Stability of Benzotriazole Derivatives with Free Cu, Zn, Co and Metal-Containing Enzymes: Binding and Interaction of Methylbenzotriazoles with Superoxide Dismutase and Vitamin B12

2nd International Conference on Advanced Materials

Abudalo, R.A.^1 ; Abudalo, M.A.^2 ; Hernandez, M.T.^3

Department of Clinical Laboratory Sciences, King Saud Bin Abdulaziz University for Health Sciences, P.O. Box. 2477, Al Ahsa

31982, Saudi Arabia^1

Chemistry Department, Jordan Universities of Science and Technology, P.O. Box 3030, Irbid

22110, Jordan^2

Department of Civil and Environmental Engineering, University of Colorado at Boulder, Campus Box 428, Boulder

CO

80309-0428, United States^3

关键词: Benzotriazole derivative;    Cobalamin (vitamin B12);    Copper centers;    Differential pulse polarography;    Enzyme systems;    Metal chelating;    Stability constants;    Super oxide dismutase;   

Others  :  https://iopscience.iop.org/article/10.1088/1757-899X/305/1/012024/pdf
DOI  :  10.1088/1757-899X/305/1/012024

来源: IOP

【 摘 要 】

Benzotriazole derivatives form very strong bonds with transition metals, and are the most widely used type of industrial corrosion inhibitor. Some benzotriazole derivatives have been implicated as hormone regulators which also carry the ability to induce uncoupling responses or otherwise inhibit respiration processes in some microorganisms. However, the mechanisms associated with benzotriazole toxicity and inhibition are unknown. Using Differential Pulse Polarography, the stability constants of commercially significant corrosion inhibitors, 4-And 5-methylbenzotriazole, coordinated with free Cu (II) and Co (III), were determined to be 1015and 108, respectively. Polarographic analyses were extended to confirm that methylbenzotriazole also binds the copper center(s) in the ubiquitous enzyme superoxide dismutase, and the Corrin site in the coenzyme cobalamin (Vitamin B12). These results suggest that the metal-chelating ability of this unique class of compounds may confer inhibition to certain enzyme systems.