Photophysical processes in the NADH-alcohol dehydrogenase complex.
Fluorescent analysis showed the high sensitivity of the NADH-alcohol dehydrogenase complex to UV irradiation. The complex reacts to UV illumination with "photoresponse," a rapid decrease in NADH fluorescence intensity to some stationary level. No such decrease was found in the NADH solution without the protein. The maximum rate of photoresponse was observed at pH 8.0, i.e, the biochemical optimum for the enzyme. It is suggested that the main reason for the photoresponse is desorption of NADH from the protein due to vibrational and conformational relaxation after photoexcitation. The data obtained point to the possibility of controlling "dark" enzymatic processes with light.
Vekshin
N L
NL
Institute of Biological Physics, Academy of Sciences of the USSR, Moscow Region, Pushchino.
D000426:Alcohol Dehydrogenase / Q000378:metabolism / Q000528:radiation effects*; D000818:Animals; D006736:Horses; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D009243:NAD / Q000378:metabolism / Q000528:radiation effects*; D010084:Oxidation-Reduction; D011485:Protein Binding / Q000528:radiation effects; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D014466:Ultraviolet Rays
D009243:NAD; D000426:Alcohol Dehydrogenase