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DEVELOPMENT OF SUPER RUBISCO FOR HIGH EFFICIENT PHOTOSYNTHESIS

Research Project

Project/Area Number 05660105
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field 応用微生物学・応用生物化学
Research InstitutionOsaka Prefecture University

Principal Investigator

WADANO Akira  OSAKA PREFECTURE UNIVERSITY,APPLIED BIOLOGICAL CHEMISTRY,ASSOCIATE PROFESSOR, 農学部, 講師 (40081575)

Project Period (FY) 1993 – 1994
Project Status Completed (Fiscal Year 1994)
Budget Amount *help
¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1994: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1993: ¥900,000 (Direct Cost: ¥900,000)
KeywordsHysteresis / RuBisCO / Fallover / Cloning / Photosynthesis / Carbon fixation
Research Abstract

When the illumination is enough under the atomospheric conditions, photosynthesis in higher plants is rate-limited in CO_2 fixation. This causes lowering of reaction efficiency of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) which is a enzyme of carbon fixation. This enzyme has only lower activity than other enzymes with 1/100 to 1/1000 activity and low affinity against substrate.
On the present study, I focused to the hysteresis with this enzyme and identified lysine residue which was related to fallover phenomena. On the other hand bacterial RuBisCO showed the inverse hysteresis so that the enzyme was converted to arginine or proline instead of lysine. These phenomena were affected by dithiothreitol ; lower was the concentration, higher the activity. From these results It suggested that the change of stereo-structure, which resulted in lysine residue, held the structure by the formation of disulfide bond and that the hysteresis was appeared.

Report

(3 results)
  • 1994 Annual Research Report   Final Research Report Summary
  • 1993 Annual Research Report
  • Research Products

    (6 results)

All Other

All Publications (6 results)

  • [Publications] A.Wadano,et al: "Bindung of ribulose 1,5-bisphosphate to the non-catalytic sites of ribulose 1,5-bisphosphate carbosylase/oxygenase and its matabolic implicvations." Plant Cell Physiol.,. 35. 317-321 (1994)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] A.Wadano,et al: "A rapid and sensitive method for determination of relative specificity of RuBisCO from various species by anion-exchange chromatography." Plant Cell Physiol.,. 37. 325-331 (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] A.Wadano,et al: "Modeling of Continuously and directlv analyzed biphasicreaction courses of ribulose 1,5-bisphosphate carboxylase/oxygenase." J.Biochem.,. 119. 487-499

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] A.Yokota, M.Higashioka, T.Taira, H.Usuda, A.Wadano, H.Murayama: "Bindung of ribulose 1,5-bisphosphate to the non-catalytic sites of ribulose 1,5-bisphosphate carboxylase/oxygenase and its metabolic implications." Plant Cell Physiol.35. 317-321 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] K.Uemura, Y.Suzuki, T.Shikanai, A.Wadano, R.G.Jensen, W.Chmara, A.Yokota.: "A rapid and sensitive method for determination of relative specificity of RuBisCO from various species by anion-exchange chromatography." Plant Cell Physiol.37. 325-331 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] A.Yokota, A.Wadano, H.Murayama.: "Modeling of Continuously and directly analyzed biphasic reaction courses of ribulose 1,5-bisphosphate carboxylase/oxygenase." J.Biochem.119. 487-499

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary

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Published: 1993-04-01   Modified: 2016-04-21  

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