Hydrogen Peroxide is Scavenged by Ascorbate-specific Peroxidase in Spinach Chloroplasts
1981/08/01 by Yoshiyuki Nakano, Kozi Asada · 38 citations
Biochemistry, Genetics and Molecular Biology · Agricultural and Biological Sciences · Neuroscience · #Photosynthetic Processes and Mechanisms #Plant Stress Responses and Tolerance #Photoreceptor and optogenetics research
paper · doi:10.1093/oxfordjournals.pcp.a076232
Abstract
Abstract Intact spinach chloroplasts scavenge hydrogen peroxide with a peroxidase that uses a photoreductant as the electron donor, but the activity of ruptured chloroplasts is very low [Nakano and Asada (1980) Plant & Cell Physiol. 21 : 1295]. Ruptured spinach chloroplasts recovered their ability to photoreduce hydrogen peroxide with the concomitant evolution of oxygen after the addition of glutathione and dehydroascorbate (DHA). In ruptured chloroplasts, DHA was photoreduced to ascorbate and oxygen was evolved in the process in the presence of glutathione. DHA reductase (EC 1.8.5.1) and a peroxidase whose electron donor is specific to L-ascorbate are localized in chloroplast stroma. These observations confirm that the electron donor for the scavenging of hydrogen peroxide in chloroplasts is L-ascorbate and that the L-ascorbate is regenerated from DHA by the system: photosystem I→ferredoxin→NADP→glutathione. A preliminary characterization of the chloroplast peroxidase is given.
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