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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 10mM Hepes (pH 7.5) as buffer, 0.1M Na2SO4 (for maintaining constant the ionic strength), following 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 (0.1mM) were prepared in distilled-deionized water and dilutions up to 0.1nM 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\u2013I complex. The inhibition constants were obtained by non-linear least-squares methods using PRISM 3, as reported earlier,9 and represent the mean from at least three different determinations. Enzyme concentrations in the assay system were: 9.2nM for hCA I, 7.6nM for hCA II, 12nM for hCA IX, and 13nM for hCA XII.7\u20139"},{"key":"10.1016\/j.bmcl.2007.11.025_bib19","doi-asserted-by":"crossref","first-page":"7024","DOI":"10.1021\/jm060807n","volume":"49","author":"Winum","year":"2006","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bmcl.2007.11.025_bib20","doi-asserted-by":"crossref","first-page":"2210","DOI":"10.1016\/j.bmcl.2007.01.113","volume":"17","author":"Temperini","year":"2007","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bmcl.2007.11.025_bib21_1","doi-asserted-by":"crossref","first-page":"2351","DOI":"10.1016\/j.bmcl.2004.01.095","volume":"14","author":"Vullo","year":"2004","journal-title":"Bioorg. Med. Chem. 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