• The Korean Journal of Mycology
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• v.17 no.3
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• pp.161-168
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• 1989

Mitochondria in L. edodes were separated and purified by stepped sucrose density gradient centrifugation. In our previous work, we have found that the activation wavelengths of the mitochondrial ATPase and ATP synthase were 680 nm and 470 nm within the range of 400-700 nm, respectively. The activities of the above enzymes with wavelengths of 300-400 nm region were investigated. The mitochondrial ATPase and ATP synthase were stimulated at 380 nm and 330 nm, respectively, for 30 min illumination compared with dark control group. They, however, were inhibited at 330 nm and 350 nm, respectively. The presence of FAD resulted in inhibition of the activity of the ATPase and stimulation of the activity of the ATP synthase by the activation and inhibition wavelengths. However, the activities of these enzymes were not changed by NADH for the above wavelengths. In the spectral properties, the oxidation of $FADH_2$ into FAD occurs in the presence of the enzymes for illumination of the activation and inhibition wavelengths. Therefore, we can predict that the mitochondrial ATPase and ATP synthase may function as oxidant in the redox reaction by the light illumination and that the light-induced pigment of the mitochondrial ATP synthase should be an oxidized form of a flavoprotein.