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New Trends in Enzyme Catalysis and Biomimetic Chemical Reactions 已有3人參與
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About two centuries ago the German poet, writer and philosopher J.W. Goethe noted that Nature is not only a great artist but also a skillful master. The contemporary generation of scientists who work in the fields of molecular biology, biochemistry and biophysics can appreciate to the fullest extent not only the internal beauty of natural molecular structures but also with what consummate skill these structures have been created. One of the wonderful creations of Nature, biological catalysis, appears as a challenging problem to chemists of the 21th century. The unique catalytic properties of enzyme, which are their precise specificity, selectivity, high rate of chemical reaction, and regulatory capacity occupy a great deal of attention. Classical and modern physical chemistry, chemical kinetics, organic, inorganic and quantum-chemistry provide an arsenal of physical methods and establish a basis for the investigation of structure and action mechanism of enzymes. The general properties of enzymes, the “ideal” chemical catalysts, are the formation of intermediates, smooth thermodynamic relief along the reaction coordinate, fulfillment of all selection rules for chemical reactions, the ability to proceed and to stop temporarily and spatially, and compatibility with the ambient media. These properties are possible by multifunctional active centers, by the unique structure of protein globules, possessing both rigidity and flexibility, and the formation of catalytic ensembles. Biochemistry returns to chemistry a plethora of knowledge about nearly “ideal” catalysts and opens the way for chemical modeling of enzyme reactions. This book is a view of enzyme catalysis by a physico-chemist with long-term experience in the investigation of structure and action mechanism of biological catalysts. This book is not intended to provide an exhaustive survey of each topic but rather a discussion of their theoretical and experimental background, and recent developments. The literature of enzyme catalysis is so vast and many scientists have made important contribution in the area, that it is impossible in the space allowed for this book to give a representative set of references. The author has tried to use reviews, and general principles of articles. He apologizes to those he has not been able to include. The first chapter of the present monograph expound upon new approaches and twists to traditional physical and kinetic methods of investigation of structure and action mechanism. The second chapter is a brief outline of current ideas on the general mechanisms of separate stages of enzyme catalytic processes. In the subsequent chapters, the author’s attention focuses on an analysis of structure and action mechanism of “tough” enzymatic processes which can not yet be effectively realized by chemists in ambient conditions: reduction of nitrogen, hydroxylation of alkans, conversion of light energy, photosynthetic water oxidation; etc. The present status of the knowledge of protein molecular dynamics (fluctuation dynamics of protein) and its paramount role in enzyme functions will be reviewed. Areas related to enzyme catalysis such as antibody catalysis, enzymes in organic solvents, enzymes in synthetic chemistry and enzyme design are outlined. In concluding chapter, a progress in chemical mimicking of “tough” enzymatic reactions is considered. |
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2014-07-15 16:16:39, 4.3 M
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