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Elucidation of reaction mechanism ofthe enzymes involved in the syntbssis of photosynthetic pigments

Research Project

Project/Area Number 18570105
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Structural biochemistry
Research InstitutionOsaka University

Principal Investigator

FUKUYAMA Keiichi  Osaka University, Graduate School of Science, Professor (80032283)

Project Period (FY) 2006 – 2007
Project Status Completed (Fiscal Year 2007)
Budget Amount *help
¥3,920,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥420,000)
Fiscal Year 2007: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2006: ¥2,100,000 (Direct Cost: ¥2,100,000)
Keywordsbilin reductase / photosynthesis / X-ray crystallography / chlorophyll / ferredoxin / bilin pigment / γ-glutamyltranspentidase / 光合成色素 / 反応中間体 / ビリベルジン / 構造性色素 / ビリン環元酵素 / 表面電荷
Research Abstract

Photosynthetic organisms utilize phytobilins, linear tetrapyrrole pigments, for photosynthesis and light sensing. Such organisms develop light harvesting systems to accomplish efficient photosynthesis in their living environments. Red algae and cyanobacteria have giant protein-pigment complexes called phycobilisomes as a light-harvesting system, in which phycobilins (one of phytobilins) are utilized for light-harvesting pigments. Phytobilins are biosynthesized from heme by heme oxygenase and ferredoxin dependent bilin reductases (FDBRs). PcyA, a member of FDBR family, is unique in reducing biliverdin Xiα (BV) to phycocyanobilin by two sequential steps, in which electrons are supplied by ferredoxin. We previously determined the crystal structure of PcyA from cyanobacterium Synechocystis sp. PCC 6803 in complex with BV. To shed light on the molecular mechanism of PcyA reaction, we synthesized the pigment, the product of the first step of PcyA reduction, and determined the crystal structure of PcyA-pigment complex. On the basis of the structure site directed mutagenesis and functional analysis are under way.
γ-Glutamyltranspeptidase (GGT) catalyzes the cleavage of such γ-glutamyl compounds as glutathione, and transfer of their γ-glutamyl group to water or to other amino acids and peptides. Azaserine and acivicin are classical and irreversible inhibitors of GGT, but their binding sites and the inhibition mechanisms remained to be defined. We have determined the crystal structures of GGT from Eacherichia coil in complex with azaserine and acivicin at 1.65 A resolution. They form a covalent bond with the Oγ atom of Thr391, the catalytic residue of GGT. Notably, in the azaserine complex the carbonyl of azaserine is attacked by Thr391 to form a tetrahedral intermediate. When acivicin is bound to GGT, a migration of the single and double bonds occurs in its dihydroisoxazole ring.

Report

(3 results)
  • 2007 Annual Research Report   Final Research Report Summary
  • 2006 Annual Research Report
  • Research Products

    (12 results)

All 2008 2007 2006 Other

All Journal Article (10 results) (of which Peer Reviewed: 4 results) Presentation (2 results)

  • [Journal Article] Mass spectroscopic identification of lysine residues of heme oxygenase-1that are involved in its interaction with NADPH-cytochrome P450 reductase2008

    • Author(s)
      Y. Higashimoto, M. Sugishima, H. Sato, H. Sakamoto, K. Fukuyama, G. Palmer, M. Noguchi
    • Journal Title

      Biochem. Biophys. Res. Commun. 367

      Pages: 852-858

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2007 Final Research Report Summary
    • Peer Reviewed
  • [Journal Article] Mass spectroscopic identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase2008

    • Author(s)
      Y., Higashimoto, M., Sugishima, H., Sato, H., Sakamoto, K., Fukuyama, G., Palmer, M., Noguchi
    • Journal Title

      Biochem. Biophys. Res. Commun 367

      Pages: 852-858

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2007 Final Research Report Summary
  • [Journal Article] Solvent Tuning of Electrochemical Potentials in the Active Sites of HiPIP Versus Ferredoxin2007

    • Author(s)
      A. Dey, F. E. Jenney Jr., M. W. W. Adams, E. Babini, Y. Takahashi, K. Fukuyama, K. O. Hodgson, B. Hedman, E. I. Solomon
    • Journal Title

      Science 318

      Pages: 1464-1468

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2007 Final Research Report Summary
    • Peer Reviewed
  • [Journal Article] Solvent Tuning of Electrochemical Potentials in the Active Sites of HiPIP Versus Ferredoxin2007

    • Author(s)
      A., Dey, F.E., Jenney, Jr., M.W.W., Adams, E., Babini, Y., Takahashi, K., Fukuyama, K.O., Hodgson, B., Hedman, E.I., Solomon
    • Journal Title

      Science 318 No.5855

      Pages: 1464-1468

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2007 Final Research Report Summary
  • [Journal Article] X-Ray Crystallographic and Biochemical Characterization of the lnhibitory Action of an lmidazole-dioxolate Compound on Heme Oxygenase2007

    • Author(s)
      M. Sugishima
    • Journal Title

      Biochemistry 46

      Pages: 1860-1867

    • Related Report
      2007 Annual Research Report
    • Peer Reviewed
  • [Journal Article] Induced-fitting and electrostatic potential change of PcyA upon substrate binding demonstrated by the crystal structure of the substrate-free form2006

    • Author(s)
      H.Hagiwara, M.Sugishima, Y.Takahashi, K.Fukuyama
    • Journal Title

      FEBS Letters 580・16

      Pages: 3823-3828

    • Related Report
      2006 Annual Research Report
  • [Journal Article] Crystal Structures of BchU,amethyltransferaseInvolvedinBacteriochlorophyll c Biosynthesis, and its Complex with S-Adenosylhomocysteine : Implications for Reaction Mechanism2006

    • Author(s)
      K.Wada, H.Yamaguchi, J.Harada, K.Niimi, S.Osumi, Y.Saga, H.Oh-oka, H.Tamiaki, K.Fukuyama
    • Journal Title

      Journal of Molecular Biology 360・4

      Pages: 839-849

    • Related Report
      2006 Annual Research Report
  • [Journal Article] フェレドキシン依存性ビリン環元酵素の構造研究2006

    • Author(s)
      杉島正一, 萩原義徳, 高橋康弘, 福山恵一
    • Journal Title

      日本結晶学会誌 48・4

      Pages: 283-289

    • Related Report
      2006 Annual Research Report
  • [Journal Article] Crystal Structures of Escherichia coli γ-Glutamyltranspeptidase in Complex with Azaserine and Acivicin: Novel Mechanistic Implication for Inhibition by Glutamine Antagonists

    • Author(s)
      K. Wada, J. Hiratake, M. Irie, T. Okada, C. Yamada, H. Kumagai, H. Suzuki, K. Fukuyama
    • Journal Title

      Journal of Molecular Biology (In press)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2007 Final Research Report Summary
    • Peer Reviewed
  • [Journal Article] Crystal Structures of Escherichia coil γ-Glutamyltranspeptidase in Complex with Azaserine and Acivicin : Novel Mechanistic Implication for Inhibition by Glutamine Antagonists

    • Author(s)
      K., Wada, J., Hiratake, M., Irie, T., Okada, C., Yamada, H., Kumagai, H., Suzuki, K., Fukuyama
    • Journal Title

      J. Mol. Biol (in press)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2007 Final Research Report Summary
  • [Presentation] Structures of phytobilin synthesis enzymes2007

    • Author(s)
      K. Fukuyama
    • Organizer
      7th International Conference on Tetrapyrrole Photoreceptors in Photosynthetic Organisms
    • Place of Presentation
      Kyoto TERRSA
    • Year and Date
      2007-12-12
    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2007 Final Research Report Summary
  • [Presentation] Structures of phytobilin synthesis enzymes2007

    • Author(s)
      K. Fukuyama
    • Organizer
      7th lnternational Conference on Tetrapyrrole Photo-receptors in Photosynthetic Organisms
    • Place of Presentation
      Kyoto, Japan
    • Year and Date
      2007-12-12
    • Related Report
      2007 Annual Research Report

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Published: 2006-04-01   Modified: 2016-04-21  

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