Kinetic And Anion Inhibition Studies Of A Beta-Carbonic Anhydrase (fbica 1) From The C-4 Plant Flaveria Bidentis(442 views) Monti SM, De Simone G, Dathan NA, Ludwig M, Vullo D, Scozzafava A, Capasso C, Supuran CT
Bioorg Med Chem Lett (ISSN: 0960-894x), 2013 Mar 15; 23(6): 1626-1630.
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
School of Chemistry and Biochemistry M310, University of Western Australia, Crawley, WA 6009, Australia
Università Degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy
Istituto di Biochimica Delle Proteine, CNR, Via P. Castellino 111, 80131 Napoli, Italy
Universit Degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy
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Kinetic And Anion Inhibition Studies Of A Beta-Carbonic Anhydrase (fbica 1) From The C-4 Plant Flaveria Bidentis
Several beta-carbonic anhydrases (CAs, EC 4. 2. 1. 1) are present in all land plants examined thus far. Here we report the first detailed biochemical characterization of one such isoform, FbiCA 1, from the C-4 plant Flaveria bidentis, which was cloned, purified and characterized as recombinant protein. FbiCA 1 has an interesting CO2 hydrase catalytic activity (k (cat) of 1. 2 x 10 (5) and k (cat) /K-m of 7. 5 x 10 (6) M-1 x s (-1)) and was moderately inhibited by most simple/complex inorganic anions. Potent FbiCA 1 inhibitors were also detected, such as trithiocarbonate, diethyldithiocarbamate, sulfamide, sulfamic acid, phenylboronic acid and phenylarsonic acid (K (I) s in the range of 4-60 mu M). Such inhibitors may be used as tools to better understand the role of various beta-CA isoforms in photosynthesis. (C) 2013 Elsevier Ltd. All rights reserved
Kinetic And Anion Inhibition Studies Of A Beta-Carbonic Anhydrase (fbica 1) From The C-4 Plant Flaveria Bidentis