메뉴 건너뛰기




Volumn 39, Issue 2, 1999, Pages 309-323

The role of protein surface charge in catalytic activity and chloroplast membrane association of the pea NADPH: Protochlorophyllide oxidoreductase (POR) as revealed by alanine scanning mutagenesis

Author keywords

Chlorophyll biosynthesis; Chloroplast development; NADPH:protochlorophyllide oxidoreductase; POR; Site directed mutagenesis

Indexed keywords

ALANINE; CATALYSIS; CHLOROPLAST; CLUSTER ANALYSIS; ENZYME ACTIVITY; MEMBRANE; MUTAGENESIS; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PLANT DEVELOPMENT; PROTEIN ANALYSIS; PROTOCHLOROPHYLLIDE OXIDOREDUCTASE;

EID: 0033063166     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006135100760     Document Type: Article
Times cited : (43)

References (51)
  • 1
    • 0028841585 scopus 로고
    • Involvement of the C-terminal tail in the activity of Drosophila alcohol dehydrogenase. Evaluation of truncated proteins constructed by site-directed mutagenesis
    • Albalat R, Valls M, Fibla J, Atrian S, Gonzàlez-Duarte R: Involvement of the C-terminal tail in the activity of Drosophila alcohol dehydrogenase. Evaluation of truncated proteins constructed by site-directed mutagenesis. Eur J Biochem 233: 508-505 (1995).
    • (1995) Eur J Biochem , vol.233 , pp. 508-1505
    • Albalat, R.1    Valls, M.2    Fibla, J.3    Atrian, S.4    Gonzàlez-Duarte, R.5
  • 2
    • 0028226211 scopus 로고
    • Protochlorophyllide reductase is homologous to human carbonyl reductase and pig 20β-hydroxysteriod dehydrogenase
    • Baker ME: Protochlorophyllide reductase is homologous to human carbonyl reductase and pig 20β-hydroxysteriod dehydrogenase. Biochem J 300: 605-607 (1994).
    • (1994) Biochem J , vol.300 , pp. 605-607
    • Baker, M.E.1
  • 3
    • 0000574962 scopus 로고
    • Photoenzymes: A novel class of biological catalysts
    • Begley TP: Photoenzymes: a novel class of biological catalysts. Ace Chem Res 27: 394-401 (1994).
    • (1994) Ace Chem Res , vol.27 , pp. 394-401
    • Begley, T.P.1
  • 4
    • 0000501058 scopus 로고
    • Protochlorophyllide reductase. I. Determination of the regiochemistry and the stereochemistry of the reduction of protochlorophyllide to chlorophyllide
    • Begley TP, Young H: Protochlorophyllide reductase. I. Determination of the regiochemistry and the stereochemistry of the reduction of protochlorophyllide to chlorophyllide. J Am Chem Soc 111: 3095-3096 (1989).
    • (1989) J Am Chem Soc , vol.111 , pp. 3095-3096
    • Begley, T.P.1    Young, H.2
  • 5
    • 0030056704 scopus 로고    scopus 로고
    • Secondary structure of NADPH:protochlorophyllide oxidoreductase examined by circular dichroism and prediction methods
    • Birve SJ, Selstam E, Johansson B-A: Secondary structure of NADPH:protochlorophyllide oxidoreductase examined by circular dichroism and prediction methods. Biochem J 317: 549-555 (1996).
    • (1996) Biochem J , vol.317 , pp. 549-555
    • Birve, S.J.1    Selstam, E.2    Johansson, B.-A.3
  • 6
    • 0029039935 scopus 로고
    • Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase
    • Cheneveret SW, Fossett NG, Chang SH, Tsigelny I, Baker ME, Lee WR: Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase. Biochem J 308: 419-423 (1995).
    • (1995) Biochem J , vol.308 , pp. 419-423
    • Cheneveret, S.W.1    Fossett, N.G.2    Chang, S.H.3    Tsigelny, I.4    Baker, M.E.5    Lee, W.R.6
  • 7
    • 0022851237 scopus 로고
    • Import of proteins into chloroplasts. Membrane integration of a thylakoid precursor protein reconstituted in chloroplast lysates
    • Cline K: Import of proteins into chloroplasts. Membrane integration of a thylakoid precursor protein reconstituted in chloroplast lysates. J Biol Chem 261: 14804-14810 (1986).
    • (1986) J Biol Chem , vol.261 , pp. 14804-14810
    • Cline, K.1
  • 8
    • 0029731659 scopus 로고    scopus 로고
    • Import and routing of nucleus-encoded chloroplast proteins
    • Cline K, Henry R: Import and routing of nucleus-encoded chloroplast proteins. Annu Rev Cell Dev Biol 12: 1-26 (1996).
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 1-26
    • Cline, K.1    Henry, R.2
  • 9
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham BC, Wells JA: High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 245: 1081-1085 (1989).
    • (1989) Science , vol.245 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 10
    • 0028003222 scopus 로고
    • Integration of nuclear-encoded proteins into carotenoid-deficient pea thylakoids
    • Dahlin C, Timko MP: Integration of nuclear-encoded proteins into carotenoid-deficient pea thylakoids. Physiol Plant 91: 212-218 (1994).
    • (1994) Physiol Plant , vol.91 , pp. 212-218
    • Dahlin, C.1    Timko, M.P.2
  • 11
    • 0029379838 scopus 로고
    • The in vitro assembly of NADPH-protochlorophyllide oxidoreductase in pea chloroplasts
    • Dahlin C, Sundqvist C, Tiniko MP: The in vitro assembly of NADPH-protochlorophyllide oxidoreductase in pea chloroplasts. Plant Mol Biol 29: 317-330 (1995).
    • (1995) Plant Mol Biol , vol.29 , pp. 317-330
    • Dahlin, C.1    Sundqvist, C.2    Tiniko, M.P.3
  • 12
    • 0030175228 scopus 로고    scopus 로고
    • Protochlorophyllide reduction: A key step in the greening of plants
    • Fujita Y: Protochlorophyllide reduction: a key step in the greening of plants. Plant Cell Physiol 37: 411-421 (1996).
    • (1996) Plant Cell Physiol , vol.37 , pp. 411-421
    • Fujita, Y.1
  • 13
    • 0025838697 scopus 로고
    • Three-dimensional structure of holo 3α, 20β-hydroxysteriod dehydrogenase: A member of a short-chain dehydrogenase family
    • Ghosh D, Weeks CM, Grochulski P, Duax WL, Erman M, Rimsay RM, Orr JC: Three-dimensional structure of holo 3α, 20β-hydroxysteriod dehydrogenase: a member of a short-chain dehydrogenase family. Proc Natl Acad Sci USA 88: 10064-10068 (1991).
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10064-10068
    • Ghosh, D.1    Weeks, C.M.2    Grochulski, P.3    Duax, W.L.4    Erman, M.5    Rimsay, R.M.6    Orr, J.C.7
  • 14
    • 0028773893 scopus 로고
    • The refined three-dimensional structure of 3α, 20β-hydroxysteriod dehydrogenase and possible roles of the residues conserved in the short-chain dehydrogenases
    • Ghosh D, Wawrzak Z, Weeks CM, Duax WL, Erman M: The refined three-dimensional structure of 3α, 20β-hydroxysteriod dehydrogenase and possible roles of the residues conserved in the short-chain dehydrogenases. Structure 2: 629-640 (1994).
    • (1994) Structure , vol.2 , pp. 629-640
    • Ghosh, D.1    Wawrzak, Z.2    Weeks, C.M.3    Duax, W.L.4    Erman, M.5
  • 15
    • 0018076305 scopus 로고
    • Reconstitution of chlorophyllide formation by isolated etioplast membranes
    • Griffiths WT: Reconstitution of chlorophyllide formation by isolated etioplast membranes. Biochem J 174: 681-692 (1978).
    • (1978) Biochem J , vol.174 , pp. 681-692
    • Griffiths, W.T.1
  • 16
    • 0018864205 scopus 로고
    • Substrate-specificity studies on protochlorophyllide reductase in barley (Hordeum vulgare) etioplast membranes
    • Griffiths WT: Substrate-specificity studies on protochlorophyllide reductase in barley (Hordeum vulgare) etioplast membranes. Biochem J 186: 267-278 (1980).
    • (1980) Biochem J , vol.186 , pp. 267-278
    • Griffiths, W.T.1
  • 17
    • 0001685686 scopus 로고
    • Protochlorophyllide photoreduction
    • Scheer H (ed) CRC Press, Boca Raton, FL
    • Griffiths WT: Protochlorophyllide photoreduction. In: Scheer H (ed) The Chlorophylls, pp. 433-449. CRC Press, Boca Raton, FL (1991).
    • (1991) The Chlorophylls , pp. 433-449
    • Griffiths, W.T.1
  • 18
    • 0030566829 scopus 로고    scopus 로고
    • The light intensity dependence of protochlorophyllide photoconversion and its significance to the catalytic mechanism of protochlorophyllide reductase
    • Griffiths WT, McHugh T, Blankenship RE: The light intensity dependence of protochlorophyllide photoconversion and its significance to the catalytic mechanism of protochlorophyllide reductase. FEBS Lett 398: 236-238 (1996).
    • (1996) FEBS Lett , vol.398 , pp. 236-238
    • Griffiths, W.T.1    McHugh, T.2    Blankenship, R.E.3
  • 20
    • 0029873809 scopus 로고    scopus 로고
    • Absolute configuration of protochlorophyllide alpha and substrate specificity of NADPH-protochlorophyllide oxidoreductase
    • Helfrich M, Schoch S, Schafer W, Ryberg M, Rudiger W: Absolute configuration of protochlorophyllide alpha and substrate specificity of NADPH-protochlorophyllide oxidoreductase. J Am Chem Soc 118: 2606-2611 (1996).
    • (1996) J Am Chem Soc , vol.118 , pp. 2606-2611
    • Helfrich, M.1    Schoch, S.2    Schafer, W.3    Ryberg, M.4    Rudiger, W.5
  • 22
    • 0026495412 scopus 로고
    • Alanine scanning mutagenesis identifies surface amino acids on Domain II of Pseudomonas exotoxin required for cytotoxicity, proper folding, and secretion into periplasm
    • Kasturi S, Kihara A, FitzGerald D, Pastan I: Alanine scanning mutagenesis identifies surface amino acids on Domain II of Pseudomonas exotoxin required for cytotoxicity, proper folding, and secretion into periplasm. J Biol Chem 267: 23427-23433 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 23427-23433
    • Kasturi, S.1    Kihara, A.2    Fitzgerald, D.3    Pastan, I.4
  • 23
    • 0000668045 scopus 로고
    • Light-induced breakdown of NADPH-protochlorophyllide oxidoreductase in vitro
    • Kay SA, Griffiths WT: Light-induced breakdown of NADPH-protochlorophyllide oxidoreductase in vitro. Plant Physiol 72: 229-236 (1983).
    • (1983) Plant Physiol , vol.72 , pp. 229-236
    • Kay, S.A.1    Griffiths, W.T.2
  • 24
    • 0027423150 scopus 로고
    • Phototransformation of monovinyl and divinyl protochlorophyllide by NADPH: Protochlorophyllide oxidoreductase of barley expressed in Escherichia coli
    • Knaust R, Seyfried B, Schmidt L, Schulz R, Senger H: Phototransformation of monovinyl and divinyl protochlorophyllide by NADPH: protochlorophyllide oxidoreductase of barley expressed in Escherichia coli. J Photochem Photobiol B -Biology 20: 161-166 (1993).
    • (1993) J Photochem Photobiol B -Biology , vol.20 , pp. 161-166
    • Knaust, R.1    Seyfried, B.2    Schmidt, L.3    Schulz, R.4    Senger, H.5
  • 26
    • 0028051740 scopus 로고
    • Structural comparisons lead to the definition of a new superfamily of NAD(P)(H)-accepting oxidoreductases: The single-domain reductases/epimerases/dehydrogenases (the 'RED' family)
    • Labesse G, Vidat-Cors A, Chomilier J, Gaudry M, Momon J-P: Structural comparisons lead to the definition of a new superfamily of NAD(P)(H)-accepting oxidoreductases: the single-domain reductases/epimerases/dehydrogenases (the 'RED' family). Biochem J 304: 95-99 (1994).
    • (1994) Biochem J , vol.304 , pp. 95-99
    • Labesse, G.1    Vidat-Cors, A.2    Chomilier, J.3    Gaudry, M.4    Momon, J.-P.5
  • 28
    • 0030061989 scopus 로고    scopus 로고
    • The pc-1 phenotype of Chlamydomonas reinhardtii results from a deletion mutation in the nuclear gene for NADPH: Protochlorophyllide oxidoreductase
    • Li J, Timko MP: The pc-1 phenotype of Chlamydomonas reinhardtii results from a deletion mutation in the nuclear gene for NADPH: protochlorophyllide oxidoreductase. Plant Mol Biol 30: 15-37 (1996).
    • (1996) Plant Mol Biol , vol.30 , pp. 15-37
    • Li, J.1    Timko, M.P.2
  • 29
    • 0026051796 scopus 로고
    • PsaD is required for the stable binding of PsaC to the photosystem I core protein of Synechococcus sp. PCC 6301
    • Li N, Zhao J, Warren PV, Warden JT, Bryan DA, Golbeck JH: PsaD is required for the stable binding of PsaC to the photosystem I core protein of Synechococcus sp. PCC 6301. Biochemistry 30: 7863-7872 (1991).
    • (1991) Biochemistry , vol.30 , pp. 7863-7872
    • Li, N.1    Zhao, J.2    Warren, P.V.3    Warden, J.T.4    Bryan, D.A.5    Golbeck, J.H.6
  • 30
    • 0000444532 scopus 로고
    • Determination of total carotenoids and chlorophylls a and b of leaf extracts in different solvents
    • Lichtenthaler HK, Weilburn AR: Determination of total carotenoids and chlorophylls a and b of leaf extracts in different solvents. Biochem Soc Trans 603: 591-592 (1983).
    • (1983) Biochem Soc Trans , vol.603 , pp. 591-592
    • Lichtenthaler, H.K.1    Weilburn, A.R.2
  • 31
    • 0030860298 scopus 로고    scopus 로고
    • Purification and kinetic analysis of pea NADPH-protochlorophyllide oxidore-ductase expressed as a fusion with maltose-binding protein in Escherichia coli
    • Martin GEM, Timko MP and Wilks HM: Purification and kinetic analysis of pea NADPH-protochlorophyllide oxidore-ductase expressed as a fusion with maltose-binding protein in Escherichia coli. Biochem J 325: 139-145 (1997).
    • (1997) Biochem J , vol.325 , pp. 139-145
    • Martin, G.E.M.1    Timko, M.P.2    Wilks, H.M.3
  • 32
    • 0015860676 scopus 로고
    • Action spectra for biosynthesis of chlorophylls a and b and β-carotene
    • Ogawa T, Inoue Y, Kitajima M, Shibata K: Action spectra for biosynthesis of chlorophylls a and b and β-carotene. Photochem Photobiol 18: 229-235 (1973).
    • (1973) Photochem Photobiol , vol.18 , pp. 229-235
    • Ogawa, T.1    Inoue, Y.2    Kitajima, M.3    Shibata, K.4
  • 34
    • 0025883535 scopus 로고
    • Characteristics of short-chain alcohol dehydrogenases and related enzymes
    • Persson B, Krook M, Jörnvall H: Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur J Biochem 200: 537-543 (1991).
    • (1991) Eur J Biochem , vol.200 , pp. 537-543
    • Persson, B.1    Krook, M.2    Jörnvall, H.3
  • 35
    • 0029926078 scopus 로고    scopus 로고
    • The regulation of enzymes involved in chlorophyll biosynthesis
    • Reinbothe S, Reinbothe C: The regulation of enzymes involved in chlorophyll biosynthesis. Eur J Biochem 237: 323-343 (1996).
    • (1996) Eur J Biochem , vol.237 , pp. 323-343
    • Reinbothe, S.1    Reinbothe, C.2
  • 36
    • 0028784796 scopus 로고
    • A light-induced protease from barley plastids degrades NADPH:protochlorophyllide oxidoreductase completed with chlorophyllide
    • Reinbothe C, Apel K, Reinbothe S: A light-induced protease from barley plastids degrades NADPH:protochlorophyllide oxidoreductase completed with chlorophyllide. Mol Cell Biol 15: 6206-6212 (1995).
    • (1995) Mol Cell Biol , vol.15 , pp. 6206-6212
    • Reinbothe, C.1    Apel, K.2    Reinbothe, S.3
  • 37
    • 0000448607 scopus 로고    scopus 로고
    • PORA and PORB, two light-dependent protochlorophyllide-reducing enzymes of angiosperm chlorophyll biosynthesis
    • Reinbothe S, Reinbothe C, Lebedev N, Apel K: PORA and PORB, two light-dependent protochlorophyllide-reducing enzymes of angiosperm chlorophyll biosynthesis. Plant Cell 8: 763-769 (1996).
    • (1996) Plant Cell , vol.8 , pp. 763-769
    • Reinbothe, S.1    Reinbothe, C.2    Lebedev, N.3    Apel, K.4
  • 38
    • 0028907432 scopus 로고
    • Enzymatic product formation impairs both the chloroplast receptor-binding function as well as translocation competence of the NADPH:protochlorophyllide oxidoreductase, a nuclear-encoded plast precursor protein
    • Reinbothe S, Reinbothe C, Runge S, Apel K: Enzymatic product formation impairs both the chloroplast receptor-binding function as well as translocation competence of the NADPH:protochlorophyllide oxidoreductase, a nuclear-encoded plast precursor protein. J Cell Biol 129: 299-308 (1995).
    • (1995) J Cell Biol , vol.129 , pp. 299-308
    • Reinbothe, S.1    Reinbothe, C.2    Runge, S.3    Apel, K.4
  • 39
    • 0029240288 scopus 로고
    • Substrate-dependent transport of the NADPH:protochlorophyllide oxidoreductase into isolated plastids
    • Reinbothe S, Runge S, Reinbothe C, van Cleve B, Apel K: Substrate-dependent transport of the NADPH:protochlorophyllide oxidoreductase into isolated plastids. Plant Cell 7: 161-172 (1995).
    • (1995) Plant Cell , vol.7 , pp. 161-172
    • Reinbothe, S.1    Runge, S.2    Reinbothe, C.3    Van Cleve, B.4    Apel, K.5
  • 40
    • 0028519276 scopus 로고
    • Targeting of proteins into and across the thylakoid membrane: A multitude of mechanisms
    • Robinson C, Klösgen RB: Targeting of proteins into and across the thylakoid membrane: a multitude of mechanisms. Plant Mol Biol 26: 15-24 (1994).
    • (1994) Plant Mol Biol , vol.26 , pp. 15-24
    • Robinson, C.1    Klösgen, R.B.2
  • 41
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A, Blundell TL: Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol 234: 779-815 (1993).
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 42
    • 0024676061 scopus 로고
    • Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli
    • Schulz R, Steinmuller K, Klaas M, Forreiter C, Rasmussen S, Hiller C, Apel K: Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli. Mol Gen Genet 217: 355-361 (1989).
    • (1989) Mol Gen Genet , vol.217 , pp. 355-361
    • Schulz, R.1    Steinmuller, K.2    Klaas, M.3    Forreiter, C.4    Rasmussen, S.5    Hiller, C.6    Apel, K.7
  • 43
    • 0026824270 scopus 로고
    • Molecular cloning, nuclear gene structure, and developmental expression of NADPH: Protochlorophyllide oxidoreductase in pea (Pisum sativum L.)
    • Spano AJ, He Z, Michel H, Hunt DF, Timko MP: Molecular cloning, nuclear gene structure, and developmental expression of NADPH: protochlorophyllide oxidoreductase in pea (Pisum sativum L.). Plant Mol Biol 18: 967-972 (1992).
    • (1992) Plant Mol Biol , vol.18 , pp. 967-972
    • Spano, A.J.1    He, Z.2    Michel, H.3    Hunt, D.F.4    Timko, M.P.5
  • 44
    • 0030869207 scopus 로고    scopus 로고
    • With chlorophyll pigments from prolamellar bodies to light-harvesting complexes
    • Sundqvist C, Dahlin C: With chlorophyll pigments from prolamellar bodies to light-harvesting complexes. Physiol Plant 100: 748-759 (1997).
    • (1997) Physiol Plant , vol.100 , pp. 748-759
    • Sundqvist, C.1    Dahlin, C.2
  • 45
    • 0029643855 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8Å resolution: The structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family
    • Tanaka N, Nonaka T, Nakanishi M, Deyashiki Y, Hara A, Mitsui Y: Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8Å resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family. Structure 4: 33-45 (1996).
    • (1996) Structure , vol.4 , pp. 33-45
    • Tanaka, N.1    Nonaka, T.2    Nakanishi, M.3    Deyashiki, Y.4    Hara, A.5    Mitsui, Y.6
  • 46
    • 0029619241 scopus 로고
    • Structures stabilizing the dimer interface on human 11β-hydroxysteriod dehydrogenase types 1 and 2 and human 15-hydroxyprostaglandin dehydrogenase and their homologues
    • Tsigelny I, Baker ME: Structures stabilizing the dimer interface on human 11β-hydroxysteriod dehydrogenase types 1 and 2 and human 15-hydroxyprostaglandin dehydrogenase and their homologues. Biochem Biophys Res Comm 217: 859-868 (1995).
    • (1995) Biochem Biophys Res Comm , vol.217 , pp. 859-868
    • Tsigelny, I.1    Baker, M.E.2
  • 47
    • 0023653468 scopus 로고
    • Synthesis of 4R- and 4S-tritium labeled NADPH for determination of the coenzyme stereospecificity of NADPH:protochlorophyllide oxidoreductase
    • Valera V, Fung M, Wessler AN, Richards: Synthesis of 4R- and 4S-tritium labeled NADPH for determination of the coenzyme stereospecificity of NADPH:protochlorophyllide oxidoreductase. Biochem Biophys Res Comm 148: 515-520 (1987).
    • (1987) Biochem Biophys Res Comm , vol.148 , pp. 515-520
    • Valera, V.1    Fung, M.2    Wessler, A.N.3    Richards4
  • 48
    • 0019495032 scopus 로고
    • Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase
    • Wermuth B: Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase. J Biol Chem 256: 1206-1213 (1981).
    • (1981) J Biol Chem , vol.256 , pp. 1206-1213
    • Wermuth, B.1
  • 49
    • 0026737363 scopus 로고
    • Systematic mutational analysis of the yeast ACT1 gene
    • Wertman KF, Drubin DG, Botstein D: Systematic mutational analysis of the yeast ACT1 gene. Genetics 132: 337-350 (1992).
    • (1992) Genetics , vol.132 , pp. 337-350
    • Wertman, K.F.1    Drubin, D.G.2    Botstein, D.3
  • 50
    • 0027174457 scopus 로고
    • 8-Vinyl reduction and chlorophyll a biosynthesis in higher plants
    • Whyte BJ, Griffiths WT: 8-Vinyl reduction and chlorophyll a biosynthesis in higher plants. Biochem J 291: 939-944 (1993).
    • (1993) Biochem J , vol.291 , pp. 939-944
    • Whyte, B.J.1    Griffiths, W.T.2
  • 51
    • 0028895568 scopus 로고
    • A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase. Identification and mutagenesis of two conserved residues that are essential for enzyme activity
    • Wilks HM, Timko MP: A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase. Identification and mutagenesis of two conserved residues that are essential for enzyme activity. Proc Natl Acad Sci USA 92: 724-728 (1995).
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 724-728
    • Wilks, H.M.1    Timko, M.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.