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Titlebook: Catalysis in Chemistry and Biochemistry Theory and Experiment; Proceedings of the T Bernard Pullman Conference proceedings 1979 D. Reidel P

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書目名稱Catalysis in Chemistry and Biochemistry Theory and Experiment
副標(biāo)題Proceedings of the T
編輯Bernard Pullman
視頻videohttp://file.papertrans.cn/223/222468/222468.mp4
叢書名稱Jerusalem Symposia
圖書封面Titlebook: Catalysis in Chemistry and Biochemistry Theory and Experiment; Proceedings of the T Bernard Pullman Conference proceedings 1979 D. Reidel P
出版日期Conference proceedings 1979
關(guān)鍵詞Coenzym; Oxidation; biochemistry; bonding; catalysis; catalyst; metals; proteins; quantum chemistry; structur
版次1
doihttps://doi.org/10.1007/978-94-009-9513-0
isbn_softcover978-94-009-9515-4
isbn_ebook978-94-009-9513-0Series ISSN 0924-4875
issn_series 0924-4875
copyrightD. Reidel Publishing Company, Dordrecht, Holland 1979
The information of publication is updating

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https://doi.org/10.1007/978-3-031-02232-6ical composition, in a large temperature range Enzymatic reactions are described. Rapid mixing of very low viscosity micromicellar solutions to record fast kinetic are discussed in comparison with results obtained in bulk water or in mixed hydro–organic solvents.
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https://doi.org/10.1007/978-3-031-02268-5he first solvation sphere. The zinc hydroxide mechanism for the enzymatic reaction is supported by the results obtained from a quantum mechanical study of the reaction 0H. + CO. ? HCO., indicating that the specific solvation in the active cleft of carbonic anhydrase may be the clue to the catalytic activity.
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Theoretical Studies on Models of the Active Site of Carbonic Anhydrase,inc, is more stable in the Glu - Thr - OH form, and the proton-relay process to that form occurs with no barrier..Further computations show that the OH + CO. reaction proceeds readily on zinc at the active site with no activation energy and a small exothermicity..The implications of these findings are discussed.
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