Cholesterol pp 57-87 | Cite as

Polyprenyl Diphosphate Synthases

  • Kyozo Ogura
  • Tanetoshi Koyama
  • Hiroshi Sagami
Chapter
Part of the Subcellular Biochemistry book series (SCBI, volume 28)

Abstract

Isoprenoids are the most diverse and abundant compounds occurring in nature. The study of isoprenoid biosynthesis began in order to increase our understanding of the process of cholesterol biosynthesis. The discovery of isopentenyl diphosphate (IPP), made independently by Lynen et al.(1958) and Bloch et al.(1959), opened the era of enzymatic studies on the fundamental chain elongation, which starts with the condensation between IPP and dimethylallyl diphosphate (DMAPP), with elimination of inorganic pyrophosphate. This chain elongation is interesting in that the reactions are regulated to proceed consecutively and terminate precisely at discrete chain lengths according to requirements of organisms. The chain length of the products varies widely from geraniol to natural rubber. In order to understand the mechanism of these reactions, it is essential to learn how many and what kinds of enzymes are involved in such chain elongation reactions.

Keywords

Micrococcus Luteus Farnesyl Diphosphate Farnesyl Pyrophosphate Isoprenoid Biosynthesis Inorganic Pyrophosphate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in to check access.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Adair, W. L., Jr., and Keller, R. K., 1982, Dolichol metabolism in rat liver: determination of the subcellular distribution of dolichyl phosphate and its site and rate of de novo biosynthesis, J. Biol. Chem. 257:8990–8996.PubMedGoogle Scholar
  2. Allen, M. C., Keenan, M. V., and Sack, J., 1976, Lactobacillus plantarum undecaprenyl pyrophosphate synthetase: purification and reaction requirements, Arch. Biochem. Biophys. 175:236–248.PubMedCrossRefGoogle Scholar
  3. Anderson, M., S., Yarger J. G., Burck, C. L, and Poulter, C. D., 1989, Farnesyl diphosphate synthase: molecular cloning, sequence, and expression of an essential gene from Saccharomyces cerevisiae, J. Biol. Chem. 264:19176–19184.PubMedGoogle Scholar
  4. Ashby, M. N., and Edwards, P. A., 1990, Elucidation of the deficiency in two yeast coenzyme Q mutants: characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase, J. Biol. Chem. 265:13157–13164.PubMedGoogle Scholar
  5. Ashby, M. N., Spear, D. H., and Edwards, P. A., 1990, Prenyltransferases: from yeast to man, in: Molecular Biology of Atherosclerosis: Twentieth Steenbock Symposium, pp. 27–34, Elsevier, New York.Google Scholar
  6. Attucci, S., Aitken, S. M., Gulick, P. J., and Ibrahim, R. K., 1995, Farnesyl pyrophosphate synthetase from white lupin: molecular cloning, expression, and purification of the expressed protein, Arch. Biochem. Biophys. 321:493–500.PubMedCrossRefGoogle Scholar
  7. Baba, T., and Allen, M. C., 1980, Prenyl transferases from Micrococcus luteus: characterization of undecaprenyl pyrophosphate synthetase, Arch. Biochem. Biophys. 200: 474–484.PubMedCrossRefGoogle Scholar
  8. Barnard, G. F., Langton, B., and Popják, G., 1978, Pseudo-isoenzyme forms of liver prenyl transferase, Biochem. Biophys. Res. Commun. 85:1097–1103.PubMedCrossRefGoogle Scholar
  9. Barnard, G. F., and Popják, G., 1980, Characterization of liver prenyl transferase and its inactivation by phenylglyoxal, Biochim. Biophys. Acta 617:169–182.PubMedCrossRefGoogle Scholar
  10. Barnard, G. F., and Popják, G., 1981, Human liver prenyltransferase and its characterization, Biochim. Biophys. Acta 661:87–99.PubMedCrossRefGoogle Scholar
  11. Bartlett, D. L., King, C.-H. R., and Poulter, C. D., 1985, Purification of farnesylpyrophosphate synthetase by affinity chromatography, Methods Enzymol. 110:171–184.PubMedCrossRefGoogle Scholar
  12. Blanchard, L., and Karst, F., 1993, Characterization of a lysine-to-glutamic acid mutation in a conservative sequence of farnesyl diphosphate synthase from Saccharomyces cerevisiae, Gene 125: 185–189.PubMedCrossRefGoogle Scholar
  13. Bloch, K., Chaykin, S., Phillips, A. H., and de Waard, A., 1959, Mevalonic acid pyrophosphate and isopentenylpyrophosphate, J. Biol. Chem. 234:2595–2608.PubMedGoogle Scholar
  14. Boguski, M. S., and McCormick, F., 1993, Proteins regulating Ras and its relatives, Nature 366: 643–654.PubMedCrossRefGoogle Scholar
  15. Carattoli, A., Romano, N., Ballario, P., Morelli, G., and Macino, G., 1991, The Neurospora crassa carotenoid biosynthetic gene (albino 3) reveals highly conserved regions among prenyltransferases. J. Biol. Chem. 266:5854–5859.PubMedGoogle Scholar
  16. Clarke, C. F., Tanaka, R. D., Svenson, K., Wamsley, M., Fogelman, A. M., and Edwards, P. A., 1987, Molecular cloning and sequence of a cholesterol-repressible enzyme related to prenyltransferase in the isoprene biosynthetic pathway, Mol. Cell. Biol. 7:3138–3146.PubMedGoogle Scholar
  17. Clarke, S., 1992, Protein isoprenylation and methylation at carboxyl-terminal cysteine residues, Annu. Rev. Biochem. 61:355–386.PubMedCrossRefGoogle Scholar
  18. Eberhardt, N. I., and Rilling, H. C., 1975, Prenyltransferase from Saccharomyces cerevisiae: purification to homogeneity and molecular properties, J. Biol. Chem. 250:863–866.PubMedGoogle Scholar
  19. Epstein, W. W., Lever, D., Leining, L. M., Bruenger, E., and Rilling, H. C., 1991, Quantitation of prenylcysteines by a selective cleavage reaction, Proc. Natl. Acad. Sci. USA 88:9668–9670.PubMedCrossRefGoogle Scholar
  20. Ericsson, J., Appelkvist, E.-L., Thelin, A., Chojnacki, T., and Daliner, G., 1992, Isoprenoid biosynthesis in rat liver peroxisomes: characterization of cis-prenyltransferase and squalene synthetase, J. Biol. Chem. 267:18708–18714.PubMedGoogle Scholar
  21. Ericsson, J., Runquist, M., Thelin, A., Andersson, M., Chojnacki, T., and Dallner, G., 1993, Distribution of prenyltransferase in rat tissues: evidence for a cytosolic all-trans-geranylgeranyl diphosphate synthase, J. Biol. Chem. 268:832–838.PubMedGoogle Scholar
  22. Fujii, H., Koyama, T., and Ogura, K., 1982, Hexaprenyl pyrophosphate synthetase from Micrococcus luteus B-P 26, J. Biol. Chem. 257:14610–14612.PubMedGoogle Scholar
  23. Fujii, H., Koyama, T., and Ogura, K., 1983, Essential protein factors for polyprenyl pyrophosphate synthetase, FEBS Lett. 161:257–260.PubMedCrossRefGoogle Scholar
  24. Fujisaki, S., Nishino, T., and Katsuki, H., 1986, Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesis, J. Biochem. 99:1327–1337.PubMedGoogle Scholar
  25. Fujisaki, S., Hara, H., Nishimura, Y., Horiuchi, K., and Nishino, T., 1990, Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli, J. Biochem. 108:995–10PubMedGoogle Scholar
  26. Goodman, D. W. S., and Popják, G., 1960, Studies on the biosynthesis of cholesterol: XII. Synthesis of allylic pyrophosphates from mevalonate and their conversion into squalene with liver enzymes, J. Lipid Res. 2:286–300.Google Scholar
  27. Gotoh, T., Koyama, T., and Ogura, K., 1987, The significance of the diphosphate linkage involved in the substrates for prenyltransferase. Geranyl-and dimethylallyl methylenediphosphonate as artificial substrates, Chem. Lett. 1627–1630.Google Scholar
  28. Gotoh, T., Koyama, T., and Ogura, K., 1988, Different roles of the diphosphate moieties of allylic and homoallylic diphosphates in prenyltransferase reaction, Biochem. Biophys. Res. Commun. 156: 396–402.PubMedCrossRefGoogle Scholar
  29. Gotoh, T., Koyama, T., and Ogura, K., 1992, Farnesyl diphosphate synthase and solanesyl diphosphate synthase reactions of diphosphate-modified allylic analogs: the significance of the diphosphate linkage involved in the allylic substrates for prenyltransferase, J. Biochem. 112:20–27.PubMedGoogle Scholar
  30. Grunler, J., Ericsson, J., and Dallner, G., 1994, Branch-point reactions in the biosynthesis of cholesterol, dolichol, ubiquinone and prenylated proteins, Biochim. Biophys. Acta 1212: 259–277.PubMedCrossRefGoogle Scholar
  31. Holloway, P. W., and Popják, G., 1967, The purification of 3,3-dimethylallyl-and geranyl-transferase and of isopentenyl pyrophosphate isomerase from pig liver, Biochem. J. 104: 57–70.PubMedGoogle Scholar
  32. Ishii, K., Sagami, H., and Ogura, K., 1983a, Farnesyl pyrophosphate synthetase located in microsomes from pig liver, J. Biochem. 93:1635–1639.PubMedGoogle Scholar
  33. Ishii, K., Sagami, H., and Ogura, K., 1983b, Decaprenyl pyrophosphate synthetase from mitochondria of pig liver, Biochem. Biophys. Res. Commun. 116:500–506.PubMedCrossRefGoogle Scholar
  34. Ishii, K., Sagami, H., and Ogura, K., 1985, Decaprenyl pyrophosphate synthetase from Paracoccus denitrificans, Biochim. Biophys. Acta 835:291–297.CrossRefGoogle Scholar
  35. Ishii, K., Sagami, H., and Ogura, K., 1986, A novel prenyltransferase from Paracoccus denitrificans, Biochem. J. 233:773–777.PubMedGoogle Scholar
  36. Jackson, S. M., Ericsson, J., Osborne, T. F., and Edwards, P., 1995, NR-Y has a novel role in sterol-dependent transcription of two cholesterogenic genes, J. Biol. Chem. 270:21445–21448.PubMedCrossRefGoogle Scholar
  37. Jeffries, L., Cawthorne, M. A., Harris, M., Diplock, A. T., Green, J., and Price, S. A., 1967, Distribution of menaquinones in aerobic Micrococcaceae, Nature 215:257–259.PubMedCrossRefGoogle Scholar
  38. Joly, A., and Edwards, P. A., 1993, Effect of site-directed mutagenesis of conserved aspartate and arginine residues upon farnesyl diphosphate synthase activity, J. Biol. Chem. 268: 26983–26989.PubMedGoogle Scholar
  39. Kandutsch, A. A., Paulus, H., Levin, E., and Bloch, K., 1964, Purification of geranylgeranyl pyrophosphate synthetase from Micrococcus lysodeikticus, J. Biol. Chem. 239:2507–2515.PubMedGoogle Scholar
  40. Koike-Takeshita, A., Koyama, T., Obata, S., and Ogura, K., 1995, Molecular cloning and nucleotide sequences of the genes for two essential proteins constituting a novel enzyme system for heptaprenyl diphosphate synthesis, J. Biol. Chem. 270:18396–18400.PubMedCrossRefGoogle Scholar
  41. Koyama, T., Saito, Y., Ogura, K., and Seto, S., 1977, Two forms of farnesyl pyrophosphate synthetase from hog liver, J. Biochem. 82:1585–1590.PubMedGoogle Scholar
  42. Koyama, T., Obata, S., Osabe, M., Takeshita, A., Yokoyama, K., Uchida, M., Nishino, T., and Ogura, K., 1993, Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: molecular cloning, sequence determination, overproduction, and purification, J. Biochem. 113:355–363.PubMedGoogle Scholar
  43. Koyama, T., Obata, S., Saito, K., Takeshita-Koike, A., and Ogura, K., 1994a, Structural and functional roles of the cysteine residues of Bacillus stearothermophilus farnesyl diphosphate synthase, Biochemistry 33:12644–12648.PubMedCrossRefGoogle Scholar
  44. Koyama, T., Saito, K., Ogura, K., Obata, S., and Takeshita, A., 1994b, Site-directed mutagenesis of farnesyl diphosphate synthase; effect of substitution on the three carboxyl-terminal amino acids, Can. J. Chem. 72:75–79.CrossRefGoogle Scholar
  45. Koyama, T., Tajima, M., Nishino, T., and Ogura, K., 1995, Significance of Phe-220 and Gln-221 in the catalytic mechanism of farnesyl diphosphate synthase of Bacillus stearothermophilus, Biochem. Biophys. Res. Commun. 212:681–686.PubMedCrossRefGoogle Scholar
  46. Koyama, T., Tajima, M., Sano, H., Doi, T., Koike-Takeshita, A., Obata, S., Nishino, T., and Ogura, K., 1996, Identification of Significant Residues in the Substrate Binding Site of Bacillus stearother-mophilus Farnesyl Diphosphate Synthase, Biochemistry, 35:9533–9538.PubMedCrossRefGoogle Scholar
  47. Krisans, S. K., Ericsson, J., Edwards, P. A., and Keller, G.-A., 1994, Farnesyl-diphosphate synthase is localized in peroxisomes, J. Biol. Chem. 269:14165–14169.PubMedGoogle Scholar
  48. Lutz, R. J., Mclain, T. M., and Sinensky, M., 1992, Feedback inhibition of polyisoprenyl pyrophosphate synthesis from mevalonate in vitro, J. Biol. Chem. 267:7983–7986.PubMedGoogle Scholar
  49. Lynen, F., Eggerer, H., Henning, U., and Kessel, I., 1958, Farnesyl-pyrophosphat und 3-Methyl-Δ3-butenyl-1-pyrophosphat, die Biologischen Vorstufen des Squalens. Zur Biosynthase der Terpene, III, Angew. Chem. 70:738–742.CrossRefGoogle Scholar
  50. Lynen, F., Agranoff, B. W., Eggerer, H., Henning, U., and Möslein, E. M., 1959, γ.γ-Dimethylallyl-pyrophosphat und Geranyl-pyrophosphat, Biologische Vorstufen des Squalens. Zur Biosynthese der Terpene, VI, Angew. Chem. 71:657–663.CrossRefGoogle Scholar
  51. Marrero, P. F., Poulter, C. D., and Edwards, P. A., 1992, Effects of site-directed mutagenesis of the highly conserved aspartate residues in domain II of farnesyl diphosphate synthase activity, J. Biol. Chem. 267:21873–21878.PubMedGoogle Scholar
  52. Matsuoka, S., Sagami, H., Kurisaki, A., and Ogura, K., 1991, Variable product specificity of microsomal dehydrodolichyl diphosphate synthase from rat liver, J. Biol. Chem. 266: 3464–3468.PubMedGoogle Scholar
  53. Muth, J. D., and Allen, M. C., 1984, Undecaprenyl pyrophosphate synthetase from Lactobacillus plantrum: a dimeric protein, Arch. Biochem. Biophys. 230:49–60.PubMedCrossRefGoogle Scholar
  54. Nakane, H., Koyama, T., Obata, S., Osabe, M., Takeshita, A., Nishino, T., Ogura, K., and Miki, K., 1993, Crystallization and preliminary X-ray diffraction studies of Bacillus stearothermophilus farnesyl diphosphate synthase expressed in Escherichia coli, J. Mol. Biol. 233:787–788.PubMedCrossRefGoogle Scholar
  55. Najarian, D., Dihanich, M. E., Martin, N. C., and Hopper, A. K., 1987, DNA sequence and transcript mapping of MOD5: features of the 5’ region which suggest two translational starts, Mol. Cell. Biol. 7:185–191.PubMedGoogle Scholar
  56. Nandi, D. L., and Porter, J. W., 1964, The enzymatic synthesis of geranylgeranyl pyrophosphate by enzymes of carrot root and pig liver, Arch. Biochem. Biophys. 105:7–19.PubMedCrossRefGoogle Scholar
  57. Nishino, T., Ogura, K., and Seto, S., 1971, Reactivity of artificial substrates for prenyltransferase, Biochim. Biophys. Acta 235:322–325.PubMedCrossRefGoogle Scholar
  58. Nishino, T., Ogura, K., and Seto, S., 1972, Substrate specificity of farnesyl pyrophosphate synthetase, J. Am. Chem. Soc. 94:6849–6853.PubMedCrossRefGoogle Scholar
  59. Ogura, K., Nishino, T., Koyama, T., and Seto, S., 1970, Enzymic condensation of 3-methyl-2-alkenyl pyrophosphates with isopentenyl pyrophosphate, J. Am. Chem. Soc. 92:6036–6041.PubMedCrossRefGoogle Scholar
  60. Ogura, K., Shinka, T., and Seto, S., 1972, The purification and properties of geranylgeranyl pyrophosphate synthetase from pumpkin fruit, J. Biochem. 72:1101–1108.PubMedGoogle Scholar
  61. Ohnuma, S., Koyama, T., and Ogura, K., 1991, Purification of solanesyl-diphosphate synthase from Micrococcus luteus. A new class of prenyltransferase, J. Biol. Chem. 266:23706–23713.PubMedGoogle Scholar
  62. Poulter, C. D., and Rilling, H., 1976, Prenyltransferase: the mechanism of the reaction, Biochemistry 15:1079–1083.PubMedCrossRefGoogle Scholar
  63. Poulter, C. D., Wiggins, P. I., and Le, A. T., 1981, Farnesylpyrophosphate synthetase. A stepwise mechanism for the 1′-4 condensation reaction, J. Am. Chem. Soc. 103:3926–3927.CrossRefGoogle Scholar
  64. Reed, B. C., and Rilling, H. C., 1975, Crystallization and partial characterization of prenyltransferase from avian liver, Biochemistry 14:50–54.PubMedCrossRefGoogle Scholar
  65. Runquist, M., Ericsson, J., Thelin, A., Chojnacki, T., and Dallner, G., 1992, Biosynthesis of trans,trans,trans-geranylgeranyl diphosphate by the cytosolic fraction from rat tissues, Biochem. Biophys. Res. Commun. 186:157–165.PubMedCrossRefGoogle Scholar
  66. Runquist, M., Ericsson, J., Thelin, A., Chojnacki, T., and Dallner, G., 1994, Isoprenoid biosynthesis in rat liver mitochondria: studies on farnesyl pyrophosphate synthase and trans-prenyl-transferase, J. Biol. Chem. 269:5804–5809.PubMedGoogle Scholar
  67. Sagami, H., Ogura, K., and Seto, S., 1977, Solanesyl pyrophosphate synthetase from Micrococcus lysodeikticus, Biochemistry 16:4616-1622.Google Scholar
  68. Sagami, H., Ishii, K., and Ogura K., 1981, Occurrence and unusual properties of geranylgeranyl pyrophosphate synthetase of pig liver, Biochem. Int. 3:669–675.Google Scholar
  69. Sagami, H., Lennarz, W. J., and Ogura, K., 1989, The biosynthesis of dehydrodolichyl phosphates by rat liver microsomes, Biochim. Biophys. Acta 1002:218–224.PubMedCrossRefGoogle Scholar
  70. Sagami, H., Matsuoka, S., and Ogura, K., 1991, Formation of Z,E,E-geranylgeranyl diphosphate by rat liver microsomes, J. Biol. Chem. 266:3458–3463.PubMedGoogle Scholar
  71. Sagami, H., Korenaga, T., Ogura, K., Steiger, A., Pyun, H.-J., and Coates, R. M., 1992, Studies on geranylgeranyl diphosphate synthase from rat liver: specific inhibition by 3-azageranylgeranyl diphosphate, Arch. Biochem. Biophys. 297:314–320.PubMedCrossRefGoogle Scholar
  72. Sagami, H., Korenaga, T., Kurisaki, A., and Ogura, K., 1993a, Biosynthesis of prenyl diphosphates by cell-free extracts from mammalian tissues, J. Biochem. 114:112–117.PubMedGoogle Scholar
  73. Sagami, H., Korenaga, T., and Ogura, K., 1993b, Geranylgeranyl diphosphate synthase catalyzing the single condensation between isopentenyl diphosphate and farnesyl diphosphate, J. Biochem. 114:118–121.PubMedGoogle Scholar
  74. Sagami, H., Morita, Y., and Ogura, K., 1994, Purification and properties of geranylgeranyl-diphosphate synthase from bovine brain, J. Biol. Chem. 269:20561–20566.PubMedGoogle Scholar
  75. Sheares, B. T., White, S. S., Molowa, D. T., Chan. K., Ding, V. D.-H., Kroon, P. A., Bostedor, R. G., and Karkas, J. D., 1989, Cloning, analysis, and bacterial expression of human farnesyl pyrophosphate synthetase and its regulation in Hep G2 cells, Biochemistry 28:8129–8135.PubMedCrossRefGoogle Scholar
  76. Song, L., and Poulter, C. D., 1994, Yeast farnesyl-diphosphate synthase: site-directed mutagenesis of residues in highly conserved prenyltransferase domain I and II, Proc. Natl. Acad. Sci. USA 91:3044–3048.PubMedCrossRefGoogle Scholar
  77. Spear. D. H., Ericsson, J., Jackson, S. M., and Edwards, P. A., 1994, Identification of a 6-Base pair element involved in the sterol-mediated transcriptional regulation of farnesyl diphosphate synthase, J. Biol. Chem. 269:25212–25218.PubMedGoogle Scholar
  78. Tachibana, A., 1994, A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloal-kaliphilic archaeon, Natronobacterium pharaonis, FEBS Lett. 341:291–294.CrossRefGoogle Scholar
  79. Takahashi, I., Ogura, K., and Seto, S., 1980, Heptaprenyl pyrophosphate synthetase from Bacillus subtilis, J. Biol. Chem. 255:4539–4543.PubMedGoogle Scholar
  80. Tarshis, L. C., Yan, M., Poulter, C. D., and Sacchettini, J. C., 1994, Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-Å resolution, Biochemistry 33:10871–10877.PubMedCrossRefGoogle Scholar
  81. Teclebrhan, H., Olsson, J., Swiezewska, E., and Dallner, G., 1993, Biosynthesis of the side chain of ubiquinone: trans-prenyltransferase in rat liver microsomes, J. Biol. Chem. 268: 23081-23068.Google Scholar
  82. Wilkin, D. J., Kutsunai, S. Y., and Edwards, P. A., 1990, Isolation and sequence of the human farnesyl pyrophosphate synthase cDNA. Coordinate regulation of the mRNAs for farnesyl pyrophosphate synthetase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and 3-hydroxy-3-methylglutaryl coenzyme A synthase by phorbol ester, J. Biol. Chem. 265: 4607–4614.PubMedGoogle Scholar
  83. Wong, T. K., and Lennarz, W. J., 1982, The site of biosynthesis and intracellular deposition of dolichol in rat liver, J. Biol. Chem. 257:6619–6624.PubMedGoogle Scholar
  84. Yeh, L.-S., and Rilling, H. C., 1977, Purification and properties of pig liver prenyltransferase. Interconvertible forms of the enzyme, Arch. Biochem. Biophys. 183:718–725.PubMedCrossRefGoogle Scholar
  85. Yoshida, I., Koyama, T., and Ogura, K., 1989a, Protection of hexaprenyl-diphosphate synthase of Micrococcus luteus B-P 26 against inactivation by sulphydryl reagents and arginine-specific reagents, Biochim. Biophys. Acta 995:138–143.PubMedCrossRefGoogle Scholar
  86. Yoshida, I., Koyama, T., and Ogura, K., 1989b, Formation of a stable and catalytically active complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26, Biochem. Biophys. Res. Commun. 160:448–452.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Kyozo Ogura
    • 1
  • Tanetoshi Koyama
    • 1
  • Hiroshi Sagami
    • 1
  1. 1.Institute for Chemical Reaction ScienceTohoku University, Katahira 2 chomeAoba-ku, SendaiJapan

Personalised recommendations