Lavi J, Raunio R, Malkov Y, Lövgren T
Biochem Biophys Res Commun. 1983 Feb 28;111(1):266-73. doi: 10.1016/s0006-291x(83)80146-6.
The effects of NADH:FMN oxidoreductase and luciferase concentrations on the light kinetics of the bacterial bioluminescent reaction were investigated. Light emission with low decay rates was obtained by regulating the conversion of NADH to NAD+ by controlling oxidoreductase activity. Constant light emission can be obtained when the oxidoreductase activity is below 2.5 U/1 in the assay system. The luciferase concentration affects the light intensity but it has no effect on the decay rate of light emission. The substrate decanal and the end-products NAD+ and capric acid had no effect on the light kinetics. The Michaelis constants of bacterial luciferase for FMNH2 and decanal were 3 X 10(-6) M and 8 X 10(-7) M, respectively, and those of oxidoreductase for FMN and NADH were 6.1 X 10(-6) M and 1.6 X 10(-5) M, respectively.
研究了NADH:FMN氧化还原酶和荧光素酶浓度对细菌生物发光反应光动力学的影响。通过控制氧化还原酶活性来调节NADH向NAD+的转化,从而获得低衰减率的发光。当分析系统中氧化还原酶活性低于2.5 U/1时,可获得恒定的发光。荧光素酶浓度影响光强度,但对发光衰减率没有影响。底物癸醛以及终产物NAD+和癸酸对光动力学没有影响。细菌荧光素酶对FMNH2和癸醛的米氏常数分别为3×10(-6) M和8×10(-7) M,氧化还原酶对FMN和NADH的米氏常数分别为6.1×10(-6) M和1.6×10(-5) M。