Reversible binding and

The interaction within the active site can be either in the form of covalent binding or in the form of quasi-irreversible (tight but slowly reversible) binding, and it can involve the protein residues, the porphyrin moiety or the catalytic center (heme iron) [8]. CYP inactivation follows a stoichiometry of one substrate molecule per enzyme molecule inactivated. To measure the stoichiometry of the inactivation, it is necessary to trap all molecules that are not specifically bound to the active site, by using an appropriate scavenger, normally GSH. 

Reversible Binding and Activation of Dioxygen and the Reactivity of Peroxo and Hydroperoxo Dicopper(II) Complexes... 

The goal of our research on the multicopper oxidases has been to determine the spectral features of the type 3 (and type 2) centers, to use these spectral features to define geometric and electronic structural differences relative to hemocyanin and tyrosinase, and to understand how these structural differences contribute to their variation in biological function. The hemocyanins and tyrosinases reversibly bind and activate dioxygen whereas the multicopper oxidases catalyze its four-electron reduction to water. 

The essential properties of a suitable extractant for an industrial application are especially related to its distinctive (selective) affinity for the substrate together with the need for reversible binding and a rapid reaction rate in both directions. Chemical stability and high lipophilicity of the complexing agent and the extracted complex are also requirements. Last but not least, the price of the extractant can be an important consideration concerning its use. 

During the chromatographic process, the reversible binding (and release) of enantiomers from the mobile phase to SO sites in the CSPs is usually fast relative to the chromatographic time scale, and is essentially under thermodynamic control. The magnitude of aR s can be related to the difference of the free energies (AAGr s) of the diastereomeric association equilibria between chiral SO and the SAs... 

Certain poisons, called uncouplers, render the inner mitochondrial membrane permeable to protons. One example is the lipid-soluble chemical 2,4-dInItrophenol (DNP), which can reversibly bind and release protons and shuttle protons across the Inner membrane from the Intermembrane space Into the matrix. As a result, DNP dissipates the proton-motive... 

Mupirocin inhibits bacterial protein synthesis by reversible binding and inhibition of isoleucyl transfer-RNA synthetase. There is no cross-resistance with other classes of antibiotics. Low-level resistance, which is not clinically significant, is due to mutations of the host gene encoding isoleucyl transfer-RNA synthetase or an extra chromosomal copy of a gene encoding a modified isoleucyl transfer-RNA synthetase. High-level resistance (MIC > 1 mg/ml) is mediated by a plasmid or chromosomal copy of mupA, which encodes a bypass synthetase that binds mupirocin poorly. 

Fig. 2. Reversible binding and oxidative function of dicopper proteins.

Brown GC (1995) Reversible binding and inhibition of catalase by nitric oxide. Eur J Biochem 232 188-191... 

Noncovalent interactions are the basis of reversible binding and recognition events in biochemical systems that rely on noncovalent interactions such as salt bridges, hydrogen bonds, and hydrophobic interactions. The binding energies of such types... 

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