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Phenol red (at a concentration of 0.2mM) has been used as indicator, working at the absorbance maximum of 557nm, with 10\u201320mM Hepes (pH 7.5, for \u03b1-CAs) or TRIS (pH 8.3 for \u03b2-CAs) as buffers, and 20mM Na2SO4 (for \u03b1-CAs) or 10\u201320mM NaClO4\u2013for \u03b2-CAs (for maintaining constant the ionic strength), following the initial rates of the CA-catalyzed CO2 hydration reaction for a period of 10\u2013100s. The CO2 concentrations ranged from 1.7 to 17mM for the determination of the kinetic parameters and inhibition constants. For each inhibitor, at least six traces of the initial 5\u201310% of the reaction have been used for determining the initial velocity. The uncatalyzed rates were determined in the same manner and subtracted from the total observed rates. Stock solutions of inhibitor (100mM) were prepared in distilled-deionized water and dilutions up to 0.01nM were done thereafter with distilled-deionized water. Inhibitor and enzyme solutions were preincubated together for 15min at room temperature prior to assay, in order to allow for the formation of the E-I complex. The inhibition constants were obtained by non-linear least-squares methods using te Cheng\u2013Prussof equation (Cheng, Y.; Prusoff, W.H. Biochem Pharmacol 1973, 22, 3099) and PRISM 3 for data analysis, whereas the kinetic parameters for the uninhibited enzymes from Lineweaver\u2013Burk plots, as reported earlier,13,14 and represent the mean from at least three different determinations. stCA 1 concentration in the assay system was of 10.3nM whereas that of stCA 2 of 13.4nM. For IC50 determinations, assays have been done at a concentrations of substrate of. 10mM."},{"key":"10.1016\/j.bmcl.2011.04.105_b0405","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1016\/j.bmcl.2009.11.124","volume":"20","author":"Temperini","year":"2010","journal-title":"Bioorg. Med. Chem. 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