An ultraviolet light sensitive target in nitrate reductase of Escherichia coli K-12.
Ultraviolet light was shown to inactivate purified nitrate reductase in the presence of reduced benzyl viologen. Loss of activity was not complete, reaching 60 to 70%. Photolysis was maximum at 345 nm. The differential spectrum between native and irradiated enzyme exhibited absorption bands at 216, 275, 314 and 365 nm. The photosensitive electron carrier could be extracted by organic solvents. It had the following absorption bands: 225, 275 and 285 nm. It was reduced by Nile blue A but not by methylene blue. The precise nature of this light sensitive molecule could not be determined although the results support the idea that this chromophore might be a naphthoquinone.
Francisco
R
R
Grupo de Biología Experimental, Facultad de Ciencias, Universidad de Los Andes, Mérida, Venezuela.
Brito
C
C
Dubourdieu
M
M
D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D009565:Nitrate Reductases / Q000037:antagonists & inhibitors / Q000528:radiation effects*; D013056:Spectrophotometry, Ultraviolet; D014466:Ultraviolet Rays
D009565:Nitrate Reductases