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Regions of the Large Subunit of Rubisco that Compose the Active Site

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Biological Control of Photosynthesis

Part of the book series: Advances in Agricultural Biotechnology ((AABI,volume 19))

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Abstract

The regulation of the amount of carbon fixed by photosynthetic organisms is ultimately controlled by the kinetic parameters of ribulose-1,5-P2 carboxylase (Rubisco). The enzyme dictates the flow of ribulose-P2 through either photosynthetic carbon reduction leading to a net gain of organic carbon, or photorespiration, the loss of fixed carbon through oxygenation. Both of these activities, carboxylation or oxygenation of ribulose-P2, are catalysed at the same active site within the large (L) subunit of Rubisco. This bifunctionality of the enzyme is quite unique especially as there is apparently no requirement for transition metal prosthetic groups e.g. Cu or Fe, normally associated with oxygenation reactions. Clearly then to understand how the enzyme partitions the bisphosphate substrate between the opposing processes of carbon fixation and oxygenation requires detailed investigation of the two activities at the molecular level, particularly the nature of the groups that compose the active site.

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Abbreviations

e.p.r.:

electron paramagnetic resonance

Br-DHB-P2 :

3-bromo-l,4-dihydroxy-2-butanone-l,4-bisphosphate

-Br-AEP:

N-(bromoacetyl) ethanolamine phosphate

N-CldP-P2 :

2-N-chloroamino-2-deoxypentitol 1,5 bisphosphate

Br-AAdP-P2 :

2-(4-bromo acetamido-ani1ino-2-deoxypentitol 1,5-bisphosphate)

TNM:

tetranitromethane

References

  1. Gutteridge S, Parry MAJ, Schmidt CNG and Feeney J: FEBS Letters 179, 3255–359 (1984).

    Google Scholar 

  2. Sue JM and Knowles JR: Biochemistry 21, 5404–5410 (1982).

    Article  PubMed  CAS  Google Scholar 

  3. Sue JM and Knowles JR: Biochemistry 21, 5410–5414 (1982).

    Article  PubMed  CAS  Google Scholar 

  4. Lorimer GH, Pierce J, Gutteridge S, Schloss JV: In Advances in Photosynthesis Research: Ed C Sybesma: Nijhoff/Junk pp.725–734 (1983).

    Google Scholar 

  5. Bhagwat AS and Ramakrishna J: Bioch Biophys Acta 662, 181–189 (1983).

    Google Scholar 

  6. Paech C: Biochemistry 24, 3194–3199 (1985).

    Article  CAS  Google Scholar 

  7. Herndon CS, Norton IL and Hartman FC: Biochemistry 21, 1380–1385 (1982).

    Article  PubMed  CAS  Google Scholar 

  8. Lorimer GH: Biochemistry 20, 1236–1240 (1981).

    Article  PubMed  CAS  Google Scholar 

  9. Donnelly MI, Springer CD and Hartman FC: Biochemistry 22, 4346–4352 (1983).

    Article  CAS  Google Scholar 

  10. Stringer CD and Hartman FC: Bioch Biophys Res Comm 80, 1043–1048 (1978).

    Article  CAS  Google Scholar 

  11. Schloss JV, Stringer CD and Hartman FC: J Biol Chem 253, 5707–5711 (1978).

    PubMed  CAS  Google Scholar 

  12. Christeller JT and Hartman FC: FEBS Letters 142, 162–165 (1982).

    Article  CAS  Google Scholar 

  13. Herndon CS and Hartman FC: J Biol Chem 259, 3102–3110 (1984).

    PubMed  CAS  Google Scholar 

  14. Gutteridge S and Parry MAJ: Bioch Soc Trans In press (1985).

    Google Scholar 

  15. Lorimer GH, Badger MR and Andrews TJ: Biochemistry 15, 723–729 (1976).

    Article  Google Scholar 

  16. Somerville CR and Somerville SC: Mol Gen Genet 193, 214–219 (1984).

    Article  CAS  Google Scholar 

  17. Nargang F, McIntosh L and Somerville CR: Mol Gen Genet 193, 220–224 (1984).

    Article  CAS  Google Scholar 

  18. Pierce J and Gutteridge S: App Environ Microbiol 49, 1094–1100 (1985).

    CAS  Google Scholar 

  19. Gutteridge S, Sigal I, Thomas B, Arentzen R, Corova A and Lorimer GH: EMBO J 3, 2737–2743 (1984).

    PubMed  CAS  Google Scholar 

  20. Gutteridge S, Parry M, Schmidt CNG and Lorimer Bioch Soc Trans 15, 629–631 (1985).

    Google Scholar 

  21. Andersson I, Tjaeder AC, Cedergren E, Braenden CI: J Biol Chem 258, 14088–90 (1983).

    PubMed  CAS  Google Scholar 

  22. Barcena JA, Pickersgill RW, Adams, MJ, Philips DC and Whatley FR: EMBO J 2, 2363–2367 (1983).

    PubMed  CAS  Google Scholar 

  23. Janson CA, Smith, WW, Eisenberg D and Hartman FC: J Biol Chem 259, 11594–11596 (1984).

    PubMed  CAS  Google Scholar 

  24. Chou PY and Fasman GD: J Mol Biol 115, 135–175 (1977).

    Article  PubMed  CAS  Google Scholar 

  25. Garnier J, Osguthorpe DJ and Robson B: J Mol Biol 120, 97–120 (1978).

    Article  PubMed  CAS  Google Scholar 

  26. Paech C, Ryan FJ and Tolbert NE: Arch Biochem Biophys 179, 279–288 (1977).

    Article  PubMed  CAS  Google Scholar 

  27. Whitman WB and Tabita FR: Biochemistry 17, 1282–1293 (1978).

    Article  PubMed  CAS  Google Scholar 

  28. Chollet R: Biochim Biophys Acta 658, 177–190 (1981).

    PubMed  CAS  Google Scholar 

  29. Robinson PD and Tabita FR: Biochem Biophys Res Comm 80, 580–585 (1978).

    Article  Google Scholar 

  30. Bhagwat AS: Plant Sci Lett 27, 345–353 (1982).

    Article  CAS  Google Scholar 

  31. Barnard G, Roy H and Myer YP: Biochemistry 22, 2697–2704 (1983).

    Article  CAS  Google Scholar 

  32. Valle EM and Valleyos RH: Arch Biochem Biophys 231, 137–145 (1984).

    Article  Google Scholar 

  33. Fraij B and Hartman FC: J Biol Chem 257, 3501–3505 (1982).

    PubMed  CAS  Google Scholar 

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Author information

Authors and Affiliations

  1. Department of Biochemistry, Rothamsted Experimental Station, Harpenden, Herts, AL5 2JQ, UK

    S. Gutteridge, A. J. Keys & M. A. J. Parry

Authors
  1. S. Gutteridge
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  2. A. J. Keys
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  3. M. A. J. Parry
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Editor information

Editors and Affiliations

  1. Laboratory of Plant Physiology, Research Station of Gorsem, B-3800, Sint-Truiden, Belgium

    R. Marcelle

  2. Department SBM, Limburgs Universitair Centrum, B-3610, Diepenbeek, Belgium

    H. Clijsters  & M. van Poucke  & 

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© 1986 Martinus Nijhoff Publishers, Dordrecht

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Gutteridge, S., Keys, A.J., Parry, M.A.J. (1986). Regions of the Large Subunit of Rubisco that Compose the Active Site. In: Marcelle, R., Clijsters, H., van Poucke, M. (eds) Biological Control of Photosynthesis. Advances in Agricultural Biotechnology, vol 19. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-4384-1_4

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  • DOI: https://doi.org/10.1007/978-94-009-4384-1_4

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-8449-9

  • Online ISBN: 978-94-009-4384-1

  • eBook Packages: Springer Book Archive

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