Glycine as a substrate for photorespiration |
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Authors: | KISAKI, TAKURO TOLBERT, N. E. |
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Affiliation: | Central Research Institute, Japan Monopoly Corporation Nishishinagawa, Tokyo, Japan |
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Abstract: | ![]() Substrates for photorespiration were examined by feeding 14Clabeled compounds to tobacco and corn leaf segments and by measuring14CO2 evolution in light and darkness. CO2 release in the darkwas rapid, but in light CO2 release was slow due to refixationby photosynthesis. Carboxyl labeled glycine was more rapidlydecarboxylated than were glyoxylate, glycolate or serine. Hydroxypyridinemethanesulfonate, an inhibitor of glycolate oxidase, blocked CO2 releasefrom glycolate but not from glycine. Isonicotynyl hydrazideblocked CO2 release from both glycine and glycolate. DCMU blockedphotosynthetic refixation of the released CO2, consequentlythe rates of CO2 release in light and dark were about equal.It was concluded that CO2 release during photo-respiration camefrom the conversion of 2 molecules of glycine to one serineand one CO2. 14CO2 release from glycine-l-14C in the dark or with DCMU inlight can be used as an assay for photorespiration ability. CO2 release from glycine and glycolate by corn leaf segmentsin the dark proceeded at the rate of that in normal tobaccoleaf. This result, together with other work on O2 exchange andenzymatic analysis, indicates that corn and other plants docarry on photorespiration, but it is not manifested by CO2 releasein light. A yellow tobacco mutant, Consolation 402, had high rates ofphotorespiration by the 14CO2 assay, nearly half (or more) asmany peroxisomes as chloroplasts, and high rates of CO2 releasefrom glycine-l-14C or glycolate-l-14C. A common tobacco, BrightYellow, had lower rates of photorespiration, fewer visible peroxisomes,and slower decarboxylation of glycine and glycolate. The amount of 14CO2 release from glycine-l-14C or glycolate-l-14Cincreased only slightly when the temperature was raised from25 to 35°C. 1Parts of this work were abstracted at the Annual Meeting (April,1969) of Japanese Society of Plant Physiologists, Kanazawa2Department of Biochemistry, Michigan State University, EastLansing, Michigan, U.S.A. (Received September 3, 1969; ) |
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