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Journal of the Operational Research Society - 相似文献
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J. Burgess R.D.W. Kemmitt N. Morton C.T. Mortimer M.P. Wilkinson 《Journal of organometallic chemistry》1980,191(2):477-480
Enthalpies, ΔH(1) ?94.8 ± 6.0 and ΔH(6) ?57.1 ± 5.1 kJ mol?1, of the following reactions have been measured calorimetrically [Pt(trans-stilbene)(PPh3)2](s) + dpcp(g) → (PPh3)2Pt(dpcb)(s) + trans-stilbene(g) (1) [Pt(trans-stilbene)(PPh3)2](s) + bcbd(g) → (PPh3)2Pt(bcpd)(s) + trans-stilbene (g) (6) where dpcp is diphenylcyclopropenone, (PPh3)2Pt(dpcb) is (1,1-bistriphenylphosphine)platinadiphenylcyclobutenone, (PPh3)2O, bcbd is benzocyclobutene-1,2-dione and (PPh3)2Pt(bcpd) is (1,1-bistriphenylphosphine)platinabenzocyclopentanedione, . It is concluded that the five-membered platinacyclo ring system in (PPh3)2Pt(dpcb) is not heavily strained. 相似文献
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Alan R. Fersht Jian-Ping Shi Anthony J. Wilkinson David M. Blow Paul Carter Mary M. Y. Waye Greg P. Winter 《Angewandte Chemie (International ed. in English)》1984,23(7):467-473
Structure-activity relationships of enzymes can now be analyzed for the first time by the systematic alteration of protein structure. Recent developments in the chemical synthesis of DNA fragments and recombinant DNA technology enable the facile modification of proteins by highly specific mutagenesis of their genes. Kinetic analysis of the mutant enzymes combined with high-resolution structural data from protein X-ray crystallography allow direct measurements on the relationships between structure and function. In particular, the strength and nature of enzyme-substrate interactions and their detailed roles in catalysis and specificity can now be studied. We have developed such analysis of enzyme structure-function by site-directed mutagenesis of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus, concentrating so far on the subtle role of hydrogen bonding in both substrate specificity and catalysis. We find that the energetics of tyrosine and ATP binding must be analyzed in terms of an exchange reaction with solvent water. Based on this idea and structural data, we have engineered an enzyme of improved enzyme-substrate affinity, and there thus appear to be real prospects of engineering proteins of new specificities, activities, and structural properties. We are also using protein engineering to gather direct information on the nature of enzyme catalysis. For example, we find the catalysis of formation of Tyr-AMP from Tyr and ATP is due largely to electrostatic and hydrogen bonding interactions that are stronger in the transition state than in the ground state—a “strain” mechanism rather than acid-base or covalent catalysis. 相似文献