Hydrogen Peroxide is Scavenged by Ascorbate-specific Peroxidase in Spinach Chloroplasts
1981/08/01 by Yoshiyuki Nakano, Kozi Asada · 10,639 citations
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · Chemistry · Neuroscience · #Antioxidant #Ascorbic acid #Biochemistry #Chemistry #Chloroplast #Dehydroascorbic acid #Enzyme #Food science #Glutathione peroxidase #Glutathione reductase #Hydrogen peroxide #Organic chemistry #Peroxidase #Peroxide #Photoreceptor and optogenetics research #Photosynthetic Processes and Mechanisms #Photosystem I #Plant Stress Responses and Tolerance #Spinach #Superoxide dismutase #Vitamin C
paper · doi:10.1093/oxfordjournals.pcp.a076232
published in Plant and Cell Physiology 22(5), 867-880 (Oxford University Press)
openalex publication_date 1981/08/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/06
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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