The epr spectra of the inhibitor derivatives of cobalt carbonic anhydrase.
The epr spectra at 4.2 K of inhibitor derivatives of cobalt carbonic anhydrase have been recorded. The spectra can be grouped into two classes according to whether the low-field signal is broad or sharp and with g ranges of 6.1-6.8, 2.3-2.9, 1.6-1.8, and 5.8-6.2, 2.2-2.8, 1.5-1.8, respectively, The two kinds of spectra have been empirically related to the features of the room-temperature solution electronic spectra. A third kind of epr spectrum with a single broad signal is obtained when the inhibitor is in large excess. The possibility of using the epr spectra for deducing the geometry of cobalt enzymes is discussed.
D000818:Animals; D001665:Binding Sites; D002257:Carbonic Anhydrase Inhibitors; D002256:Carbonic Anhydrases / Q000097:blood; D002417:Cattle; D003035:Cobalt / Q000494:pharmacology*; D004578:Electron Spin Resonance Spectroscopy; D004912:Erythrocytes / Q000201:enzymology; D007527:Isoenzymes / Q000037:antagonists & inhibitors; D007700:Kinetics; D011485:Protein Binding; D011487:Protein Conformation; D015032:Zinc / Q000494:pharmacology
D002257:Carbonic Anhydrase Inhibitors; D007527:Isoenzymes; D003035:Cobalt; D002256:Carbonic Anhydrases; D015032:Zinc