Elementary reaction

About: Elementary reaction is a research topic. Over the lifetime, 2972 publications have been published within this topic receiving 76110 citations.

Mechanism of reaction of myeloperoxidase with hydrogen peroxide and chloride ion

Abstract: The reaction of myeloperoxidase compound I (MPO-I) with chloride ion is widely assumed to produce the bacterial killing agent after phagocytosis. Two values of the rate constant for this important reaction have been published previously: 4.7 x 106 M-1.s-1 measured at 25 degrees C [Marquez, L.A. and Dunford, H.B. (1995) J. Biol. Chem. 270, 30434-30440], and 2.5 x 104 M-1.s-1 at 15 degrees C [Furtmuller, P.G., Burner, U. & Obinger, C. (1998) Biochemistry 37, 17923-17930]. The present paper is the result of a collaboration of the two groups to resolve the discrepancy in the rate constants. It was found that the rate constant for the reaction of compound I, generated from myeloperoxidase (MPO) and excess hydrogen peroxide with chloride, decreased with increasing chloride concentration. The rate constant published in 1995 was measured over a lower chloride concentration range; the 1998 rate constant at a higher range. Therefore the observed conversion of compound I to native enzyme in the presence of hydrogen peroxide and chloride ion cannot be attributed solely to the single elementary reaction MPO-I + Cl- --> MPO + HOCl. The simplest mechanism for the overall reaction which fit the experimental data is the following: MPO+H2O2 rk-1k1 MPO-I+H2O MPO-I+Cl- rk-2k2 MPO-I-Cl- MPO-I-Cl- -->k3 MPO+HOCl where MPO-I-Cl- is a chlorinating intermediate. We can now say that the 1995 rate constant is k2 and the corresponding reaction is rate-controlling at low [Cl-]. At high [Cl-], the reaction with rate constant k3 is rate controlling. The 1998 rate constant for high [Cl-] is a composite rate constant, approximated by k2k3/k-2. Values of k1 and k-1 are known from the literature. Results of this study yielded k2 = 2.2 x 106 M-1.s-1, k-2 = 1.9 x 105 s-1 and k3 = 5.2 x 104 s-1. Essentially identical results were obtained using human myeloperoxidase and beef spleen myeloperoxidase.

Force-activated reactivity switch in a bimolecular chemical reaction.

Abstract: The effect of mechanical force on the free-energy surface that governs a chemical reaction is largely unknown. The combination of protein engineering with single-molecule force-clamp spectroscopy allows us to study the influence of mechanical force on the rate at which a protein disulfide bond is reduced by nucleophiles in a bimolecular substitution reaction (S(N)2). We found that cleavage of a protein disulfide bond by hydroxide anions exhibits an abrupt reactivity 'switch' at ∼500 pN, after which the accelerating effect of force on the rate of an S(N)2 chemical reaction greatly diminishes. We propose that an abrupt force-induced conformational change of the protein disulfide bond shifts its ground state, drastically changing its reactivity in S(N)2 chemical reactions. Our experiments directly demonstrate the action of a force-activated switch in the chemical reactivity of a single molecule.

Generalized composite degradation kinetics for polymeric systems under isothermal and nonisothermal conditions

Abstract: A composite degradation methodology is extended to the conversion-dependence function in order to explain the importance of multiple reaction mechanisms which might be considered to be involved in degradation processes. Based on two elementary reaction mechanisms, a specific form of the model equation is derived, which is capable of describing various types of degradation behavior showing sigmoidal rate as well as deceleratory rate. The conversion-dependence function is derived to be independent of the Arrhenius-type reaction constant or temperature, and thus the kinetic parameters are determined by analytic methods that have been developed for isothermal and dynamic-heating experiments without any modification or additional assumptions. The developed model equation is tested by predicting the isothermal master curve of polyether-ether-ketone (PEEK), which is used as a model system in this study. The activation energies of the model system are analyzed using comparable methods for isothermal and dynamic experiments, which compare favorably in terms of the activation energy as a function of conversion. The resulting model equation, based on the kinetic parameters determined by isothermal experiments, can accurately predict both isothermal and dynamic-heating thermogravimetry utilizing the same constants and identical reaction mechanisms without additional assumption.