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Catalytic inactivation of human carbonic anhydrase I by a metallopeptide-sulfonamide conjugate is mediated by oxidation of active site residues.

Oxidation of active site residues (His and Trp), following catalytic inactivation of human carbonic anhydrase I by a copper−ATCUN conjugate of sulfanilimide, is evidenced by mass spectrometric analysis of tryptic and chymotryptic digests of the modified CA-I. Accordingly, residue oxidation rather than protein cleavage is the demonstrated mode of inactivation. An apparent second-order rate constant, k2 ∼ 7600 M-1min-1, has been determined for catalytic inactivation of CA-I.