T.C.2    Davis, M.I.3    Kemsley, J.N.4    Lee, S.-K.5
  • 79
    • 0000125603 scopus 로고
    • Effects of iron and oxygen on chlorophyll biosynthesis. 1. In vivo observations on iron and oxygen-deficient plants
    • Spiller SC, Castelfranco AM, Castelfranco PA. 1982. Effects of iron and oxygen on chlorophyll biosynthesis. 1. In vivo observations on iron and oxygen-deficient plants. Plant Physiol. 69:107-11
    • (1982) Plant Physiol. , vol.69 , pp. 107-111
    • Spiller, S.C.1    Castelfranco, A.M.2    Castelfranco, P.A.3
  • 80
    • 0035823556 scopus 로고    scopus 로고
    • A new member of the family of di-iron carboxylate proteins. Coq7 (clk-1), a membrane-bound hydroxylase involved in ubiquinone biosynthesis
    • Stenmark P, Grünler J, Mattsson J, Sindelar PJ, Nordlund P, Berthold DA. 2001. A new member of the family of di-iron carboxylate proteins. Coq7 (clk-1), a membrane-bound hydroxylase involved in ubiquinone biosynthesis. J. Biol. Chem. 276:33297-300
    • (2001) J. Biol. Chem. , vol.276 , pp. 33297-33300
    • Stenmark, P.1    Grünler, J.2    Mattsson, J.3    Sindelar, P.J.4    Nordlund, P.5    Berthold, D.A.6
  • 82
    • 0037156868 scopus 로고    scopus 로고
    • Activation of the plant mitochondrial alternative oxidase: Insights from site-directed mutagenesis
    • Umbach AL, Gonzàlez-Meler MA, Sweet CR, Siedow JN. 2002. Activation of the plant mitochondrial alternative oxidase: insights from site-directed mutagenesis. Biochim. Biophys. Acta 1554:118-28
    • (2002) Biochim. Biophys. Acta , vol.1554 , pp. 118-128
    • Umbach, A.L.1    Gonzàlez-Meler, M.A.2    Sweet, C.R.3    Siedow, J.N.4
  • 83
    • 0027140930 scopus 로고
    • Covalent and noncovalent dimers of the cyanide-resistant alternative oxidase protein in higher plant mitochondria and their relationship to enzyme activity
    • Umbach AL, Siedow JN. 1993. Covalent and noncovalent dimers of the cyanide-resistant alternative oxidase protein in higher plant mitochondria and their relationship to enzyme activity. Plant Physiol. 103:845-54
    • (1993) Plant Physiol. , vol.103 , pp. 845-854
    • Umbach, A.L.1    Siedow, J.N.2
  • 84
    • 0029744459 scopus 로고    scopus 로고
    • The reaction of the soybean cotyledon mitochondrial cyanide-resistant oxidase with sulfhydryl reagents suggests that α-keto acid activation involves the formation of a thiohemiacetal
    • Umbach AL, Siedow JN. 1996. The reaction of the soybean cotyledon mitochondrial cyanide-resistant oxidase with sulfhydryl reagents suggests that α-keto acid activation involves the formation of a thiohemiacetal. J. Biol. Chem. 271:25019-26
    • (1996) J. Biol. Chem. , vol.271 , pp. 25019-25026
    • Umbach, A.L.1    Siedow, J.N.2
  • 85
    • 0034659895 scopus 로고    scopus 로고
    • The cyanide-resistant alternative oxidases from the fungi Pichia stipitis and Neurospora crassa are monomeric and lack regulatory features of the plant enzyme
    • Umbach AL, Siedow JN. 2000. The cyanide-resistant alternative oxidases from the fungi Pichia stipitis and Neurospora crassa are monomeric and lack regulatory features of the plant enzyme. Arch. Biochem. Biophys. 378:234-45
    • (2000) Arch. Biochem. Biophys. , vol.378 , pp. 234-245
    • Umbach, A.L.1    Siedow, J.N.2
  • 86
    • 0028859022 scopus 로고
    • Alternative oxidase activity in tobacco leaf mitochondria. Dependence on tricarboxylic acid cycle-mediated redox regulation and pyruvate activation
    • Vanlerberghe GC, Day DA, Wiskich JT, Vanlerberghe AE, McIntosh L. 1995. Alternative oxidase activity in tobacco leaf mitochondria. Dependence on tricarboxylic acid cycle-mediated redox regulation and pyruvate activation. Plant Physiol. 109:353-61
    • (1995) Plant Physiol. , vol.109 , pp. 353-361
    • Vanlerberghe, G.C.1    Day, D.A.2    Wiskich, J.T.3    Vanlerberghe, A.E.4    McIntosh, L.5
  • 88
    • 0031772075 scopus 로고    scopus 로고
    • Molecular localization of a redox-modulated process regulating plant mitochondrial electron transport
    • Vanlerberghe GC, McIntosh L, Yip JY. 1998. Molecular localization of a redox-modulated process regulating plant mitochondrial electron transport. Plant Cell 10:1551-60
    • (1998) Plant Cell , vol.10 , pp. 1551-1560
    • Vanlerberghe, G.C.1    McIntosh, L.2    Yip, J.Y.3
  • 89
    • 0034283755 scopus 로고    scopus 로고
    • Cyanide-resistant respiration is frequent, but confined to yeasts incapable of aerobic fermentation
    • Veiga A, Arrabaça JD, Loureiro-Dias MC. 2000. Cyanide-resistant respiration is frequent, but confined to yeasts incapable of aerobic fermentation. FEMS Microbiol. Lett. 190:93-97
    • (2000) FEMS Microbiol. Lett. , vol.190 , pp. 93-97
    • Veiga, A.1    Arrabaça, J.D.2    Loureiro-Dias, M.C.3
  • 90
    • 0025857510 scopus 로고
    • Synthesis of divinyl protochlorophyllide. Enzymological properties of the Mg-protoporphyrin IX monomethyl ester oxidative cyclase system
    • Walker CJ, Castelfranco PA, Whyte BJ. 1991. Synthesis of divinyl protochlorophyllide. Enzymological properties of the Mg-protoporphyrin IX monomethyl ester oxidative cyclase system. Biochem. J. 276:691-97
    • (1991) Biochem. J. , vol.276 , pp. 691-697
    • Walker, C.J.1    Castelfranco, P.A.2    Whyte, B.J.3
  • 91
    • 0038379056 scopus 로고    scopus 로고
    • Identification of xantha l-35 and viridis k-23 as mutants of the Mg-protoporphyrin monomethyl ester cyclase of chlorophyllsynthesis in barley (Hordeum vulgare)
    • Walker CJ, Kannangara CG, Von Wettstein D. 1997. Identification of xantha l-35 and viridis k-23 as mutants of the Mg-protoporphyrin monomethyl ester cyclase of chlorophyllsynthesis in barley (Hordeum vulgare). Plant Physiol. 114:708
    • (1997) Plant Physiol. , vol.114 , pp. 708
    • Walker, C.J.1    Kannangara, C.G.2    Von Wettstein, D.3
  • 92
    • 0024288967 scopus 로고
    • The magnesium-protoporphyrin IX (oxidative) cyclase system. Studies on the mechanism and specificity of the reaction sequence
    • Walker CJ, Mansfield KE, Rezzano IN, Hanamoto CM, Smith KM, Castelfranco PA. 1988. The magnesium-protoporphyrin IX (oxidative) cyclase system. Studies on the mechanism and specificity of the reaction sequence. Biochem. J. 255:685-92
    • (1988) Biochem. J. , vol.255 , pp. 685-692
    • Walker, C.J.1    Mansfield, K.E.2    Rezzano, I.N.3    Hanamoto, C.M.4    Smith, K.M.5    Castelfranco, P.A.6
  • 93
    • 0024969308 scopus 로고
    • Incorporation of atmospheric oxygen into the carbonyl functionality of the protochlorophyllide isocyclic ring
    • Walker CJ, Mansfield KE, Smith KM, Castelfranco PA. 1989. Incorporation of atmospheric oxygen into the carbonyl functionality of the protochlorophyllide isocyclic ring. Biochem. J. 257:599-602
    • (1989) Biochem. J. , vol.257 , pp. 599-602
    • Walker, C.J.1    Mansfield, K.E.2    Smith, K.M.3    Castelfranco, P.A.4
  • 94
    • 0030769202 scopus 로고    scopus 로고
    • Structure and function of a squalene cyclase
    • Wendt KU, Poralla K, Schulz GE. 1997. Structure and function of a squalene cyclase. Science 277:1811-15
    • (1997) Science , vol.277 , pp. 1811-1815
    • Wendt, K.U.1    Poralla, K.2    Schulz, G.E.3
  • 95
    • 0027461261 scopus 로고
    • Further observations on the Mg-protoporphryin IX monomethyl ester (oxidative) cyclase system
    • Whyte BJ, Castelfranco PA. 1993. Further observations on the Mg-protoporphryin IX monomethyl ester (oxidative) cyclase system. Biochem. J. 290:355-59
    • (1993) Biochem. J. , vol.290 , pp. 355-359
    • Whyte, B.J.1    Castelfranco, P.A.2
  • 96
    • 0028950419 scopus 로고
    • Mutations in the clk-1 gene of Caenorhabditis elegans affect developmental and behavioral timing
    • Wong A, Boutis P, Hekimi S. 1995. Mutations in the clk-1 gene of Caenorhabditis elegans affect developmental and behavioral timing. Genetics 139:1247-59
    • (1995) Genetics , vol.139 , pp. 1247-1259
    • Wong, A.1    Boutis, P.2    Hekimi, S.3
  • 98
    • 0032741833 scopus 로고    scopus 로고
    • The IMMUTANS variegation locus of Arabidopsis defines a mitochondrial alternative oxidase homolog that functions during early chloroplast biogenesis
    • Wu D, Wright DA, Wetzel C, Voytas DF, Rodermel S. 1999. The IMMUTANS variegation locus of Arabidopsis defines a mitochondrial alternative oxidase homolog that functions during early chloroplast biogenesis. Plant Cell 11:43-55
    • (1999) Plant Cell , vol.11 , pp. 43-55
    • Wu, D.1    Wright, D.A.2    Wetzel, C.3    Voytas, D.F.4    Rodermel, S.5
  • 100
    • 0034942538 scopus 로고    scopus 로고
    • Mitochondrial alternative oxidase acts to dampen the generation of active oxygen species during a period of rapid respiration induced to support a high rate of nutrient uptake
    • Yip JY, Vanlerberghe GC. 2001. Mitochondrial alternative oxidase acts to dampen the generation of active oxygen species during a period of rapid respiration induced to support a high rate of nutrient uptake. Physiol. Plant. 112:327-33
    • (2001) Physiol. Plant. , vol.112 , pp. 327-333
    • Yip, J.Y.1    Vanlerberghe, G.C.2
  • 101
    • 0031728069 scopus 로고    scopus 로고
    • PNZIP is a novel mesophyll-specific cDNA that is regulated by phytochrome and a circadian rhythm and encodes a protein with a leucine zipper motif
    • Zheng CC, Porat R, Lu P, O'Neill SD. 1998. PNZIP is a novel mesophyll-specific cDNA that is regulated by phytochrome and a circadian rhythm and encodes a protein with a leucine zipper motif. Plant Physiol. 116:27-35
    • (1998) Plant Physiol. , vol.116 , pp. 27-35
    • Zheng, C.C.1    Porat, R.2    Lu, P.3    O'Neill, S.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.