Home LiteratureArticle Details
PMID: 24276943 Published · ppublish English Journal Article

Some relationships between the biochemistry of photosynthesis and the gas exchange of leaves.

Planta ·Vol. 153 ·No. 4 ·1981-12-00 ·Pages 376-87

von Caemmerer S, Farquhar GD

Abstract

A series of experiments is presented investigating short term and long term changes of the nature of the response of rate of CO2 assimilation to intercellular p(CO2). The relationships between CO2 assimilation rate and biochemical components of leaf photosynthesis, such as ribulose-bisphosphate (RuP2) carboxylase-oxygenase activity and electron transport capacity are examined and related to current theory of CO2 assimilation in leaves of C3 species. It was found that the response of the rate of CO2 assimilation to irradiance, partial pressure of O2, p(O2), and temperature was different at low and high intercellular p(CO2), suggesting that CO2 assimilation rate is governed by different processes at low and high intercellular p(CO2). In longer term changes in CO2 assimilation rate, induced by different growth conditions, the initial slope of the response of CO2 assimilation rate to intercellular p(CO2) could be correlated to in vitro measurements of RuP2 carboxylase activity. Also, CO2 assimilation rate at high p(CO2) could be correlated to in vitro measurements of electron transport rate. These results are consistent with the hypothesis that CO2 assimilation rate is limited by the RuP2 saturated rate of the RuP2 carboxylase-oxygenase at low intercellular p(CO2) and by the rate allowed by RuP2 regeneration capacity at high intercellular p(CO2).

Authors & Affiliations
2 authors, click to expand affiliations / ORCID
von Caemmerer S
Department of Environmental Biology, Research School of Biological Sciences, Australian National University, P.O. Box 475, 2601, Canberra City, A.C.T., Australia.
Farquhar G D
References (19)
19 references, click to expand
  1. Carbon dioxide assimilation by leaves, isolated chloroplasts, and ribulose bisphosphate carboxylase from spinach.
    Plant Physiol. 1975 Jun;55(6):1087-92 PMID: 16659216
  2. Rate-limiting processes in photosynthesis at saturating light intensities.
    Nature. 1968 Nov 2;220(5166):453-7 PMID: 5686156
  3. Light-mediated activation of stromal sedoheptulose bisphosphatase.
    Biochem J. 1980 Dec 1;191(3):845-9 PMID: 6269533
  4. Stomatal function in relation to leaf metabolism and environment.
    Symp Soc Exp Biol. 1977;31:471-505 PMID: 756635
  5. Autocatalysis and light activation of enzymes in relation to photosynthetic induction in wheat chloroplasts.
    Arch Biochem Biophys. 1980 Apr 1;200(2):575-82 PMID: 7436424
  6. Oxygen Inhibition of Photosynthesis: II. Kinetic Characteristics as Affected by Temperature.
    Plant Physiol. 1977 May;59(5):991-9 PMID: 16659982
  7. Oxygen exchange in leaves in the light.
    Plant Physiol. 1980 Aug;66(2):302-7 PMID: 16661426
  8. Influence of certain environmental factors on photosynthesis and photorespiration in Simmondsia chinensis.
    Planta. 1977 Jan;134(2):127-32 PMID: 24419690
  9. COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS.
    Plant Physiol. 1949 Jan;24(1):1-15 PMID: 16654194
  10. Effect of Light Intensity during Growth on Photoinhibition of Intact Attached Bean Leaflets.
    Plant Physiol. 1980 Jun;65(6):1181-7 PMID: 16661356
  11. The significance of light activation of enzymes during the induction phase of photosynthesis in isolated chloroplasts.
    Arch Biochem Biophys. 1980 Jul;202(2):617-23 PMID: 6257171
  12. Elevated atmospheric partial pressure of CO2 and plant growth : I. Interactions of nitrogen nutrition and photosynthetic capacity in C3 and C4 plants.
    Oecologia. 1979 Dec;44(1):68-74 PMID: 28310466
  13. Energy transduction in chloroplasts: structure and function of the ATPase complex.
    Annu Rev Biochem. 1980;49:111-38 PMID: 6447471
  14. Models describing the kinetics of ribulose biphosphate carboxylase-oxygenase.
    Arch Biochem Biophys. 1979 Apr 1;193(2):456-68 PMID: 464606
  15. A model for the kinetics of activation and catalysis of ribulose 1,5-bisphosphate carboxylase.
    Biochem J. 1976 Dec 1;159(3):563-70 PMID: 12741
  16. Ribulose bisphosphate carboxylase--lack of dark inactivation of the enzyme in experiments with protoplasts.
    FEBS Lett. 1979 Jan 15;97(2):296-300 PMID: 761634
  17. D-Ribulose-1,5-bisphosphate carboxylase-oxygenase. Improved methods for the activation and assay of catalytic activities.
    Anal Biochem. 1977 Mar;78(1):66-75 PMID: 848758
  18. The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications.
    Biochemistry. 1976 Feb 10;15(3):529-36 PMID: 3199
  19. A biochemical model of photosynthetic CO2 assimilation in leaves of C 3 species.
    Planta. 1980 Jun;149(1):78-90 PMID: 24306196
Article Info
Journal
Planta
Abbr.
Planta
ISSN
0032-0935
Published
1981-12-00
Pages
376-87
Language
English
Region
Germany
NLM ID
1250576
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com