The interaction of cobalt (II) complexes with bovine apocarbonic anhydrase B.
The second-order rate constants for interaction of a number of cobalt(II) complexes (including the aquated ion) with bovine apocarbonic anhydrase have been measured at pH equal to 7.5, 25 degrees C and I equal 0.1 M. The ease of entry of cobalt decreases, in general, as the number of its coordinated watersdecreases. The highest complexes (bis or tris) do not react. The Mono cobalt(II) -8-quinolinol-5-sulfonate and, particularly, 8-quinolinol complexes react very much more rapidly with apoenzyme than does Co(H20)6-2+ ion. The results are discussed.
D000818:Animals; D001051:Apoenzymes; D001059:Apoproteins; D001665:Binding Sites; D002256:Carbonic Anhydrases; D002417:Cattle; D003035:Cobalt; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008433:Mathematics; D009994:Osmolar Concentration; D011485:Protein Binding; D011487:Protein Conformation; D011804:Quinolines; D013329:Structure-Activity Relationship; D013451:Sulfonic Acids; D013696:Temperature; D014867:Water
D001051:Apoenzymes; D001059:Apoproteins; D011804:Quinolines; D013451:Sulfonic Acids; D014867:Water; D003035:Cobalt; D002256:Carbonic Anhydrases