CHEMISTRY AND BIOCHEMISTRY OF ENERGY TRANSFER

基团转移反应的机理及其催化作用 在酶和非酶系统和机制中研究 把化学能转换成功，我们将用 肌浆网钙转运ATPase。这 主体是控制和发挥健康和健康的重要因素 有病的肌肉。精确固定和熵损失在生物信息学中的作用 将对酶催化进行部分和完全的探讨 辅酶A转移酶的底物和通过检测小分子 远离基团的取代基大小的变化 反应基团的底物。速率和平衡常数 用于水溶液中氢键的形成和断裂 将会被检查。钙内化和钙离子交换的机制 钙ATPase的内部钙结合部位将是 特色化的。将通过搜索来检查磷酰基转移 对于一般的碱基催化和对于裂解的催化 碱性磷酸酶作用下的磷酸化吡啶。酰基氰化物 将作为胰凝乳酶的底物进行检测，以尝试 估计质子转移到离开基团的作用 催化；协同质子转移到离开氰化物是 不可能。质子间转移的机理 将通过确定布朗斯特德来检查电负性原子 总酸和总碱的标图和同位素效应 涉及扩散控制的酯氨解催化 质子转移。酰基卤化物的反应将被研究到 评估酰基离子中间体的重要性以及 双分子替代机制的可能性。这个 从碳中脱除质子的机理将用 以硫离子为活化基团确定是否有 过渡态结构随反应物变化的变化 结构；这些化合物预计会有一个小的内在 质子转移的障碍，可能使这种变化更多 容易察觉的。

Mechanisms of group transfer reactions and their catalysis will be studied in enzymic and nonenzymic systems and mechanisms for the conversion of chemical energy into work will be examined with the calcium-transporting ATPase of sarcoplasmic reticulum. This subject is important in the control and function of healthy and diseased muscle. The role of exact fixation and entropy loss in enzyme catalysis will be probed with partial and complete substrates for Coenzyme A transferase and by examining small changes in the size of substituents that are remote from the reacting groups of substrates. Rate and equilibrium constants for formation and breaking of hydrogen bonds in aqueous solution will be examined. The mechanism of calcium internalization and the internal calcium binding site of the calcium ATPase will be characterized. Phosphoryl transfer will be examined by a search for general base catalysis and for catalysis of the cleavage of phosphorylated pyridines by alkaline phosphatase. Acyl cyanides will be examined as substrates for chymotrypsin in an attempt to estimate the role of proton transfer to the leaving group in catalysis; concerted proton transfer to the leaving cyanide is not possible. The mechanism of proton transfer between electronegative atoms will be examined by determining Bronsted plots and isotope effects for general acid and general base catalysis of ester aminolysis involving diffusion-controlled proton transfer. Reactions of acyl halides will be examined to evaluate the importance of acylium ion intermediates and the possibility of a bimolecular substitution mechanism. The mechanism of proton removal from carbon will be studied using the sulfonium ion as activating group to determine if there are changes in transition state structure with changing reactant structure; these compounds are expected to have a small intrinsic barrier for proton transfer that may make such changes more readily detectible.