Recent progress in porphyrin and chlorophyll biosynthesis

Photochemistry and Photobiology

Volumn 65, Issue 3, 1997, Pages 492-516

  Porra, Robert J ^a,b  

^a UNIVERSITY OF MUNICH   (Germany)

^b CSIRO   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0030971852     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1997.tb08596.x     Document Type: Review

References (302)

1. Battersby, A. R. and F. J. Leeper (1990) Biosynthesis of the pigments of life: mechanistic studies on the conversion of porphobilinogen to uroporphyrinogen III. Chem. Rev. 90, 1261-1274.
2. Scheer, H. (1991) Chemistry of chlorophylls. In Chlorophylls (Edited by H. Scheer), pp. 3-30. CRC Press, Boca Raton, FL.
3. Jordan, P. M. (ed.) (1991) Biosynthesis of Tetrapyrroles. Elsevier, Amsterdam.
4. Deisenhofer, J. and J. R. Norris (eds.) (1993) The Photosynthetic Reaction Center. Academic Press, New York.
5. Senge, M. O. (1993). Recent advances in the biosynthesis and chemistry of the chlorophylls. Photochem. Photobiol. 57, 189-206.
6. Bryant, D. A. (ed.) (1994). The Molecular Biology of Cyanobacteria. Kluwer, Dordrecht.
7. Chadwick, D. J. and K. Ackrill (eds.) (1994). The Biosynthesis of the Tetrapyrrole Pigments. Ciba Symposium 180, John Wiley and Sons, Chichester.
8. Blankenship, R., M. T. Madigan and C. E. Bauer (eds.) (1995) Anoxygenic Photosynthetic Bacteria. Kluwer, Dordrecht.
9. 12. Science 264, 1551-1557.
10. Avissar, Y. J. and P. A. Moberg (1995) The common origins of the pigments of life: early steps of chlorophyll biosynthesis. Photosynth. Res. 44, 221-242.
11. Jeffrey, S. W. (1997) Appendix B: structural relationships between algal chlorophylls. In Phytoplankton Pigments in Oceanography: Guidelines to Modern Methods. (Edited by S. W. Jeffrey, R. F. C. Mantoura and S. W. Wright), pp. 566-571. UNESCO, Paris.
12. Kessel, D. (1984) Tumor localization and photosensitization by derivatives of haematoporphyrin: a review. IEEE J. Quantum Electronics QE-23, 1718-1720
13. Bonnett, R. (1989) Tumour photochemotherapy. Spectrum 218, 8-10.
14. Moss, G. P. (1987) Nomenclature of tetrapyrroles. Pure & Appl. Chem. 59, 779-832.
15. Bauer, C. E., D. W. Bollivar and J. Y. Suzuki (1993) Genetic analysis of photopigment biosynthesis in Eubacteria: a guiding light for algae and plants. J. Bacteriol. 175, 3919-3925.
16. Jordan, P. M. (1991) The biosynthesis of 5-aminolaevulinic acid and its transformation into uroporphyrinogen III. In Biosynthesis of Tetrapyrroles (Edited by P. M. Jordan), pp. 1-66. Elsevier, Amsterdam.
17. Warren, M. J., E. Bolt and S. C. Woodcock (1994) 5-Aminolaevulinic acid and uroporphyrinogen methylase: two key control enzymes of tetrapyrrole biosynthesis and modification. In The Biosynthesis of the Tetrapyrrole Pigments, Ciba Symposium 180 (Edited by D. J. Chadwick and K. Ackrill), pp. 26-40. John Wiley and Sons, Chichester.
18. Ferreira, G. C., P. J. Neame and H. A. Dailey (1993) Heme biosynthesis in mammalian systems: evidence of a Schiff base linkage between the pyridoxal 5́-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase. Protein Sci. 2, 1959-1965.
19. Ferreira, G. C. and J. Gong (1995) 5-Aminolevulinate synthase and the first step of heme biosynthesis. J. Bioenerg. Biomembr. 27, 151-159.
20. Ferreira, G. C., U. Vajapey, O. Hafez, G. A. Hunter and M. J. Barber (1995) Aminolevulinate synthase: lysine 313 is not essential for binding the pyridoxal phosphate co-factor but is essential for catalysis. Protein Sci. 4, 1001-1006.
21. Gong, J. and G. C. Ferreira (1995) Aminolevulinate synthase: functionally important residues at a glycine loop, a putative pyridoxal phosphate co-factor binding site. Biochemistry 34, 1678-1685.
22. Avissar, Y. J., J. G. Ormerod and S. I. Beale (1989) Distribution of δ-aminolevulinic acid biosynthetic pathways among phototropic bacterial groups. Arch. Microbiol. 151, 513-519.
23. Kannangara, C. G., S. P. Gough, P. Bruyant, J. K. Hoober, A. Kahn and D. von Wettstein (1988) tRNA as a cofactor in δ-aminolevulinate biosynthesis: steps that regulate chlorophyll synthesis. Trends Biochem. Sci. 13, 139-143.
24. Laver, W. G., A. Neuberger and S. Udenfriend (1958) The initial stages in the biosynthesis of porphyrins. 1. The formation of δ-aminolaevulic acid by particles obtained from chicken erythrocytes. Biochem. J. 70, 4-14.
25. Borthwick, I. A., G. Srivastava, J. D. Brooker, B. K. May and W. H. Elliott (1983) Purification of 5-aminolaevulinate synthase from liver mitochondria of chick embryo. Eur. J. Biochem. 129, 615-620.
26. Ohashi, A. and G. Kikuchi (1979) Purification and some properties of two forms of 8-aminolevulinate synthase from rat liver cytosol. J. Biochem. 85, 239-247.
27. Beale, S. I., T. Foley and V. Dzelzkalns (1981) δ-Aminolaevulinic acid synthase from Euglena gracilis. Proc Nat. Acad. Sci USA. 78, 1666-1669.
28. Weinstein, J. D. and S. I. Beale (1983) Separate physiological roles and subcellular compartments for two tetrapyrrole biosynthetic pathways in Euglena gracilis. J. Biol. Chem. 258, 6799-6807.
29. 5 and the Shemin pathway, in the pigment mutant C-2A' of Scenedesmus obliquus. Z. Naturforsch. C 48, 584-589.
30. Porra, R. J., R. Barnes and O. T. G. Jones (1972) The level and subcellular distribution of δ-aminolaevulinate synthase activity in semi-anaerobic and aerobic yeast. Hoppe-Seyler's Z. Physiol. Chem. 353, 1365-1368.
31. Volland, C. and F. Felix (1984) Isolation and properties of 5-aminolaevulinate synthase from Saccharomyces cerevisiae. Eur. J. Biochem. 142, 551-557.
32. Bawden, M. J., I. A. Borthwick, H. M. Healy, C. P. Morris, B. K. May and W. H. Elliott (1987) Sequence of human 5-aminolaevulinate synthase cDNA. Nucleic Acids Res. 15, 8563.
33. Maguire, D. J., A. R. Day, I. A. Borthwick, G. Srivastava, P. I. Wigley, B. K. May and W. H. Elliott (1986) Nucleotide sequence of the chicken 5-aminolaevulinate synthase gene. Nucleic Acids Res. 14, 1379-1391.
34. Urban-Grimal, D., C. Volland, T. Garnier, P. Dehoux and R. Labbe-Bois (1986) The nucleotide sequence of the HEM1 gene and evidence for a precursor form of the mitochondrial 5-aminolaevulinate synthase in Saccharomyces cerevisiae. Eur. J. Biochem. 156, 511-519.
35. Kikuchi, G., A. Kumar, P. Talmage and D. Shemin (1958) The enzymatic synthesis of δ-aminolevulinic acid. J. Biol. Chem. 233, 1214-1219.
36. Lascelles, J. (1959) Adaptation to form bacteriochlorophyll in Rhodopseudomonas spheroides: changes in activity of enzymes concerned in pyrrole synthesis. Biochem. J. 72, 508-518.
37. Lascelles, J. (1960) The synthesis of enzymes concerned in bacteriochlorophyll formation in growing cultures of Rhodopseudomonas spheroides. J. Gen. Microbiol. 23, 487-498.
38. McClung, C. R., J. E. Somerville, M. L. Guerinot and B. K. Chelm (1987) Structure of the Bradyrhizobium japonicum gene hem A encoding 5-aminolevulinic acid synthase. Gene 54, 133-139.
39. Leong, S. A., P. H. Williams and G. S. Ditta (1985) Analysis of the 5′ regulatory region of 5-aminolevulinic acid synthetase. Nucleic Acids Res. 13, 5965-5976.
40. Yang, H. S. and J. K. Hoober (1995) Divergent pathways for δ-aminolevulinic acid synthesis in two species of Arthrobacter. FEMS Microbiol. Lett. 134, 259-263.
41. Tanaka, T., K. Sasaki, N. Noparatnaraporn and N. Nishio (1994) Utilization of volatile fatty acids from anaerobic digestion liquor of sewage sludge for 5-aminolevulinic acid production by photosynthetic bacteria. World J. Microbiol. Biotechnol. 10, 677-680.
42. Granick, S. (1966) The induction in vitro of the synthesis of 5-aminolevulinic acid synthetase in chemical porphyria: a response to certain drugs, sex hormones and foreign chemicals. J. Biol. Chem. 241, 1359-1375.
43. Sassa, S. and S. Granick (1970) The induction of δ-aminolevulinic acid synthetase in chick embryo liver cells in culture. Proc. Natl. Acad. Sci. USA. 67, 517-522.
44. Bottomley, S. S. and G. A. Smithee (1968) Characterization and measurement of δ-aminolevulinate synthase in bone marrow cell mitochondria. Biochim. Biophys. Acta 159, 27-37.
45. Srivastava, G., J. D. Brooker, B. K. May and W. H. Elliott (1980) Haem control in experimental porphyria: the effect of haemin on the induction of δ-aminolaevulinate synthase in isolated chick-embryo liver cells. Biochem. J. 188, 781-788.
46. Burnham, B. F. and J. Lascelles (1963) Control of porphyrin biosynthesis by a negative-feedback mechanism. Biochem. J. 87, 462-472.
47. Pirola, B. A., G. Srivistava, I. A. Borthwick, J. D. Brooker, B. K. May and W. H. Elliot (1984) Effect of heme on the activity of chick embryo liver mitochondrial δ-aminolevulinate synthase. FEBS Lett. 166, 298-300.
48. Yamauchi, K., N. Hayashi and G. Kikuchi (1980) Translocation of δ-aminolevulinate synthase from the cytosol to the mitochondria and its regulation by haem. J. Biol. Chem. 235, 1746-1751.
49. Srivistava, G., I. A. Borthwick, J. D. Brooker, J. C. Wallace, B. K. May and W. H. Elliott (1983) Hemin inhibits transfer of pre-δ-aminolevulinate synthase into chick embryo liver mitochondria. Biochem. Biophys. Res. Commun. 117, 344-349.
50. Cable, E. E., J. W. Cable and H. L. Bonkovsky (1993) Repression of hepatic δ-aminolevinate synthase by heme and metalloporphyrins: relationship to inhibition of heme oxygenase. Hepatology 18, 119-127.
51. Battle, A. M. D. C. (1993) Porphyrins, porphyrias, cancer and photodynamic therapy: a model for carcinogenesis. J. Photochem. Photobiol. B Biol. 20, 5-22.
52. Orth, K., K. Koenig, F. Genze and A. Rueck (1994) Photodynamic therapy of experimental colonic tumours with 5-aminolevulinic-acid-induced endogenous porphyrins. J. Cancer Res. Clin. Oncol. 120, 657-661.
53. Hua, Z., S. L. Gibson, T. H. Foster and R. Hilf (1995) Effectiveness of δ-aminolevulinic acid-induced protoporphyrin as a photosensitizer for photodynamic therapy in vivo. Cancer Res. 55, 1723-1731.
54. He, D., S. Behar, N. Nomura, S. Sassa and H. W. Lim (1995) The effect of ALA and radiation on porphyrin/heme biosynthesis in endothelial cells. Photochem. Photobiol. 61, 656-661.
55. Rebeiz, N., S. Arkins, C. A. Rebeiz, J. Simon, J. F. Zachary and K. W. Kelley (1996) Induction of tumor necrosis by δ-aminolevulinic acid and 1,10-phenanthroline photodynamic therapy. Cancer Res. 56, 339-344.
56. Haertel, H., G. Walter and T. Hanke (1993) Photoinduced damage in leaf segments of wheat (Triticum aestivum L.) and lettuce (Lactuca sativa L.) treated with 5-aminolevulinic acid: I. Effects on the components of the photosynthetic apparatus. J. Plant Physiol. 142, 230-236.
57. McKie, J., C. Lucas and A. Smith (1981) δ-Aminolaevulinate biosynthesis in the cyanobacterium Synechococcus 6301. Phytochemistry 20, 1547-1549.
58. 5 pathway in a methylotroph. J. Gen. Microbiol. 139, 2931-2938.
59. Beale, S. I., S. P. Gough and S. Granick (1975) Biosynthesis of δ-aminolevulinic acid from the intact carbon skeleton of glutamic acid in greening barley. Proc. Natl. Acad. Sci. USA 72, 2719-2723.
60. 14C incorporation from exogenous compounds into δ-aminolevulinic acid by greening cucumber cotyledons. Biochem. Biophys. Res. Commun. 52, 143-149; but, also see correctly printed version in 53, 366-367.
61. 13C-NMR evidence for the pathway of chlorophyll biosynthesis in green algae. Biochem. Biophys. Res. Commun. 105, 647-652.
62. 5 pathway over the Shemin pathway in chlorophyll biosynthesis in higher plants and of the formation of the methyl ester group of chlorophyll from glycine. Eur. J. Biochem. 130, 509-516
63. Wang, W.-Y., S. P. Gough and C. G. Kannangara (1981) Biosynthesis of δ-aminolevulinate in greening barley leaves. IV. Isolation of three soluble enzymes required for the conversion of glutamate to δ-aminolevulinate. Carlsberg Res. Commun. 46, 243-257.
64. Kannangara, C. G., R. V. Andersen, B. Pontoppidan, R. Willows and D. von Wettstein (1994) Enzymic and mechanistic studies on the conversion of glutamate to 5-aminolaevulinate. In The Biosynthesis of Tetrapyrrole Pigments, Ciba Foundation Symposium No. 180 (edited by D. J. Chadwick and K. Ackrill), pp. 3-25. John Wiley and Sons, Chichester.
65. Kannangara, C. G., S. P. Gough, R. P. Oliver and S. K. Rasmussen (1984) Biosynthesis of δ-aminolevulinate in greening barley leaves. VI. Activation of glutamate by ligation to RNA. Carlsberg Res. Commun. 49, 417-437.
66. Glu reductase, the enzyme that directs glutamate to chlorophyll biosynthesis. Eur. J. Biochem. 225, 529-537.
67. Jahn, D. (1992) Complex formation between glutamyl tRNA synthetase and glutamyl tRNA reductase during the tRNA dependent synthesis of 5-aminolevulinic acid in Chlamydomonas reinhardtii. FEBS Lett. 314, 77-80.
68. Houen, G., S. P. Gough and C. G. Kannangara (1983) δ-Aminolevulinate synthesis in greening barley V. The structure of glutamate-1-semialdehyde. Carlsberg Res. Commun. 48, 567-572.
69. Kannangara, C. G. and S. P. Gough (1978) Biosynthesis of δ-aminolevulinate in greening barley leaves: glutamate 1-semialdehyde aminotransferase. Carlsberg Res. Commun. 43, 185-194.
70. Hoober, J. K., A. Kahn, D. E. Ash, S. P. Gough and C. G. Kannangara (1988) Biosynthesis of δ-aminolevulinate in greening barley leaves: IX. Structure of the substrate, mode of gabaculine inhibition and the mechanism of glutamate-1-semialdehyde aminotransferase. Carlsberg Res. Commun. 53, 11-25.
71. Pugh, C. E., J. L. Harwood and R. A. John (1992) Mechanism of glutamate semialdehyde aminotransferase. Roles of diamino-intermediates and dioxo-intermediates in the synthesis of aminolevulinate. J. Biol. Chem. 267, 1584-1588.
72. Friedmann, H. C., M. E. Duban, A. Valasinas and B. Frydman (1992) The enantioselective participation of (S) and (R)-diaminovaleric acids in the formation of δ-aminolevulinic acid in cyanobacteria. Biochem. Biophys. Res. Commun. 185, 60-68.
73. Wang. W.-Y., D.-D. Huang, D. Stachon, S. P. Gough and C. G. Kannangara (1984) Purification, characterization and fractionation of the δ-aminolevulinic acid synthesizing enzymes from light-grown Chlamydomonas reinhardtii cells. Plant Physiol. 74, 569-575.
74. Rieble, S and S. I. Beale (1988) Transformation of glutamate to δ-aminolevulinic acid by soluble extracts of Synechocystis PCC6803 and other oxygenic bacteria. J. Biol. Chem. 263, 8864-8871.
75. Schön, A., G. Krupp, S. Gough, S. Berry-Lowe, C. G. Kannangara and D. Söll (1986) The RNA required for the first step of chlorophyll biosynthesis is a chloroplast tRNA. Nature 322, 281-284.
76. Andersen, R. V. (1992) Characterization of a barley tRNA synthetase involved in chlorophyll biosynthesis. In Research in Photosynthesis, Vol. 3 (Edited by N. Murata), pp. 27-30. Kluwer, The Hague.
77. Mayer, S. M., S. Rieble and S. I. Beale (1994) Metal requirements of enzymes catalysing the conversion of glutamate to δ-aminolevulinic acid in extracts of Chlorella vulgaris and Synechocystis sp. PCC 6803. Arch. Biochem. Biophys. 312, 203-209.
78. Vothknecht, U. C., H. Senger and D. Dörnemann (1994) Purification and partial characterization of a glutamyl-tRNA synthetase from the unicellular green alga Scenedesmus obliquus, mutant C-2A'. Planta 192, 256-260.
79. Hori, N., M. Kumar, E. Verkamp and D. Söll (1996) 5-Aminolevulinic acid formation in Arabidopsis thaliana. Plant Physiol. Biochem. 34, 3-9.
80. Glu involved in recognition by barley chloroplast glutamyl-tRNA synthetase and glutamyl-tRNA reductase. Biochim. Biophys. Acta 1263, 228-234.
81. Glu uncouples protein and chlorophyll biosynthesis. Proc. Natl. Acad. Sci. USA 91, 7947-7951.
82. Jahn, D., E. Verkamp and D. Söll (1992) Glutamyl transfer RNA: a precursor of heme and chlorophyll biosynthesis. Trends Biochem. Sci. 17, 215-218.
83. Smith, M. A., C. G. Kannangara and B. Grimm (1992) Glutamate 1-semialdehyde aminotransferase: anomalous enantiomeric reaction and enzyme mechanism. Biochemistry 31, 11249-11254.
84. Smith, M. A., B. Grimm, C. G. Kannangara and D. von Wettstein (1991) Spectral kinetics of glutamate-1-semialdehyde aminomutase of Synechococcus, Proc. Natl. Acad. Sci. USA 88, 9775-9779.
85. Grimm, B., M. A. Smith and D. von Wettstein (1992) The role of Lys-272 in the pyridoxal-5-phosphate active site of Synecchococcus glutamate-1-semialdehyde aminotransferase. Eur. J. Biochem. 206, 579-585.
86. Beale, S. I. and J. Weinstein (1991) Biochemistry and regulation of photosynthetic pigment formation in plants and algae. In Biosynthesis of Tetrapyrroles (Edited by P. M. Jordan), pp. 155-235. Elsevier, Amsterdam
87. Mayer, S. M., E. Gawlita, Y. J. Avissar, V. E. Anderson and S. I. Beale (1993) Intermolecular nitrogen transfer in the enzymic conversion of glutamate to δ-aminolevulinic acid by extracts of Chlorella vulgaris. Plant Physiol. 101, 1029-1038.
88. Tyacke, R. J., J. L. Harwood and R. A. John (1993) Properties of the pyridoxaldimine form of glutamate semialdehyde aminotransferase (glutamate-1-semialdehyde 2,1-aminomutase) and analysis of its role as an intermediate in the formation of aminolaevulinate. Biochem. J. 293, 697-701.
89. Kah, A., D. Dörnemann and H. Senger (1988) Isolation and purification to apparent homogeneity of 4,5-dioxovalerate aminotransferase from Scenedesmus obliquas mutant C-2A'. Z. Naturforsch. 43c, 563-568.
90. Breu, V. and D. Dörnemann (1988) Forrmation of 5-aminolevulinate via glutamate-1-semialdehyde and 4,5-dioxovalerate with participation of an RNA component in Scenedesmus obliquas mutant C-2A'. Biochim. Biophys. Acta 967, 135-140.
91. Soper, T. S. and J. M. Manning (1982) Inactivation of pyridoxal phosphate enzymes by gabaculine: correlation with enzymic exchange of β-protons. J. Biol. Chem. 257, 13930-13936.
92. 2 terminus and an internal amino acid substitution. J. Biol. Chem. 266, 12495-12505.
93. Matters, G. L. and S. I. Beale (1994) Biosynthesis of δ-aminolevulinic acid from glutamate by Sulfolobus solfataricus. Arch. Microbiol. 161, 272-276.
94. Oh-Hama, T., N. J. Stolowich and A. I. Scott (1993) 5-Aminolevulinic acid biosynthesis in Propionibacterium shermanii and Halobacterium salinarium: distribution of the two pathways of 5-aminolevulinic acid biosynthesis in prokaryotes. J. Gen. Appl. Microbiol. 39, 513-519.
95. Kojima, I., K. Maruhashi, Y. Fujiwara, T. Saito, M. Kajiwara and M. Mizutani (1993) Identification of the porphyrins produced from isopropanol by Arthrobacter hyalinus. J. Ferment. Bioeng. 75, 353-358.
96. Kojima, I., K. Maruhashi, H. Sato and Y. Fujiwara (1993) A highly active producer of coproporphyrin III and uroporphyrin III. J. Ferment. Bioeng. 76, 527-529.
97. Kajiwara, M., M. Mizutani, R. Matsuda, K. I. Hara and I. Kojima (1994) A new biosynthetic pathway of porphyrins from isopropanol. J. Ferment. Bioeng. 77, 626-629.
98. Meller, E. and E. Harel (1978) The pathway of 5-aminolevulinic acid synthesis in Chlorella vulgaris and in Freymyella diplosiphon. In Chloroplast Development (Edited by G. Akoyunoglou and J.-H. Argyroudi-Akoyunoglou), pp. 51-57. Balaban, Philadelphia.
99. Jurgenson, J. E., S. I. Beale and R. F. Troxler (1976) Biosynthesis of δ-aminolevulinic acid in the unicellular rhodophyte, Cyanidium caldarium. Biochem. Biophys. Res. Commun. 69, 149-157.
100. Beale, S. I. (1971) Studies on the biosynthesis and metabolism of δ-aminolevulinic acid in Chlorella. Plant Physiol. 48, 316-319.
101. Porra, R. J. and L. H. Grimme (1974) Chlorophyll synthesis and intracellular fluctuations of 5-aminolaevulinate formation during regreening of nitrogen-deficient Chlorella fusca. Arch. Biochem. Biophys. 148, 37-43.
102. Ilag, L. L., A. M. Kumar and D. Söll (1994) Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis. Plant Cell 6, 265-275.
103. Masuda, T., H. Ohta, Y. Shioi and K. I. Takamiya (1996) Light regulation of 5-aminolevulinic acid-synthesis system in Cucumis sativus: light stimulates activity of glutamyl-tRNA reductase during greening. Plant Physiol. Biochem. 34, 11-16.
104. Matters, G. E. and S. I. Beale (1995) Blue-light-regulated expression of genes for two early steps of chlorophyll biosynthesis in Chlamydomonas reinhardtii. Plant Physiol. 109, 471-479.
105. Glu. Plant Cell Physiol. 35, 183-188.
106. Masuda, T., H. Ohta, Y. Shioi, H. Tsuji and K. I. Takamiya (1995) Stimulation of glutamyl-tRNA reductase activity by benzyladenine in greening cucumber cotyledons. Plant Cell Physiol. 36, 1237-1243.
107. Woodard, S. I. and H. A. Dailey (1995) Regulation of heme biosynthesis in Escherichia coli. Arch. Biochem. Biophys. 316, 110-115.
108. 5 pathway in seedlings of virescent mutant rice. Plant Cell Physiol. 35, 445-449.
109. Jilani, A., S. Kar, S. Bose and B. C. Tripathy (1996) Regulation of the carotenoid content and chloroplast development by levulinic acid. Physiol. Plant. 96, 139-145.
110. Spencer, P. and P. M. Jordan (1994) 5-Aminolaevulinic acid dehydratase: characterization of the a and β metal-binding sites of the Escherichia coli enzyme. In The Biosynthesis of the Tetrapyrrole Pigments, Ciba Foundation Symposium 180 (Edited by D. J. Chadwick and K. Ackrill), pp. 50-69. John Wiley and Sons, Chichester.
111. Spencer, P. and P. M. Jordan (1993) Purification and characterization of 5-aminolaevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain. Biochem. J. 290, 279-287.
112. Gibbs, P. N. B., A.-G. Chaudry and P. M. Jordan (1985) Purification and properties of 5-aminolaevulinate dehydratase from human erythrocytes. Biochem. J. 230, 25-34.
113. Jordan, P. M. and J. S. Seehra (1986) Purification of porphobilinogen synthase from bovine liver. Methods Enzymol. 123, 427-434.
114. Schmid, R. and D. Shemin (1955) The enzymatic formation of porphobilinogen from δ-amino levulinic acid and its conversion to protoporphyrin. J. Am. Chem. Soc. 77, 506-508.
115. Borralho, L. M., C. H. D. Ortiz, A. D. Panek and J. R. Mattoon (1990) Purification of δ-aminolevulinic acid dehydratase from genetically engineered yeast. Yeast 6, 319-330.
116. Spencer, P. and P. M. Jordan (1994) Investigation of the nature of the two metal-binding sites in 5-aminolaevulinic acid dehydratase from Escherichia coli. Biochem. J. 300, 373-381.
117. Nandi, D. L., K. F. Baker-Cohen and D. Shemin (1968) δ-aminolevulinic acid dehydratase of Rhodopseudomonas sphaeroides. 1. Isolation and properties. J. Biol. Chem. 243, 1224-1230.
118. Liedgens, W., C. Lütz and H. A. W. Schneider (1983) Molecular properties of 5-aminolevulinic acid dehydratase of Spinacea oleracea. Eur. J. Biochem. 135, 75-79.
119. Polking, G. F., D. J. Hannapel and R. J. Gladon (1995) Characterization of a cDNA encoding 5-aminolevulinic acid dehydratase in tomato (Lycopersicon esculentum Mill.). Plant Cell Rep, 14, 366-369.
120. Jaffe, E. K. (1995) Porphobilinogen synthase, the first source of heme's asymmetry. J. Bioenerg. Biomembr. 27, 169-179.
121. Sopena de Kracoff, Y. E., A. M. P. de Sancovich and H. A. Sancovich (1995) Evidence of an essential lysine in pig-liver 5-amino levulinic acid dehydratase. Int. J. Biochem. Cell Biol. 27, 1331-1339.
122. Gibbs, P. N. B. and P. M. Jordan (1986) Identification of lysine at the active site of human 5-aminolaevulinate dehydratase. Biochem. J. 236, 447-451.
123. Spencer, P. and P. M. Jordan (1995) Characterization of the two 5-aminolaevulinic acid binding sites, the A and P sites, of 5-aminolaevulinic acid dehydratase from Escherichia coli. Biochem. J. 305, 151-158.
124. Nandi, D. L. and D. Shemin (1986a) δ-Aminolevulinic acid dehydratase of Rhodopseudomonas spheroides. II. Association to polymers and dissociation to sub-units. J. Biol. Chem. 243, 1231-1235.
125. Nandi, D. L. and D. Shemin (1986b) δ-Aminolevulinic acid dehydratase of Rhodopseudomonas spheroides. III. Mechanism of porphobilinogen synthesis. J. Biol. Chem. 243, 1236-1242.
126. Boese, Q. F., A. J. Spano, J. Li and M. P. Timko (1991) Aminolevulinic acid dehydratase in pea (Pisum sativum L.). Identification of an unusual metal-binding domain in the plant enzyme. J. Biol. Chem. 266, 17060-17066.
127. Petrovich, R. M., S. Litwin and E. K. Jaffe (1996) Bradyrhizobium japonicum porphobilinogen synthase uses two Mg(II) and monovalent cations. J. Biol. Chem. 271, 8692-8699.
128. Chauhan, S. and M. R. O'Brian (1995) A mutant Bradyrhizobium japonicum δ-aminolevulinic acid dehydratase with an altered metal requirement in situ for tetrapyrrole biosynthesis in soybean root nodules J. Biol. Chem. 270, 19823-19827.
129. Matters, G. L. and S. I. Beale (1995) Structure and expression of the Chlamydomonas reinhardtii alad gene encoding the chlorophyll biosynthetic enzyme, δ-aminolevulinic acid dehydratase (porphobilinogen synthase). Plant Mol. Biol. 27, 607-617.
130. Afonso, S. G., S. Chinarro, R. Enriquez de Salamanca and A. M. D. Battle (1994) δ-Aminolevulinic acid dehydratase inactivation by uroporphyrin I in light and darkness. Int. J. Biochem. 26, 255-258.
131. Jordan, P. M. (1994) The biosynthesis of uroporphyrinogen III: mechanism of action of porphobilinogen deaminase. In The Biosynthesis of the Tetrapyrrole Pigments, Ciba Foundation Symposium 180 (Edited by D. J. Chadwick and K. Ackrill), pp. 70-96. John Wiley and Sons, Chichester.
132. Lambert, R., P. D. Brownlie, S. C. Woodcock, G. V. Louie, J. C. Cooper, M. J. Warren and P. M. Jordan, T. L. Blundell and S. P. Wood (1994) Structural studies on porphobilinogen deaminase. In The Biosynthesis of the Tetrapyrrole Pigments, Ciba Foundation Symposium 180 (Edited by D. J. Chadwick and K. Ackrill), pp. 97-110. John Wiley and Sons, Chichester.
133. Leeper, F. J. (1994) The evidence for a spirocyclic intermediate in the formation of uroporphyrinogen III by cosynthase. In The Biosynthesis of the Tetrapyrrole Pigments, Ciba Foundation Symposium 180 (Edited by D. J. Chadwick and K. Ackrill), pp. 111-130. John Wiley and Sons, Chichester.
134. Hart, G. J., A. D. Miller, F. J. Leeper and A. R. Battersby (1987) Biosynthesis of the natural porphyrins: proof that hydroxymethylbilane synthase (porphobilinogen deaminase) uses a novel binding group in its catalytic action. J. Chem. Soc. Chem. Commun. 1987, 1762-1765.
135. 13C-NMR studies on the pyrromethane cofactor of hydroxymethylbilane synthase. Tetrahedron Lett. 29, 2591-2594.
136. 13C-n.m.r. FEBS Lett. 235, 189-193.
137. Battersby, A. R., C. J. R. Fookes, G. W. J. Matcham and E. McDonald (1979) Order of assembly of the four pyrrole rings of the natural porphyrins. J. Chem. Soc. Chem. Commun. 1979, 539-541.
138. Battersby, A. R., C. J. R. Fookes, K. E. Gustafson-Potter, G. W. J. Matcham and E. McDonald (1979) Proof by synthesis that unrearranged hydroxymethylbilane is the product from deaminase and substrate for cosynthase in the biosynthesis of uroporphyrinogen III. J. Chem. Soc. Chem. Commun. 1979, 316-319.
139. Woodcock, S. C. and P. M. Jordan (1994) Evidence for the participation of aspartate-84 as a catalytic group at the active site of porphobilinogen deaminase obtained by site-directed mutagenesis of the hemC gene of Escherichia coli. Biochemistry 33, 2688-2695.
140. Lander, M., A. R. Pitt, P. R. Alefounder, D. Bardy, C. Abell A. R. Battersby (1991) Studies on the mechanism of hydroxymethylbilane synthase concerning the role of arginine residues in substrate binding. Biochem. J. 275, 447-452.
141. Jordan, P. M. and S. C. Woodcock (1991) Mutagenesis of arginine residues in the catalytic cleft of Escherichia coli porphobilinogen deaminase that affects dipyrromethane cofactor assembly and tetrapyrrole chain initiation and elongation. Biochem. J. 280, 445-449.
142. Louie, G. V, P. D. Brownlie, R. Lambert, J. B. Cooper, T. L. Blundell, S. P. Wood, M. J. Warren, S. C. Woodcock and P. M. Jordan (1992) Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site. Nature 359, 33-39.
143. Warren, M. J., S. Gul, R. T. Aplin, A. I. Scott, C. A. Roessner, P. O'Grady and P. M. Shoolingin-Jordan (1995) Evidence for conformational changes in Escherichia coli porphobilinogen deaminase during stepwise pyrrole chain elongation monitored by increased reactivity of cysteine-134 to alkylation by N-ethylmaleimide. Biochemistry 34, 11288-11295.
144. Juhnat, A. A., D. Dörnemann and H. Senger (1994) Purification and kinetic studies on a porphobilinogen deaminase from the unicellular green alga Scenedesmus obliquus. Planta 193, 123-130.
145. Araujo, L. S., M. E. Lombardo and A. M. D. C. Battle (1994) Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae. Int. J. Biochem. 26, 1377-1381.
146. Harris, W. F., R. S. Burkhalter, W. Lin and R. Timkovich (1993) Enhancement of bacterial porphyrin biosynthesis by exogenous aminolevulinic acid and isomer specificity of the products. Biorg. Chem. 21, 209-220.
147. Stark, W. M., G. J. Hart and A. R. Battersby (1986) Synthetic studies on the proposed spiro intermediate for biosynthesis of the natural porphyrins: inhibition of cosynthetase. J. Chem. Soc. Chem. Commun. 1986, 465-467.
148. Akhtar, M. (1991) Mechanism and stereochemistry of the enzymes involved in the conversion of uroporphyrinogen III to haem. In Biosynthesis of tetrapyrroles (Edited by P. M. Jordan), pp. 67-99. Elsevier, Amsterdam.
149. Akhtar, M. (1994) The modification of acetate and propionate side chains during the biosynthesis of haem and chlorophylls: mechanistic and stereochemical studies. In The Biosynthesis of the Tetrapyrrole Pigments, Ciba Foundation Symposium 180 (Edited by D. J. Chadwick and K. Ackrill), pp. 131-155. John Wiley and Sons, Chichester.
150. Jackson, A. H., H. A. Sangovich, A. M. Ferramola, N. Evans, D. E. Game and S. A. Matlin (1976) Macrocyclic intermediates in the biosynthesis of porphyrins. Phil. Trans. R. Soc. Lond. B 273, 191-206.
151. Lash, T. D. (1991) Action of uroporphyrinogen decarboxylase on uroporphyrinogen III: a reassessment of the clockwise decarboxylation hypothesis. Biochem. J. 278, 901-902.
152. Luo, J. and C. K. Lim (1994) Order of uroporphyrinogen III decarboxylation on incubation of porphobilinogen and uroporphyrinogen III with erythrocyte uroporphyrinogen decarboxylase. Biochem. J. 289, 529-532.
153. Jackson, A. H., H. A. Sancovich, D. E. Ferramola and E. M. Sancovich (1980) Synthetic and biosynthetic studies on porphyrins. III. Structures of intermediates between uroporphyrinogen III and coproporphyrinogen III: synthesis of fourteen heptcarboxylic, hexacarboxylic and pentacarboxylic porphyrins related to uroporphyrin III. Biorg. Chem. 9, 71-120.
154. Cavaleiro, J. A. S., J. W. Kenner and K. M. Smith (1974) Pyrroles and related compounds. XXXII. Biosynthesis of protoporphyrin IX from coproporphyrin III. J. Chem. Soc. Perkin Trans. 1974, 1188-1194.
155. Tait, G. H. (1972) Coproporphyrinogenase activity in extracts from Rhodopseudomonas sphaeroides and Chromatium D. Biochem. J. 128, 1159-1169.
156. Akutsu, H., J. S. Park and S. Sano (1993) L-Methionine methyl is specifically incorporated into the C-2 and C-7 positions of the porphyrin of cytochrome c3 in a strictly anaerobic bacterium, Desulfovibrio vulgaris. J. Am. Chem. Soc. 115, 12185-12186.
157. Bollivar, D. W., T. Elliott and S. I. Beale (1995) Anaerobic protoporphyrin biosynthesis does not require incorporation of methyl groups from methionine. J. Bacteriol. 177, 5778-5783.
158. Kohno, H., T. Furukawa, T. Yoshinaga, R. Tukunaga and S. Taketani (1993) Coproporphyrinogen oxidase: purification, molecular cloning and induction of mRNA during erythroid differentiation. J. Biol. Chem. 268, 21359-21363.
159. Camadro, J. M., H. Chambon, J. Jolles and P. Labbe (1986) Purification and properties of coproporphyrinogen oxidase from the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 156, 579-587.
160. Yoshinaga, T. and S. Sano (1980) Coproporphyrinogen oxidase. I. Purification and properties and activation by phospholipids. J. Biol. Chem. 255, 4722-4726.
161. Yoshinaga, T. and S. Sano (1980) Coproporphyrinogen oxidase. II. Reaction mechanism and role of tyrosine residues on activity. J. Biol. Chem. 255, 4727-4731.
162. Kruse, E., H. P. Mock and B. Grimm (1995) Coproporphyrinogen III oxidase from barley and tobacco sequence analysis and initial expression studies. Planta 196, 796-803.
163. Hansson, M. and L. Hederstedt (1994) Bacillus subtilis Hem Y is a peripheral membrane protein essential for protohaem IX synthesis which can oxidise coproporphyrinogen III and protoporphyrinogen IX. J. Bacteriol. 176, 5962-5970
164. Dailey, T. A., P. Meissner and H. A. Dailey (1994) Expression of a cloned protoporphyrinogen oxidase. J. Biol. Chem. 269, 813-815.
165. Sano, S. and S. Granick (1961) Mitochondrial coproporphyrinogen oxidase and protoporphyrin formation. J. Biol. Chem. 236, 1173-1180.
166. Jacobs, J. M., N. J. Jacobs and A. E. De Maggio (1982) Protoporphyrinogen oxidation in chloroplasts and plant mitochondria, a step in heme and chlorophyll synthesis. Arch. Biochem. Biophys. 218, 233-239.
167. Jacobs, J. M. and N. J. Jacobs (1984) Protoporphyrinogen oxidase, an enzymatic step in heme and chlorophyll synthesis: partial characterization of the reaction in plant organelles and comparison with mammalian and bacterial systems. Arch. Biochem. Biophys. 229, 312-319.
168. Camadro, J. M., D. Urban-Grimal and P. Labbe (1982) A new assay for protoporphyrinogen oxidase. Evidence for a total deficiency in that activity in a heme-less mutant of Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 106, 724-730.
169. Camadro, J. M. and P. Labbe (1996) Cloning and characterization of the yeast HEM14 gene coding for protoporphyrinogen oxidase, the molecular target of diphenylether-type herbicides. J. Biol. Chem. 271, 9120-9128.
170. Matringe, M., J. M. Camadro, P. Labbe and R. Scalla (1989) Protoporphyrinogen oxidase as a molecular target for diphenyl ether herbicides. Biochem. J. 260, 231-235.
171. Becerril, J. M. and S. O. Duke (1989) Protoporphyrin IX content correlates with activity of photobleaching herbicides. Plant Physiol. 90, 1175-1181.
172. Jacobs, J. M. and N. J. Jacobs (1981) Protoporphyrinogen oxidase in Rhodopseudomonas spheroides, a step in heme and bacteriochlorophyll synthesis. Arch. Biochem. Biophys. 211, 305-311.
173. Hannson, M. and L. Hederstedt (1992) Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes. J. Bacteriol. 174, 8081-8093.
174. Sassarman, A., J. Letowski, G. Czaika, V. Ramirez, M. A. Nead, J. M. Jacobs and R. Morais (1993) Nucleotide sequence of the hemG gene involved in the protoporphyrinogen oxidase activity of Escherichia coli K12. Can. J. Microbiol. 39, 1155-1161.
175. Klemm, D. J. and L. L. Barton (1987) Purification and properties of protoporphyrinogen oxidase from an anaerobic bacterium, Desulfovibrio gigas. J. Bacteriol. 169, 5209-5215.
176. Dailey, H. A. and T. A. Dailey (1996) Protoporphyrinogen oxidase of Myxococcus xanthus: expression, purification and characterization of the cloned enzyme, J. Biol. Chem. 271, 8714-8718.
177. Labbe-Bois, R. (1990) The ferrochelatase from Saccharomyces cerevisiae: sequence, disruption and expression of its structural gene HEM 15. J. Biol. Chem. 265, 7278-7283.
178. Porra, R. J. and O. T. G. Jones (1963) Studies on ferrochelatase: 1. assay and properties of ferrochelatase from a pig-liver mitochondrial extract. Biochem. J. 87, 181-185.
179. Porra, R. J. and O. T. G. Jones (1963) Studies on ferrochelatase: 2. an investigation of the role of ferrochelatase in the biosynthesis of various haem prosthetic groups. Biochem. J. 87, 186-192.
180. Jones, O. T. G. (1967) Haem synthesis by isolated chloroplasts. Biochem. Biophys. Res. Commun. 28, 671-674.
181. Porra, R. J. and J. Lascelles (1968) Studies on ferrochelatase: the enzymic formation of haem in proplastids, chloroplasts and plant mitochondria. Biochem. J. 108, 343-348.
182. Gorchein, A. (1972) Magnesium protoporphyrin chelatase activity in Rhodopseudomonas spheroides: studies with whole cells. Biochem. J. 127, 97-106.
183. Gorchein, A. (1973) Control of magnesium protoporphyrin chelatase activity in Rhodopseudomonas spheroides role of light, oxygen, and electron and energy transfer. Biochem. J. 134, 833-845.
184. Gibson, L. C. D., R. D. Willows, C. G. Kannangara, D. von Wettstein and C. N. Hunter (1995) Magnesium-protoporphyrin chelatase of Rhodobacter sphaeroides: reconstitution of activity by combining the products of the BchH, I, and D genes expressed in Escherichia coli. Proc. Nat. Acad. Sci. USA 92, 1941-1944.
185. 12 biosynthesis in Pseudomonas denitrificans. J. Bacteriol. 174, 7445-7451.
186. Hudson, A., R. Carpenter, S. Doyle and E. S. Coen (1993) Olive: a key gene required for chlorophyll biosynthesis in Antirrhinum majus. EMBO J. 12, 3711-3719.
187. Walker, C. J. and J. D. Weinstein (1991) In vitro assay of the chlorophyll biosynthetic enzyme Mg-chelatase: resolution of the activity into soluble and membrane-bound fractions. Proc. Natl. Acad. Sci. USA 88, 5789-5793.
188. Hartwell, J. G. and J. D. Weinstein (1992) Cucumber chloroplast magnesium chelatase. Plant Physiol. 99, 4. [Abstract 20]
189. Richter, M. L. and K. G. Reinits (1982) The synthesis of magnesium protoporphyrin IX by etiochloroplast membrane preparations. Biochim. Biophys. Acta 717, 255-264.
190. Gibson, K. L., A. Neuberger and G. H. Tait (1963) Studies on the biosynthesis of porphyrin and bacteriochlorophyll by Rhodopseudomonas spheroides. 4. S-adenosylmethionine-magnesium-protoporphyrin methyltransferase. Biochem. J. 88, 325-334.
191. Ebbon, J. G. and G. H. Tait (1969) Studies on S-adenosylmethionine-magnesium-protoporphyrin methyl-transferase in Euglena gracilis strain Z. Biochem. J. 111, 573-582.
192. Ellsworth, R. K., J. P. Dullaghan and M. E. St. Pierre (1974) The reaction mechanism of S-adenosyl-L-methionine : Mg protoporphyrin IX methyltransferase of wheat. Photosynthetica 8, 375-383.
193. Yee, W. C., S. J. Eglsaer and W. R. Richards (1989) Confirmation of a ping-pong mechanism for S-adenosyl-L-methionine: Mg protoporphyrin methyltransferase of etiolated wheat by an exchange mechanism. Biochem. Biophys. Res. Commun. 162, 483-490.
194. 13C-nuclear magnetic resonance studies of the biosynthesis of 5-aminolevulinic acid destined for chlorophyll biosynthesis in dark-grown Scenedesmus obliquus. Plant Sci. 42, 153-158.
195. 5 pathway and evidence of a new route for the incorporation of glycine. Biochem. Int. 5, 345-350.
196. 13C-nuclear magnetic resonance studies on bacteriochlorophyll a biosynthesis in Rhodpseudomonas spheroides S. Arch. Biochem. Biophys. 237, 72-79.
197. Bollivar, D. W., Z. Y. Jiang, C. E. Bauer and S. I. Beale (1994) Heterologous expression of the BchM gene product from Rhodobacter capsulatus and demonstration that it encodes S-adenosyl-L-methionine : Mg-protoporphyrin IX methyltransferase. J. Bacteriol. 176, 5290-5296.
198. Gibson, L. C. D. and C. N. Hunter (1994) The bacteriochlorophyll synthesis gene, bchM, of Rhodobacter sphaeroides encodes S-adenosyl-L-methionine : Mg protoporphyrin IX methyltransferase. FEBS Lett. 352, 127-130.
199. 5 methylester from Mg-protoporphine IX monomethyl ester as observed in Chlorella mutants. Arch. Biochem. Biophys. 125, 269-277.
200. 5 obtained from Chlorella mutants. Arch. Biochem. Biophys. 130, 374-383.
201. 1-oxo and 3-acetyl groups of bacteriochlorophyll a from water in Rhodobacter sphaeroides cells adapting from respiratory to photosynthetic conditions: evidence for an anaerobic pathway for the formation of isocyclic ring E. FEBS Lett. 371, 21-24.
202. 18O-labelling and mass spectrometry. In Photosynthesis: From Light to Biosphere, Vol. 3 (Edited by P. Mathis), pp. 881-885. Kluwer, Dordrecht.
203. Porra, R. J., W. Schäfer, N. Gad'on, I. Katheder, G. Drews and H. Scheer (1996) Origin of the two carbonyl oxygens of bacteriochlorophyll a: demonstration of two different pathways for the formation of ring E in Rhodobacter sphaeroides and Roseobacter denitrificans and a common hydratase mechanism for 3-acetyl group formation. Eur. J. Biochem. 239, 85-92.
204. Walker, C. J., K. E. Mansfield, K. M. Smith and P. A. Castelfranco (1989) Incorporation of atmospheric oxygen into the carbonyl functionality of the protochlorophyllide isocyclic ring. Biochem. J. 257, 599-602.
205. Schneegurt, M. A. and S. I. Beale (1992) Origin of the chlorophyll b formyl oxygen in Chlorella vulgaris. Biochemistry 31, 11677-11683.
206. Porra, R. J., W. Schäfer, E. Cmiel, I. Katheder and H. Scheer (1993) Derivation of the formyl group oxygen of chlorophyll b from molecular oxygen in greening leaves of a higher plant (Zea mays). FEBS Lett. 371, 21-24.
207. 2 in greening maize leaves. Eur. J. Biochem. 219, 671-679.
208. 5. Plant Physiol. 70, 987-993.
209. Nasrulhaq-Boyce, A., W. T. Griffiths and O. T. G. Jones (1987) The use of continuous assays to characterize the oxidative cyclase that synthesizes the chlorophyll isocyclic ring. Biochem. J. 243, 23-29.
210. Bollivar, D. W. and S. I. Beale (1995) Formation of the isocyclic ring of chlorophyll by isolated Chlamydomonas reinhardtii chloroplasts. Photosynth. Res. 43, 113-124.
211. Whyte, B. J. and P. A. Castelfranco (1993) Further observations on the Mg-protoporphyrin IX monomethylester (oxidative) cyclase system. Biochem. J. 276, 691-697.
212. Hayaishi, O. (1987) General properties and biological functions of oxygenases. In Molecular Mechanisms of Oxygen Activation (Edited by O. Hayaishi), pp. 1-28. Academic Press, London.
213. Walker, C. J., K. E. Mansfield, I. N. Rezzano, C. M. Hanamoto, K. M. Smith and P. A. Castelfranco (1988) The magnesium-protoporphyrin IX (oxidative) cyclase system: studies on the mechanism and specificity of the reaction. Biochem. J. 255, 685-692.
214. Rebeiz, C. A., S. M. Wu, M. Kuhadja, H. Daniell and E. J. Perkins (1983) Chlorophyll a biosynthetic routes and chlorophyll a chemical heterogeneity in plants. Mol. Cell. Biochem. 57, 97-125.
215. Richards, W. R., M. Fung, A. N. Wessler and S. B. Hinchingeri (1987) Purification and properties of three later-stage enzymes of chlorophyll synthesis. In Progress in Photosynthesis Research, Vol. IV (Edited by J. Biggens), pp. 475-482. Martinus Nijhoff, Dordrecht.
216. 5 monomethyl ester, a protochlorophyll-like pigment produced by Rhodopseudomonas spheroides. Biochem. J. 89, 182-189.
217. Ellsworth, R. K. and A. S. Hsing (1973) The reduction of vinyl side-chains of Mg-protoporphyrin IX monomethyl ester in vitro. Biochim. Biophys. Acta 313, 119-129.
218. Duggan, J. X. and C. A. Rebeiz (1982) Chloroplast biogenesis. 42. Conversion of divinyl chlorophyllide a to monovinyl chlorophyllide a in vivo and in vitro. Plant Sci. Lett. 27, 137-145.
219. Fujita, Y. (1996) Protochlorophyllide reduction: a key step in the greening of plants. Plant Cell Physiol. 34, 411-412.
220. Reinbothe, S., C. Reinbothe, N. Lebedev and K. Apel (1996) PORA and PORB, two light-dependent protochlorophyllide-reducing enzymes of angiosperm chlorophyll biosynthesis. Plant Cell 8, 763-769.
221. Griffiths, W. T. (1978) Reconstitution of chlorophyll formation by isolated etioplast membranes. Biochem. J. 174, 681-692.
222. Apel, K., H.-J. Santel, T. E. Redlinger and H. Falk (1980) The protochlorophyllide holochrome of barley. Isolation and characterization of the NADPH : protochlorophyllide oxidoreductase. Eur. J. Biochem. 111, 251-258.
223. Wilks, H. M. and M. P. Timko (1995) 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.
224. 3H]N-phenylmaleimide. Biochem. J. 195, 93-101.
225. Dehesh, K., M. Klaas, I. Häuser and K. Apel (1986) Light-induced changes in the distribution of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.): 1. Localization by immunoblotting in isolated plastids and total leaf extracts. Planta 169, 162-171.
226. Teakle, J. R. and W. T. Griffiths (1993) Cloning, characterization and import studies on protochlorophyllide reductase from wheat (Triticum aestivum). Biochem. J. 296, 225-230.
227. Schoch, S., M. Helfrich, B. Wiktorsson, C. Sundqvist, W. Rüdiger and M. Ryberg (1995) Photoreduction of zinc protopheophorbide b with NADPH-protochlorophyllide oxidoreductase from etiolated wheat (Triticum aestivum). Eur. J. Biochem. 229, 291-298.
228. Virgin, H. I., A. Kahn and D. von Wettstein (1963) The physiology of chlorophyll formation in relation to structural changes in chloroplasts. Photochem. Photobiol. 2, 83-91.
229. Høyer-Hansen, G. and D. J. Simpson (1977) Changes in the polypeptide composition of internal membranes of barley plastids during greening. Carlsberg. Res. Commun. 42, 379-389.
230. Ikeuchi, M. and S. Murakami (1983) Separation and characterization of prolamellar bodies and prothylakoids from squash etioplasts. Plant Cell Physiol. 24, 71-80.
231. Dehesh, K. and M. Ryberg (1985) The NADPH-protochlorophyllide oxidoreductase is the major constituent of prolamellar bodies in wheat (Triticum aestivum L.). Planta 164, 396-399.
232. Reinbothe, S., S. Runge, C. Reinbothe, B. van Cleve and K. Apel (1995) Substrate-dependent transport of the NADPH: protochlorophyllide oxidoreductase into isolated plastids. Plant Cell 7, 161-172.
233. Reinbothe, S., C. Reinbothe, S. Runge and K. Apel (1995) Enzymatic product formation impairs both the chloroplast receptor binding function as well as translocation competence of the NADPH : protochlorophyllide oxidoreductase, a nuclear encoded plastid protein. J. Cell. Biol. 129, 299-308.
234. Reinbothe, S., C. Reinbothe, H. Holtdorf and K. Apel (1995) Two NADPH : protochlorophyllide oxidoreductases in barley: evidence for the selective disappearance of PORA during the light-induced greening of etiolated seedlings. Plant Cell 7, 1933-1940.
235. Reinbothe, C., K. Apel and S. Reinbothe (1995) A light-induced protease from barley plastids degrades NADPH : protochlorophyllide oxidoreductases complexed with chlorophyllide. Mol. Cell Biol. 15, 6206-6212.
236. Apel, K. (1981) The protochlorophyllide holochrome of barley (Hordeum vulgare L.). Phytochrome-induced decrease of translatable mRNA coding for the NADPH : protochlorophyllide oxidoreductase. Eur. J. Biochem. 120, 89-93.
237. Batschauer, A. and K. Apel (1984) An inverse control by phytochrome of the expression of two nuclear genes in barley. Eur. J. Biochem. 143, 593-597.
238. Mösinger, E., A. Batschauer, E. Schäfer and K. Apel (1985) Phytochrome control on in vitro transcription of specific genes in isolated nuclei from barley (Hordeum valgare). Eur. J. Biochem. 147, 137-142.
239. Armstrong, G. A., S. Runge, G. Frick, U. Sperling and K. Apel (1995) Identification of protochlorophyllide oxidoreductases A and B: a branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana. Plant Physiol. 108, 1505-1517.
240. Holtdorf, H., S. Reinbothe, C. Reinbothe, B. Bereza and K. Apel (1995) Two routes of chlorophyllide synthesis that are differently regulated by light in barley (Hordeum vulgare L.). Proc. Natl. Acad. Sci. USA 92, 3254-3258.
241. Fujita, Y., Y. Takahashi, F. Shonai, Y. Ogura and H. Matsubara (1991) Cloning nucleotide sequences and differential expression of NifH and NifH-like (frxC) genes from the filamentous nitrogen-fixing cyanobacteria Plectonema boryanum. Plant Cell Physiol. 32, 1093-1106.
242. Fujita, Y., Y. Takahashi, M. Chuganji and H. Matsubara (1992) The NifH-like (frxC) gene is involved in the biosynthesis of chlorophyll in the filamentous cyanobacterium Plectonema boryanum. Plant Cell Physiol. 33, 81-92.
243. Yang, Z. and C. E. Bauer (1990) Rhodobacter capsulatus genes involved in the early steps of the bacteriochlorophyll biosynthetic pathway. J. Bacteriol. 172, 5001-5010.
244. Fujita, Y., Y. Takahashi, T. Kohchi, H. Ozeki, K. Ohyama and H. Matsubara (1989) Identification of a novel nifH-like (frxC) protein in chloroplasts of the liverwort Marchantia polymorpha. Plant Mol. Biol. 13, 551-561.
245. Choquet, Y., M. Rahire, J. Girad-Bascou, J. Erikson and J.-D. Rochaix (1992). A chloroplast gene is required for the light-independant accumulation of chlorophyll in Chlamydomonas reinhardtii. EMBO J. 11, 1697-1704.
246. Kohchi, T., H. Shirai, H. Fukuzawa, T. Sano, T. Komano, K. Umesono, H. Inokuchi, H. Ozeki and K. Ohyama (1988) Structure and organization of Marchantia polymorpha chloroplast genome. IV. Inverted repeat and small single copy regions. J. Mol. Biol. 203, 353-372.
247. Fujita, Y., H. Matsumoto, Y. Takahashi and H. Matsubara (1993) Identification of a nifDK-like gene (ORF 467) involved in the biosynthesis of chlorophyll in the cyanobacterium, Plectonema boryanum. Plant Cell Physiol. 34, 305-314.
248. Umesono, K., H. Inokuchi, Y. Shiki, M. Tsudzuki, H. Fukuzawa, T. Kohchi, H. Shirai, K. Ohyama and H. Ozeki (1988) Structure and organization of Marchantia polymorpha chloroplast genome. II. Gene organization of the large single copy region from rps' 12 to atpB. J. Mol. Biol. 203, 299-331.
249. Fujita, Y., H. Takagi and T. Hase (1996) Identification of the chlB gene and the gene product essential for light-independent chlorophyll biosynthesis in the cyanobacterium, Plectonema boryanum. Plant Cell Physiol. 37, 313-323.
250. Burke, D. H., M. Alberti and J. E. Hearst (1993) The Rhodobacter capsulatus chlorin reductase-encoding locus, bchlA, consists of three genes, bchX, bchY and bchz. J. Bacteriol. 175, 2407-2413.
251. Wakasugi, T., J. Tsudzuki, S. Ito, K. Nakashima, T. Tsudzuki and M. Sugiura (1994) Loss of all ndh genes as determined by sequencing the entire chloroplast genome of the black pine Pinus thunbergii. Proc. Natl. Acad. Sci. USA 91, 9794-9798.
252. Lidholm, J. and P. Gustafsson (1991) Homologues of the green algal gidA gene and the liverwort frxC gene are present on the chloroplast genomes of conifers. Plant Mol. Biol. 17, 787-798.
253. Forreiter, C. and K. Apel (1993) Light-independent and light-dependent protochlorophyllide-reducing activities and two distinct NADPH-protochlorophyllide oxidoreductase polypeptides in mountain pine (Pinus mugo). Planta 190, 536-545.
254. Spano, A. J., Z. He and M. P. Timko (1992) NADPH : protochlorophyllide oxidoreductases in white pine (Pinus strobus) and loblolly pine (P. taeda). Mol. Gen. Genet. 236, 86-95.
255. Adamson, H. Y. and N. Packer (1984) Dark synthesis of chlorophyll in vivo and dark reduction of protochlorophyllide in vitro by pea chloroplasts. In Protochlorophyllide and Greening (Edited by C. Sironval and M. Brouers). pp. 353-363, Martinus Nijhoff/Dr. W. Jung Publishers, The Hague.
256. Adamson, H. Y., W. T. Griffiths, N. Packer and M. Sutherland (1985) Light-independent accumulation of chlorophyll a and b in green barley (Hordeum vulgare). Physiol. Plant. 64, 345-352.
257. Ford, C. and W.-Y. Wang (1980) Three new yellow loci in Chlamydomanas reinhardtii. Mol. Gen. Genet. 179, 259-263.
258. Ford, C. and W.-Y. Wang (1980) Temperature-sensitive yellow mutants of Chlamydomonas reinhardtii. Mol. Gen. Genet. 180, 5-10.
259. Ford, C. and W.-Y. Wang (1982) Instability at the y-1 locus of Chlamydomonas reinhardtii. Mol. Gen. Genet. 187, 286-290.
260. Ford, C., S. Mitchell and W.-Y. Wang (1983). Characterization of NADPH : protochlorophyllide oxidoreductase in the y-7 and pc1 y-7 mutants of Chlamydomonas reinhardtii. Mol. Gen. Genet. 192, 290-292.
261. Rüdiger, W. and S. Schoch (1988) Chlorophylls. In Plant Pigments (Edited by T. W. Goodwin), pp. 1-59. Academic Press, London.
262. Rüdiger, W. and S. Schoch (1991) The last steps in chlorophyll biosynthesis. In Chlorophylls (Edited by H. Scheer), pp. 451-464. CRC Press, Boca Raton, FL.
263. Rüdiger, W., J. Benz and C. Guthoff (1980) Detection and partial characterization of activity of chlorophyll synthetase in etioplast membranes. Eur. J. Biochem. 109, 193-200.
264. Soll, J., G. Schultz, W. Rüdiger and J. Benz (1983) Hydrogenation of geranylgeraniol. Two pathways exist in spinach chloroplasts. Plant Physiol. 71, 849-854.
265. Goodwin, T. W. and E. I. Mercer (1963) The regulation of sterol and carotenoid metabolism in germinating seedlings. Biochem. Soc. Symp., No. 24, pp. 37-41.
266. Green, T. R., D. T. Dennis and C. A. West (1975) Compartmentalization of isopentenyl pyrophosphate isomerase and prenyl transferase in developing castor bean endosperm. Biochem. Biophys. Res. Commun. 64, 976-982.
267. Rüdiger, W. and J. Benz (1984) Synthesis of chloroplast pigments. In Chloroplast Biogenesis (Edited by R. J. Ellis), pp. 225-244. Cambridge University Press, Cambridge, UK.
268. Schoch, S., U. Lempert and W. Rüdiger (1977) über die letzten Stufen der Chlorophyll-Biosynthese. Zwischenprodukte zwischen Chlorophyllid und phytolhaltigem Chlorophyll. Z. Pflanzenphysiol. 83, 427-436.
269. 14C-isopentenyldiphosphate, geraniol and farnesol into chlorophyll in plastid membrane fractions of Avenu sativa L. Z. Pflanzenphysiol. 102, 95-100.
270. Benz, J. and W. Rüdiger (1981) Chlorophyll biosynthesis: various chlorophyllides as exogenous substrates for chlorophyll synthetase. Z. Naturforsch. 36c, 51-57.
271. Kotzabasis, K. and H. Senger (1989) Biosynthesis of chlorophyll b in pigment mutant C-2A' of Scenedesmus obliquus. Physiol. Plant. 76, 474-478.
272. Tanaka, A. and H. Tsuji (1981) Changes in chlorophyll a and b content in dark-incubated cotyledons excised from illuminated seedlings. Plant Physiol. 68, 567-570.
273. Walmsley, J. and H. Y. Adamson (1989) Chlorophyll accumulation and breakdown in light-grown barley transferred to darkness: effect of seedling age. Physiol. Plant. 77, 312-319.
274. 14C]glutamic acid) evidence of dark chlorophyll synthesis in the absence of chlorophyll accumulation. Physiol. Plant. 93, 435-444.
275. Ito, H., Y. Tanaka, H. Tsuji and A. Tanaka (1993) Conversion of chlorophyll b to chlorophyll a by isolated cucumber etioplasts. Arch. Biochem. Biophys. 306, 148-151.
276. Ito, H., S. Takaichi, H. Tsuji and A. Tanaka (1994) Properties of synthesis of chlorophyll a from chlorophyll b in cucumber etioplasts. J. Biol. Chem. 269, 22034-22038.
277. Ito, H. and A. Tanaka (1996) Determination of the activity of chlorophyll b to chlorophyll a conversion during greening of etiolated cucumber cotyledons by using pyrochlorophyllide b. Plant Physiol. Biochem. 34, 35-40.
278. Scheumann, V., S. Schoch, M. Helfrich and W. Rüdiger (1996) Reduction of the formyl group of Zn-pheophytin b in vitro and in vivo: a model for the chlorophyll b to a transformation. Z. Naturforsch. 51c, 185-194.
279. 5 pathway in Chromatium. Arch. Biochem. Biophys. 246, 192-198.
280. Pudek, M. R. and W. R. Richards (1975) A possible alternate pathway of bacteriochlorophyll biosynthesis in a mutant of Rhodopseudomonas sphaeroides. Biochemistry 14, 3132-3137.
281. Jones, O. T. G. (1963) The inhibition of bacteriochlorophyll biosynthesis in Rhodopseudomonas sphaeroides by 8-hydroxyquinoline. Biochem. J. 88, 335-343.
282. Jones, O. T. G. (1964) Studies on the structure of a pigment related to chlorophyll a produced by Rhodopseudomonas sphaeroides. Biochem. J. 91, 572-576.
283. Biel, A. J. and B. L. Marrs (1983) Transcriptional regulation of several genes for bacteriochlorophyll biosynthesis in Rhodopseudomonas sphaeroides in response to oxygen. J. Bacteriol. 156, 686-694.
284. Burke, D. H., M. Alberti and J. E. Hearst (1993) bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter capsulatus and identification of the third subunit of light-independent protochlorophyllide reductase in bacteria and plants. J. Bacteriol. 175, 2414-2422.
285. Leeper, F. J. (1981) Intermediate steps in the biosynthesis of chlorophylls. In Chlorophylls (Edited by H. Scheer), pp. 408-431. CRC Press, Boca Raton, FL.
286. Michalski, T. J., J. E. Hunter, M. K. Bowman, U. Smith, K. Bardeen, H. Gest, J. R. Morris and J. J. Katz (1987) Bacteriopheophytin g: properties and some speculation on a possible primary role for bacteriochlorophylls b and g in the biosynthesis of chlorophylls. Proc. Natl. Acad. Sci. USA 84, 2570-2574.
287. Smith, K. M. (1991) The structure and biosynthesis of bacter-iochlorophylls. In Biosynthesis of Tetrapyrroles (Edited by P. M. Jordan), pp. 237-255. Elsevier, Amsterdam.
288. Porra, R. J., E. E. Pfündel and N. Engel (1997) Metabolism and function of photosynthetic pigments. In Phytoplankton Pigments in Oceanography: Guidelines to Modern Methods (Edited by S. W. Jeffrey, R. F. C. Mantoura and S. W. Wright), pp. 85-126. UNESCO, Paris.
289. Kenner, G. W., J. Rimmer, K. M. Smith and J. F. Unsworth (1978) Pyrroles and related compounds. Part 39. Structural and biosynthetic studies of Chlorobium chlorophylls-660 (bacteriochlorophyll c). Incorporations of methionine and porphobilinogen. J. Chem. Soc. Perkin Trans. 110, 845-852.
290. 12. J. Am. Chem. Soc. 101, 3655-3656.
291. 13C-NMR evidence for bacteriochlorophyll formation in the green sulfur bacterium, Prosthecochloris. Eur. J. Biochem. 159, 189-194.
292. Wilhelm, C. (1990) The biochemistry and physiology of light-harvesting processes in chlorophyll b- and chlorophyll c-containing algae. Plant Physiol. Biochem. 28, 293-306.
293. Schmitt, A., G. Frank, P. James, W. Staudenmann, H. Zuber and C. Wilhelm (1994) Polypeptide sequence of the chlorophyll a/b/c-binding protein of the prasinophycean alga Mantoniella squamata. Photosynth. Res. 40, 269-277.
294. Jeffrey, S. W. and M. Vesk (1997) Introduction to marine phytoplankton and their pigment signatures. In Phytoplankton Pigments in Oceanography: Guidelines to Modern Methods (Edited by S. W. Jeffrey, R. F. C. Mantoura and S. W. Wright), pp. 37-84. UNESCO, Paris.
295. Dougherty, R. C., H. H. Strain, W. A. Svec, R. A. Uphaus and J. J. Katz (1970) The structure, properties and distribution of chlorophyll c. J. Am. Chem. Soc. 92, 2826-2833.
296. 3, a novel marine photosynthetic pigment. J. Chem. Soc. Chem. Commun. 23, 1827-1828.
297. 5 monomethyl ester, a protochlorophyll-like pigment present in some unicellular flagellates. Phytochemistry 5, 223-229.
298. Larkum, A. W. D., C. Scaramuzzi, R. G. Hiller, G. C. Cox and A. C. Turner (1994) A light-harvesting chlorophyll c-like pigment in Prochloron. Proc. Natl. Acad. Sci. USA 91, 679-683.
299. Wilhelm, C., I. Lenartz-Weiler, I. Wiedemann and A. Wild (1986) The light-harvesting system of a Micromonas species (Prasinophyceae): the combination of three different chlorophyll species in one single chlorophyll-protein complex. Phycologia 25, 304-312.
300. 1 from the green alga Matoniella squamata. Biochim. Biophys. Acta 892, 23-29.
301. Garredo, J. L., M. Zapatra and S. Muñiz (1995) Spectral characterization of new chlorophyll c pigments isolated from Emiliana huxleyi (Prymnesiophyceae) by high performance liquid chromatography. J. Phycol. 31, 761-768.
302. Beale, S. I. (1984) Biosynthesis of photosynthetic pigments. In Chloroplast Biogenesis (Edited by N. R. Baker and J. Barber), pp. 135-205. Elsevier, Amsterdam.