Anion inhibition study of the β-carbonic anhydrase (CahB1) from the cyanobacterium Coleofasciculus chthonoplastes (ex-Microcoleus chthonoplastes)

Research Area: Uncategorized Year: 2014
Type of Publication: Article
Journal: Bioorganic and Medicinal Chemistry Volume: 22
Number: 5 Pages: 1667-1671
cited By (since 1996)0
We investigated the catalytic activity and inhibition of the β-class carbonic anhydrase (CA, EC CahB1, from the relict cyanobacterium Coleofasciculus chthonoplastes (previously denominated Microcoleus chthonoplastes). The enzyme showed good activity as a catalyst for the CO 2 hydration, with a kcat of 2.4 × 105 s-1 and a kcat/Km of 6.3 × 107 M-1 s-1. A range of inorganic anions and small molecules were investigated as inhibitors of CahB1. Perchlorate and tetrafluoroborate did not inhibit the enzyme (KIs >200 mM) whereas selenate and selenocyanide were ineffective inhibitors too, with KIs of 29.9-48.61 mM. The halides, pseudohalides, carbonate, bicarbonate, trithiocarbonate and a range of heavy metal ions-containing anions were submillimolar-millimolar inhibitors (KIs in the range of 0.15-0.90 mM). The best CahB1 inhibitors were N,N-diethyldithiocarbamate, sulfamate, sulfamide, phenylboronic acid and phenylarsonic acid, with KIs in the range of 8-75 μM, whereas acetazolamide inhibited the enzyme with a KI of 76 nM. This is the first kinetic and inhibition study of a cyanobacterial CA. As these enzymes are widespread in many cyanobacteria, being crucial for the carbon concentrating mechanism which assures substrate to RubisCO for the CO 2 fixation by these organisms, a detailed kinetic/inhibition study may be essential for a better understanding of this superfamily of metalloenzymes and for potential biotechnological applications in biomimetic CO2 capture processes. © 2014 Elsevier Ltd. All rights reserved.
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