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

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 enhan...

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Bibliographic Details
Published in:Photosynthesis research 1987-01, Vol.12 (2), p.155-164
Main Authors: Rao, S, Kamath, G, Maralihalli, G, Bhagwat, A S
Format: Article
Language:English
Online Access:Get full text
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Summary: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.
ISSN:0166-8595
DOI:10.1007/BF00047945