근자외선 영역 (300 nm-400 nm)의 각 파장별 광조사에 따른 mitochondrial ATP synthase는 330 nm의 조사에서 어두운 상태의 대조구에 비하여 가장 활성화되었으며, 350 nm에서는 그 활성이 억제되었다. 또한, mitochondria ATPase는 380 nm의 조사에서 가장 활성화되었으며 330 nm에서는 활성이 억제됨으로써, mitochondrial ATP synthase와는 상반된 경향을 보였다. Flavin은 470 nm의 광조사에 따른 mitochondrial ATP synthase의 활성화를 유발하였으며 680 nm의 광조사에 의한 mitochondrial ATPase의 활성도를 억제함으로써, ATP synthase의 청색광에 대한 광수용체의 역할을 하는 것으로 추정되며, flavin inhibitor의 PAA 또는 KI의 처리 후 470 nm의 조사에 의한 ATP synthase의 활성도 감소현상은 이를 뒷받침해준다. Mitochondrial ATP synthase 및 ATPase는 NADH의 존재하에서 각 활성화파장의 조사에 대하여 활성도 변화를 나타내지 않음으로써, 두 효소의 광에 의한 활성화와 무관함을 보였다.
The activity changes of the mitochondrial ATP synthase and ATPase illuminated with near-UV lights (300-400 nm) have been observed and the effects of FAD and NADH on the light activation of the enzyme have been investigated in mitochondria of Lentinus edodes. The mitochondrial ATP synthase and ATPase were stimulated by the illuminations of 330 nm and 380 nm, but inhibited by 350 nm and 330 nm compared with dark control group, respectively. FAD, a flavin, induced the activation of the mitochondrial ATP synthase by the liiumantions of activation (470 nm) and inhibition (350 nm) wavelengths. It, however, inhibited the activity of mitochondrial ATPase by the illuminations of activations (680 nm) and inhibition (330 nm) wavelengths. The activity of the mitochondrial ATP synthase which had been treated with flavin inhibitor such as phenylacetic acid (PAA) or potassium iodide (KI), was inhibited by 470 nm illumination. But, when the mitochondrial ATPase was illuminated with 680 nm in the presence of PAA or KI, the activity of it did not change. The activities of the enzyme with NADH were not affected by the illuminations of activation and inhibition wavelengths. From these results, it is suggested that a endogeneous flavoprotein serves as the photorecptor for blue light activation of the mitochondrial ATP synthase in L. edodes.
