Anion inhibition studies of the fastest carbonic anhydrase (CA) known, the extremo-CA from the bacterium Sulfurihydrogenibium azorense.
The α-carbonic anhydrase (CA, EC 4.2.1.1) from the extremophilic bacterium Sulfurihydrogenibium azorense, SazCA, is the fastest CA known to date as a catalyst for CO(2) hydration to bicarbonate and protons. We report an inhibition study of this enzyme with inorganic anions and several other small molecules known to interact with these metalloenzymes. Bicarbonate, carbonate and sulfate were ineffective SazCA inhibitors whereas most other inorganic anions were submillimolar inhibitors. The best inhibition was observed with trithiocarbonate, diethyldithiocarbamate, sulfamide, sulfamate, phenylboronic, and phenylarsonic acid, which showed inhibition constants in the range of 3-39 μM. As SazCA is very stable at high temperatures (being an 'extremo-CA') and very effective as a catalyst, the inhibition studies reported here may be crucial for designing biotechnological applications for this enzyme, for example for CO(2) capture processes.
Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy.
Daniela
D
Vullo
Viviana
V
De Luca
Andrea
A
Scozzafava
Vincenzo
V
Carginale
Mosè
M
Rossi
Claudiu T
CT
Supuran
Clemente
C
Capasso
D000595:Amino Acid Sequence; D000838:Anions / Q000737:chemistry* / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology*; D002245:Carbon Dioxide / Q000737:chemistry / Q000378:metabolism; D002257:Carbonic Anhydrase Inhibitors / Q000737:chemistry* / Q000378:metabolism; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D002384:Catalysis; D007700:Kinetics; D008969:Molecular Sequence Data; D010802:Phylogeny; D011485:Protein Binding; D016415:Sequence Alignment; D013696:Temperature
D000838:Anions; D002257:Carbonic Anhydrase Inhibitors; D002245:Carbon Dioxide; D002256:Carbonic Anhydrases