Cavity active

Carbonic anhydrase an insight into the zinc binding site and into the active cavity through metal substitution. I. Bertini, C. Luchinat and A. Scozzafava, Struct. Bonding (Berlin), 1982, 48, 46-92 (296). 

Bertini I, Luchinat C, Scozzafava A (1982) Carbonic Anhydrase An Insight into the Zinc Binding Site and into the Active Cavity Through Metal Substitution. 48 45-91 Bertrand P (1991) Application of Electron Transfer Theories to Biological Systems. 75 1-48 Bill E, see Trautwein AX (1991) 78 1-96 Bino A, see Ardon M (1987) 65 1-28 Blanchard M, see Linares C (1977) 33 179-207 Blasse G, see Powell RC (1980) 42 43-96... 

Bertini, /., Luchinat, C., Scozzafava, A. Carbonic Anhydrase An Insight into the Zinc Binding Site and into the Active Cavity Through Metal Substitution. Vol. 48, pp. 45-91. 

Figure 2.5 Idealized representation of an active cavity (a) situation at maximum boiling suppression (b) situation at incipient boiling. (From Dwyer, 1976. Copyright 1976 by American Nuclear Society, LaGrange Park, IL. Reprinted with permission.)... 

When the active cavity size spectrum is limited, the treatment of Davis and Anderson (1966) (Sec. 4.2.1.1) should be employed here as well. 

These studies, extended to bovine, human, yeast, and to mutants human SOD Lys—143 and Ile-143 (which substitute the native Arg) have shown strict conservation of the active cavity as far as the metal ion is concerned (37). 

Some of the materials highlighted in this review offer novel redox-active cavities, which are candidates for studies on chemistry within cavities, especially processes which involve molecular recognition by donor-acceptor ii-Jt interactions, or by electron transfer mechanisms, e.g. coordination of a lone pair to a metal center, or formation of radical cation/radical anion pairs by charge transfer. The attachment of redox-active dendrimers to electrode surfaces (by chemical bonding, physical deposition, or screen printing) to form modified electrodes should provide interesting novel electron relay systems. 

Fig. 10.10 Surroundings of the active site of bovine CuZn-SOD (A)42) and schematic drawing of its active cavity (B)90). In (A), main chain shown in black bonds, ligand side chain open bonds, and other side chains with solid atoms and open bonds.

When the CH concentration is below saturation, the rate-limiting step in the catalytic process of CuZn-SOD is the diffusion of O2 to the active site channel and its binding to the Cu2+. After entering the active cavity, O2 diffuses to the coordination sphere of the Cu. This step involves a displacement of the Cu2+-bound water molecule by O2 and the formation of bonds among O2, the Cu2+ ion and Arg-143. The reduction of the Cu2+ is... 

Banci, L., Schroder, S. and Kollman, P. A. (1992) Molecular Dynamics Characterization of the Active Cavity of Carboxypeptidase A and Some of Its Inhibitor Adducts, Proteins Struct. Func. Gen 13, 288 -305. 

Site and into the Active Cavity Through Metal Substitution. Vol. 48, pp. 45-91. 

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