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

作者：Vullo Daniela; Kupriyanova Elena V; Scozzafava Andrea; Capasso Clemente; Supuran Claudiu T^*

来源：Bioorganic & Medicinal Chemistry, 2014, 22(5): 1667-1671.

DOI：10.1016/j.bmc.2014.01.026

• Carbonic anhydrase
• beta-Class
• Anion
• Enzyme inhibitor
• Cyanobacterium
• Carbon concentrating mechanism
• CO2 capture

We investigated the catalytic activity and inhibition of the beta-class carbonic anhydrase (CA, EC 4.2.1.1) CahB1, from the relict cyanobacterium Coleofasciculus chthonoplastes (previously denominated Microcoleus chthonoplastes). The enzyme showed good activity as a catalyst for the CO2 hydration, with a k(cat) of 2.4 x 10(5) s (1) and a k(cat)/K-m of 6.3 x 10(7) 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 (K(I)s >200 mM) whereas selenate and selenocyanide were ineffective inhibitors too, with K(I)s 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 (K(I)s 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 K(I)s in the range of 8-75 mu M, whereas acetazolamide inhibited the enzyme with a K-I 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 CO2 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.

• 出版日期2014-3-1