Buy Carbonic anhydrase metabolism is a key factor in the toxicity of CO"2 and COS but not CS"2 toward the flour beetle Tribolium castaneum [Coleoptera: Tenebrionidae] ... Biochemistry and Physiology, Part C] by V.S. Haritos, G. Dojchinov available and for sale on Brightsurf

View Larger Image	Carbonic anhydrase metabolism is a key factor in the toxicity of CO"2 and COS but not CS"2 toward the flour beetle Tribolium castaneum [Coleoptera: Tenebrionidae] ... Biochemistry and Physiology, Part C] by V.S. Haritos, G. Dojchinov List Price:  $10.95 Available:  Available for download now Studio:  Elsevier Binding:  Digital Publication Date:  January 01, 2005 Publisher:  Elsevier
FORMATS HTML EDITORIAL REVIEWS Product Description This digital document is a journal article from Comparative Biochemistry and Physiology, Part C, published by Elsevier in 2005. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser. Description: The analogues carbon dioxide (CO"2), carbonyl sulfide (COS) and carbon disulfide (CS"2) have been useful as substrate probes for enzyme activities. Here we explored the affinity of the enzyme carbonic anhydrase for its natural substrate CO"2, as well as COS and CS"2 (1) by in vitro kinetic metabolism studies using pure enzyme and (2) through mortality bioassay of insects exposed to toxic levels of each of the gases during carbonic anhydrase inhibition. Hydrolysis of COS to form hydrogen sulfide was catalysed rapidly showing parameters K"m 1.86 mM and K"c"a"t 41 s^-^1 at 25 ^oC; however, the specificity constant (K"c"a"t/K"m) was 4000-fold lower than the reported value for carbonic anhydrase-catalysed hydration of CO"2. Carbonic anhydrase-mediated CS"2 metabolism was a further 65,000-fold lower than COS. Both results demonstrate the deactivating effect toward the enzyme of sulfur substitution for oxygen in the molecule. We also investigated the role of carbonic anhydrases in CO"2, COS and CS"2 toxicity using a specific inhibitor, acetazolamide, administered to Tribolium castaneum (Herbst) larvae via the diet. CO"2 toxicity was greatly enhanced by up to seven-fold in acetazolamide-treated larvae indicating that carbonic anhydrases are a key protective enzyme in elevated CO"2 concentrations. Conversely, mortality was reduced by up to 12-fold in acetazolamide-treated larvae exposed to COS due to reduced formation of toxic hydrogen sulfide. CS"2 toxicity was unaffected by acetazolamide. These results show that carbonic anhydrase has a key role in toxicity of the substrates CO"2 and COS but not CS"2, despite minor differences in chemical formulae.