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Rao S, Kamath G, Maralihalli G, et al. Photoinactivation of δ-aminolevulinic acid dehydratase from maize by flavin mononuclotide. Photosynth Res. 1987;12(2):155-64doi: 10.1007/BF00047945.
Rao, S., Kamath, G., Maralihalli, G., & Bhagwat, A. S. (1987). Photoinactivation of δ-aminolevulinic acid dehydratase from maize by flavin mononuclotide. Photosynthesis research, 12(2), 155-64. https://doi.org/10.1007/BF00047945
Rao, S, et al. "Photoinactivation of δ-aminolevulinic acid dehydratase from maize by flavin mononuclotide." Photosynthesis research vol. 12,2 (1987): 155-64. doi: https://doi.org/10.1007/BF00047945
Rao S, Kamath G, Maralihalli G, Bhagwat AS. Photoinactivation of δ-aminolevulinic acid dehydratase from maize by flavin mononuclotide. Photosynth Res. 1987 Jan;12(2):155-64. doi: 10.1007/BF00047945. PMID: 24435638.
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Photosynth Res. 1987 Jan;12(2):155-64. doi: 10.1007/BF00047945.

Photoinactivation of δ-aminolevulinic acid dehydratase from maize by flavin mononuclotide.

Photosynthesis research

S Rao, G Kamath, G Maralihalli, A S Bhagwat

Affiliations

  1. Molecular Biology and Agriculture Division, Bhabha Atomic Research Centre, Trombay, 400 085, Bombay, India.

PMID: 24435638 DOI: 10.1007/BF00047945

Abstract

The δ-aminolevulinic acid dehydratase activity was irreversibly inactivated by irradiation of the enzyme in presence of flavin mononucleotide. The loss of enzyme activity was dependent on time of irradiation, concentration of FMN and intensity of irradiance. It required oxygen and was markedly enhanced in heavy water. The presence of levulinic acid (a competitive inhibitor of δ-ALAD) during irradiation prevented the inactivation considerably indicating photooxidative damage at or near the active site. Superoxide dismutase, sodium benzoate and sodium formate offered no protection, but singlet oxygen quenchers like azide and tryptophan were effective. NADH, electron donor to excited flavins, also prevented the loss of enzyme activity. These results indicate that singlet oxygen produced by light absorption of FMN was responsible for the photooxidative inhibition of the enzyme.

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