Biophysical Studies of Metalloenzymes

拟建的生物物理研究包括两部分：金属酶的电子-核双共振（endor）研究；蛋白质复合物内远距离电子转移的研究。Hoffman博士从事(i)氢化酶的金属中心，（ii）极端嗜热菌的金属酶的多频连续波和脉冲endoror研究项目。混合金属血红蛋白杂交体提供了在刚性和晶体学定义的环境中研究电子转移的最佳系统。利用这个系统，霍夫曼博士将检查电子转移到氦温度的温度响应。他还将探讨控制非共价电子转移配合物所显示的合作结合转变的界面构象动力学。恩多光谱是回答许多关于金属酶活性位点结构和功能的基本问题的首选技术。远距离电子转移是最基本的化学和生物反应之一，但也是最难研究的反应之一。

The proposed biophysical studies comprises of two parts: electron-nuclear double resonance (endor) investigations of metalloenzymes; studies of long-range electron transfer within protein complexes. Dr. Hoffman is engaged in a program of multi- frequency cw and pulsed endor investigations of (i) the metal centers of hydrogenases, (ii) metalloenzymes from extreme thermophiles. Mixed-metal hemoglobin hybrids provide the optimal system for studying electron transfer within a rigid and crystallographically defined environment. Using this system Dr. Hoffman will examine the temperature response of electron transfer down to helium temperatures. He will also probe the interfacial conformational dynamics that control a cooperative binding transition displayed by non-covalent electron transfer complexes. %%% Endor spectroscopy is the technique of choice for answering many of the fundamental questions about the structure and function of metalloenzyme active sites. Long-range electron transfer is one of the most fundamental chemical and biological reactions, yet one of the most difficult to study.