Pre-loading of chlorophyll synthase with tetraprenyl diphosphate is an obligatory step in chlorophyll biosynthesis

Biological Chemistry

Volumn 383, Issue 11, 2002, Pages 1769-1778

  Schmid, Heide C ^a   Rassadina, Valentina ^b   Oster, Ulrike ^a   Schoch, Siegrid ^a   Rüdiger, Wolfhart ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b INSTITUTE OF PHOTOBIOLOGY   (Belarus)

Author keywords

Chlorophyll biosynthesis; Ping pong reaction mechanism; Prenylation reaction; Zinc pheophorbides

Indexed keywords

CHLOROPHYLL; CHLOROPHYLLIDE; PHOSPHATE; RECOMBINANT ENZYME; SYNTHETASE;

AMINO ACID SEQUENCE; ARTICLE; BARLEY; BIOSYNTHESIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; ESTERIFICATION; INCUBATION TIME; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION;

AVENA SATIVA; BLOTTING, WESTERN; CARBON-OXYGEN LIGASES; CARRIER PROTEINS; CHLOROPHYLL; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CLONING, MOLECULAR; DITERPENES; ESCHERICHIA COLI; KINETICS; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS;

AVENA; AVENA SATIVA; ESCHERICHIA COLI; HORDEUM VULGARE SUBSP. VULGARE;

EID: 12244256370     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2002.198     Document Type: Article

References (29)

1. Beisiegel, U. (1986). Protein blotting. Electrophoresis 7, 1-18.
2. Bollivar, D. W., Wang, S., Allen, J. P., and Bauer, C. E. (1994). Molecular genetic analysis of terminal steps in bacteriochlorophyll a biosynthesis: characterization of a Rhodobacter capsulatus strain that synthesizes geranylgeraniol-esterified bacteriochlorophyll a. Biochemistry 33, 12763-12768.
3. Domanskii, V. P., and Rüdiger, W. (2001). On the nature of the two pathways in chlorophyll formation from protochlorophyllide. Photosynth. Res. 68, 131-139.
4. Gaubier, P., Wu, H.-J., Laudie, M., Delseny, M., and Grellet, F. (1995). A Chl synthetase gene from Arabidopsis thaliana. Mol. Gen. Genet. 249, 58-64.
5. Griffiths, W. T. (1991). Protochlorophyllide photoreduction. In: Chlorophylls, H. Scheer, ed. (Boca Raton, USA: CRC Press, Inc.), pp. 433-450.
6. Helfrich, M. (1995). Chemische Modifikation von Chlorophyll-Vorstufen und deren Verwendung zur Charakterisierung von Enzymen der Chlorophyll-Biosynthese. Ph.D. Thesis, University of Munich, Germany.
7. Helfrich, M., Schoch, S., Lempert, U., Cmiel, E., and Rüdiger, W. (1994). Chlorophyll synthetase cannot synthesize chlorophyll a'. Eur. J. Biochem. 219, 267-275.
8. Helfrich, M., Schoch, S., Schäfer, W., Ryberg, M., and Rüdiger, W. (1996). Absolute configuration of protochlorophyllide a and substrate specificity of NADPH-protochlorophyllide oxidoreductase. J. Am. Chem. Soc. 118, 2606-2611.
9. Holt, A. S., and Morley, H. V. (1959). A proposed structure for chlorophyll d. Can. J. Chem. 37, 507-514.
10. Jones, I. D., White, R. C., Gibbs, E., and Butler, L. S. (1977). Estimation of zinc pheophytins, chlorophylls, and pheophytins in mixtures in diethyl ether or 80% acetone by spectrophotometry and fluorometry. Agric. Food Chem. 25, 146-149.
11. Keller, Y., Bouvier, F. D., and Harlingue, A. (1998). Metabolic compartmentation of plastid prenyllipid biosynthesis: evidence for the involvement of a multifunctional CHL P. Eur. J. Biochem. 251, 413-417.
12. Klement, H., Helfrich, M., Schoch, S., Oster, U., and Rüdiger, W. (1999). Pigment-free NADPH:protochlorophyllide oxidoreductase from Avena sativa L.: purification and substrate specificity. Eur. J. Biochem. 265, 862-874.
13. Kral, A. M., Diehl, R. E., deSolms, S. J., Williams, T. M., Kohl, N. E., and Omer, C. A. (1997). Mutational analysis of conserved residues of the B-subunit of human farnesyl: protein transferase. J. Biol. Chem. 272, 27319-27323.
14. Kyhse-Andersen, J. (1984). Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods 10, 203-209.
15. Lebedev, N., and Timko, M. P. (1998). Protochlorophyllide photoreduction. Photosynth. Res. 58, 5-23.
16. Lindsten, A., Welch, C. J., Schoch, S., Ryberg, M., Rüdiger, W., and Sundqvist, C. (1990). Chlorophyll synthase is latent in well preserved prolamellar bodies of etiolated wheat. Physiol. Plant. 80, 277-285.
17. Lopez, J. C., Ryan, S., and Blankenship, R. E. (1996). Sequence of the bxhG gene from Chloroflexus aurantiacus: relationship between chlorophyll synthase and other polyprenyltransferases. J. Bacteriol. 178, 3369-3373.
18. Oster, U., and Rüdiger, W. (1997). The G4 gene of Arabidopsis thaliana encodes a chlorophyll synthase of etiolated plants. Bot. Acta 110, 420-423.
19. Oster, U., Bauer, C. E., and Rüdiger, W. (1997). Characterization of chlorophyll a and bacteriochlorophyll a synthases by heterologous expression in Escherichia coli. J. Biol. Chem. 272, 9671-9676.
20. Melzer, M., and Heide, L. (1994). Characterization of polyprenyidiphosphate:4-hydroxybenzoate polyprenyltransferase from Escherichia coli. Biochim. Biophys. Acta 1212, 93-102.
21. Pennington, F. C., Strain, H. H., Svec, W. A., and Katz, J. J. (1964). Preparation and properties of pyrochlorophyll a, methyl pyrochlorophyllide a, pyropheophytin a, and methyl pyropheophorbide a derived from chlorophyll by decarbomethoxylation. J. Am. Chem. Soc. 86, 1418-1426.
22. Porra, R. J. (1991). Recent advances and re-assessments in chlorophyll extraction and assay procedures for terrestrial, aquatic, and marine organisms, including recalcitrant algae. In: Chlorophylls, H. Scheer, ed. (Boca Raton, USA: CRC Press, Inc.), pp. 31-57.
23. Schmid, H. C., Oster, U., Kögel, J., Lenz, S., and Rüdiger, W. (2001). Cloning and characterisation of chlorophyll synthase from Avena sativa. Biol. Chem. 382, 903-911.
24. Schoch, S. (1978). The esterification of chlorophyllide a in greening bean leaves. Z. Naturforsch. 33, 712-714.
25. Schoch, S., Lempert, U., and Rüdiger, W. (1977). Über die letzten Stufen der Chlorophyllbiosynthese: Zwischenprodukte zwischen Chlorophyllid und phytolhaltigem Chlorophyll. Z. Pflanzenphysiol. 83, 427-436.
26. Soll, J., Schultz, G., Rüdiger, W., and Benz, J. (1983). Hydrogenation of geranylgeraniol: two pathways exist in spinach chloroplasts. Plant Physiol. 71, 849-854.
27. Tarshis, L. C., Proteau, P. J., Kellogg, B. A., Sacchettini, J. C., and Poulter, C. D. (1996). Regulation of product chain length by isoprenyl diphosphate synthases. Proc. Natl. Acad. Sci. USA 93, 15018-15023.
28. Voet, D., and Voet, J. G. (1990). Biochemistry (New York, USA: Wiley & Sons, Inc.), p. 348.
29. Wang, K., and Ohnuma, S. (1999). Chain-length determination mechanism of isoprenyl diphosphate synthases and implications for molecular evolution. Trends Biochem. Sci. 24, 445-451.