A cyanide-aldehyde complex inhibits bacterial luciferase.
نویسنده
چکیده
Cyanide at high (millimolar) concentrations inhibited in the in vitro Vibrio harveyi luciferase reaction. Cyanide reacted with free aldehyde to form an inhibitor. Inhibitor formation was accelerated by alkaline conditions and bovine serum albumin.
منابع مشابه
Affinity labeling of the aldehyde site of bacterial luciferase.
2-Bromo[1-14C]1-decanal was synthesized as an affinity labeling probe for the aliphatic aldehyde site of Vibrio harveyi luciferase. In the presence of excess amounts of this probe, the inactivation of bacterial luciferase occurred following apparent first order kinetics. This inactivation was markedly retarded in the presence of decanal but neither butanal (a very poor aldehyde substrate) nor F...
متن کاملInteraction of bacterial luciferase with aldehyde substrates and inhibitors.
Bacterial luciferase catalyzes the reaction of FMNH2, O2, and an aliphatic aldehyde to yield the carboxylic acid, FMN, water and blue-green light. The kinetics of the bacterial luciferase reaction were measured by stopped-flow spectrophotometry at pH 7 and 25 degrees C for the series of aldehydes from n-heptanal to n-undecanal. The rate of formation of the 4a-hydroperoxyflavin intermediate was ...
متن کاملThe oxygenated bacterial luciferase-flavin intermediate. Reaction products via the light and dark pathways.
The identity and stoichiometry of the reaction products of the oxygenated reduced flavin bacterial luciferase intermediate isolated by Sephadex chromatography at low temperature have been determined under two conditions, allowing the reaction to go to completion by warming either in the presence or absence of long chain aliphatic aldehyde. In the latter case, very little bioluminescence occurs,...
متن کاملStopped-flow kinetic analysis of the bacterial luciferase reaction.
The kinetics of the reaction catalyzed by bacterial luciferase have been measured by stopped-flow spectrophotometry at pH 7 and 25 degrees C. Luciferase catalyzes the formation of visible light, FMN, and a carboxylic acid from FMNH2, O2, and the corresponding aldehyde. The time courses for the formation and decay of the various intermediates have been followed by monitoring the absorbance chang...
متن کاملThe Purification Properties, and Chemiluminescent Quantum Yield of Bacterial Luciferase.
In the purified bacterial bioluminescent system obtained from Photobacterium jischeri it has been shown that the first step involves the reduction of enzyme by reduced flavin mononucleotide, followed by a combination of reduced enzyme with molecular oxygen (I). The proposed reaction scheme illustrates that aldehyde (RCHO) then reacts with a hypothetical peroxide intermediate to form a complex w...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of bacteriology
دوره 172 8 شماره
صفحات -
تاریخ انتشار 1990