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• W2019456042 abstract "Cryoenzymology was initially used to slow down enzyme-catalyzed reactions so as to stabilize intermediates for further study. During the course of this early work, it became clear that cryoenzymology could be extended to other ends and some of these are described. First, the use of a cryosolvent on its own (or together with temperature) as a perturbant has allowed a resolution of the substrate binding steps of certain enzymes (myosin, d-amino acid oxidase, peroxidase and cytochrome P450). Second, by the use of cryosolvent and temperature, coupled with the classical physico-chemical perturbants, one can selectively modulate the various steps of an enzyme pathway. This approach can lead to an understanding of the mechanism of enzyme regulation. Finally, by carrying out experiments over a wide range of temperatures (−30°C–+30°C) and pressure (up to several kbars) in specially constructed fast reaction equipment, one can study the thermodynamic properties of the individual rate constants describing the interconversions of reaction intermediates. Experiments with creatine kinase, cytochrome P450 and peroxidase are described. The thermodynamic parameters ΔH, ΔG, ΔS and ΔV are thus measured and when this is done under different solvent conditions one can, at least within the theories available, attempt an approach to the problem of protein dynamics. A ses origines la cryoenzymologie était principalement destinée à ralentir les réactions enzymatiques dans le but de stabiliser et donc d'étudier des intermédiaires jalonnant une réaction enzymatique. Au cours du temps, diverses extensions sont apparues qui sont présentées dans cet article. La première concerne l'action des cryosolvants couplée ou non à celle de la température qui permet de détecter sur quelques exemples les étapes de fixation du substrat sur l'enzyme (myosine, d-aminoacide oxydase, peroxydase, cytochrome P450). L'action de ces mêmes perturbants conjuguée à celle des paramètres physico-chimiques classiques montre que les diverses étapes d'une réaction enzymatique sont plus ou moins modulables par l'environnement et que de telles modulations constituent autant de mécanismes régulateurs du déroulement de la réaction. Enfin, des balayages de température sur une large échelle (−30°C–+30°C) et de pression (jusqu'à plusieurs kbar) ont permis, à l'aide d'appareils spécialement construits, d'étudier les caractéristiques des constantes de vitesse individuelles d'interconversion entre complexes enzymatiques (creatine kinase, cytochrome P450, peroxydase). Divers paramètres thermodynamiques (ΔG, ΔH, ΔS, ΔV) sont ainsi mesurés dans des conditions de milieu variées et permettent, dans la limite des concepts actuels, de discuter du rôle fonctionnel de la dynamique des protéines." @default.
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• W2019456042 date "1986-09-01" @default.
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• W2019456042 title "New trends in cryoenzymology: Probing the functional role of protein dynamics by single-step kinetics" @default.
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• W2019456042 doi "https://doi.org/10.1016/s0300-9084(86)80178-x" @default.
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