Skip to main content
Plant Physiology logoLink to Plant Physiology
. 1983 Mar;71(3):568–573. doi: 10.1104/pp.71.3.568

Influence of Oxygen and Temperature on the Dark Inactivation of Pyruvate, Orthophosphate Dikinase and NADP-Malate Dehydrogenase in Maize 1

Hitoshi Nakamoto 1, Gerald E Edwards 1
PMCID: PMC1066079  PMID: 16662868

Abstract

The influence of oxygen and temperature on the inactivation of pyruvate, Pi dikinase and NADP-malate dehydrogenase was studied in Zea mays. O2 was required for inactivation of both pyruvate, Pi dikinase and NADP-malate dehydrogenase in the dark in vivo. The rate of inactivation under 2% O2 was only slightly lower than that at 21% O2. The in vitro inactivation of pyruvate, Pi dikinase, while dependent on adenine nucleotides (ADP + ATP), did not require O2.

The postillumination inactivation of pyruvate, Pi dikinase in leaves was strongly dependent on temperature. As temperature was decreased in the dark, there was a lag period of increasing length (e.g. at 17°C there was a lag of about 25 minutes) before inactivation proceeded. Following the lag period, the rate of inactivation decreased with decreasing temperature. The half-time for dark inactivation was about 7 minutes at 32°C and 45 minutes at 17°C. The inactivation of pyruvate, Pi dikinase in vitro following extraction from illuminated leaves was also strongly dependent on temperature, but occurred without a lag period. In contrast, NADP-malate dehydrogenase was rapidly inactivated in leaves (half-time of approximately 3 minutes) during the postillumination period without a lag, and there was little effect of temperature between 10 and 32°C. The results are discussed in relation to known differences in the mechanism of activation/inactivation of the two enzymes.

Full text

PDF
568

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Chapman K. S., Hatch M. D. Regulation of C4 photosynthesis: mechanism of activation and inactivation of extracted pyruvate, inorganic phosphate dikinase in relation to dark/light regulation. Arch Biochem Biophys. 1981 Aug;210(1):82–89. doi: 10.1016/0003-9861(81)90166-1. [DOI] [PubMed] [Google Scholar]
  2. Hatch M. D. Regulation of enzymes in C4 photosynthesis. Curr Top Cell Regul. 1978;14:1–27. [PubMed] [Google Scholar]
  3. Hatch M. D., Slack C. R. NADP-specific malate dehydrogenase and glycerate kinase in leaves and evidence for their location in chloroplasts. Biochem Biophys Res Commun. 1969 Mar 10;34(5):589–593. doi: 10.1016/0006-291x(69)90778-5. [DOI] [PubMed] [Google Scholar]
  4. Hatch M. D., Slack C. R. Studies on the mechanism of activation and inactivation of pyruvate, phosphate dikinase. A possible regulatory role for the enzyme in the C4 dicarboxylic acid pathway of photosynthesis. Biochem J. 1969 May;112(5):549–558. doi: 10.1042/bj1120549. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Helmerhorst E., Stokes G. B. Microcentrifuge desalting: a rapid, quantitative method for desalting small amounts of protein. Anal Biochem. 1980 May 1;104(1):130–135. doi: 10.1016/0003-2697(80)90287-0. [DOI] [PubMed] [Google Scholar]
  6. Jacquot J. P., Buchanan B. B. Enzyme Regulation in C(4) Photosynthesis : PURIFICATION AND PROPERTIES OF THIOREDOXIN-LINKED NADP-MALATE DEHYDROGENASE FROM CORN LEAVES. Plant Physiol. 1981 Aug;68(2):300–304. doi: 10.1104/pp.68.2.300. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Johnson H. S., Hatch M. D. Properties and regulation of leaf nicotinamide-adenine dinucleotide phosphate-malate dehydrogenase and 'malic' enzyme in plants with the C4-dicarboxylic acid pathway of photosynthesis. Biochem J. 1970 Sep;119(2):273–280. doi: 10.1042/bj1190273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Kagawa T., Hatch M. D. Regulation of C4 photosynthesis: characterization of a protein factor mediating the activation and inactivation of NADP-malate dehydrogenase. Arch Biochem Biophys. 1977 Nov;184(1):290–297. doi: 10.1016/0003-9861(77)90353-8. [DOI] [PubMed] [Google Scholar]
  9. Leegood R. C., Walker D. A. Activation of fructose 1,6-bisphosphatase in darkened intact chloroplasts by NADPH. Arch Biochem Biophys. 1981 Dec;212(2):644–650. doi: 10.1016/0003-9861(81)90408-2. [DOI] [PubMed] [Google Scholar]
  10. Nakamoto H., Sugiyama T. Partial characterization of the in vitro activation of inactive pyruvate, pi dikinase from darkened maize leaves. Plant Physiol. 1982 Apr;69(4):749–753. doi: 10.1104/pp.69.4.749. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Shirahashi K., Hayakawa S., Sugiyama T. Cold lability of pyruvate, orthophosphate dikinase in the maize leaf. Plant Physiol. 1978 Nov;62(5):826–830. doi: 10.1104/pp.62.5.826. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Wintermans J. F., de Mots A. Spectrophotometric characteristics of chlorophylls a and b and their pheophytins in ethanol. Biochim Biophys Acta. 1965 Nov 29;109(2):448–453. doi: 10.1016/0926-6585(65)90170-6. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES