Effects of Glycine Hydroxamate, Carbon Dioxide, and Oxygen on Photorespiratory Carbon and Nitrogen Metabolism in Spinach Mesophyll Cells
Author(s) -
Arthur L. Lawyer,
Karen L. Cornwell,
Sherry L. Gee,
James A. Bassham
Publication year - 1982
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.69.5.1136
Subject(s) - photorespiration , glycine , serine , spinacia , glycine cleavage system , glyoxylate cycle , spinach , biochemistry , metabolism , serine hydroxymethyltransferase , chemistry , photosynthesis , amino acid , chloroplast , gene , enzyme
The effects of added glycine hydroxamate on the photosynthetic incorporation of (14)CO(2) into metabolites by isolated mesophyll cells of spinach (Spinacia oleracea L.) was investigated under conditions favorable to photorespiratory (PR) metabolism (0.04% CO(2) and 20% O(2)) and under conditions leading to nonphotorespiratory (NPR) metabolism (0.2% CO(2) and 2.7% O(2)). Glycine hydroxamate (GH) is a competitive inhibitor of the photorespiratory conversion of glycine to serine, CO(2) and NH(4) (+). During PR fixation, addition of the inhibitor increased glycine and decreased glutamine labeling. In contrast, labeling of glycine decreased under NPR conditions. This suggests that when the rate of glycolate synthesis is slow, the primary route of glycine synthesis is through serine rather than from glycolate. GH addition increased serine labeling under PR conditions but not under NPR conditions. This increase in serine labeling at a time when glycine to serine conversion is partially blocked by the inhibitor may be due to serine accumulation via the "reverse" flow of photorespiration from 3-P-glycerate to hydroxypyruvate when glycine levels are high. GH increased glyoxylate and decreased glycolate labeling. These observations are discussed with respect to possible glyoxylate feedback inhibition of photorespiration.
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