STRUCTURE & FUNCTION OF PHOTOSYNTHETIC REACTION CENTERS

结构

• 批准号: 2734324
• 负责人: GEORGE FEHER
• 金额: $ 42.87万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN DIEGO
• 依托单位国家: 美国
• 财政年份: 1976
• 资助国家: 美国
• 起止时间: 1976-05-10 至 2000-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2734324
• 关键词: Chlamydomonas; X ray crystallography; atomic force microscopy; bioenergetics; computer simulation; crystallization; cytochrome c; dielectric property; electron density; electron nuclear double resonance spectroscopy; electron spin resonance spectroscopy; electron transport; hydrogen bond; ionic bond; lysozyme; molecular dynamics; mutant; oxidation reduction reaction; photosynthesis; photosynthetic bacteria; photosynthetic reaction centers; photosystem; protein structure function; quinones; structural biology

DESCRIPTION: In the broadest sense, Dr. Feher's objective is to understand biological processes and phenomena in terms of physical mechanisms; i.e., on a molecular level. The main problem addressed in this proposal deals with the conversion of electromagnetic energy into chemical energy; i.e., photosynthesis. This is one of the most basic processes in biology; all energy of the living world is derived from it. At the heart of the photosynthetic process is a membrane bound protein-pigment complex called the reaction center (RC). Dr. Feher studies the structure and function of the RC and the secondary donor, cytochrome c2. The mechanisms of electron and proton transfers that take place in the RC are of general interest and importance in all living systems. For instance, the processes that occur in mitochondria (e.g. in mammalian cells) can be viewed as the reverse process of photosynthesis utilizing similar mechanisms. Furthermore, the RC, being the best characterized membrane bound protein, serves as an excellent model for other membrane proteins that perform important functions in a variety of biochemical processes. The necessity of having single crystals to determine structures led Dr. Feher to a basic investigation of the crystallization mechanisms of macromolecules. Crystallization, in addition to being of great practical importance, serves as an example of molecular association (recognition); a ubiquitous phenomenon throughout the living world. The fields and methodologies involved in this work are interdisciplinary, ranging from physics to chemistry and molecular biology. The techniques used are: X-ray crystallography, electron and atomic force microscopy, optical and magnetic (EPR/ENDOR) spectroscopy, computational (e.g. Monte Carlo simulations), protein chemistry and recombinant DNA techniques. The specific problems addressed are: The three-dimensional structure of native and mutant RCs from the photosynthetic bacterium Rb. sphaeroides, the structures of cytochrome c2, the RC-cyt c2 complex, the RC from photosystem II of green plants; electron transfers in RCs, calculation of electrostatic energies in RCs and the mechanism of crystallization of biological macromolecules.

描述：在最广泛的意义上，Feher博士的目标是了解 物理机制方面的生物过程和现象;即，对 分子水平。 本建议所涉及的主要问题是： 电磁能转化为化学能;即， 光合作用 这是生物学中最基本的过程之一， 生命世界的能量来源于它。在心脏的 光合作用过程是一种膜结合的蛋白质-色素复合物， 反应中心（RC）。 Feher博士研究了 RC和第二供体细胞色素c2。 电子机制 和在RC中发生的质子转移是普遍感兴趣的， 在所有生命系统中的重要性。 例如，发生在 线粒体（例如哺乳动物细胞中的线粒体）可以被看作是相反的过程 光合作用利用类似的机制。 此外，作为 最好的特征膜结合蛋白，作为一个很好的模型， 对于其他在多种细胞膜中发挥重要功能的膜蛋白， 生化过程 必须有单晶体来确定结构，这使得Dr。 本文主要研究了非晶合金的结晶机理， 大分子 结晶除了具有很大的实用性外， 重要性，作为分子缔合（识别）的一个例子; 在整个生命世界中无处不在的现象。 这项工作涉及的领域和方法是跨学科的， 从物理学到化学和分子生物学。 的技术 使用的是：X射线晶体学，电子和原子力显微镜， 光学和磁性（EPR/ENDOR）光谱学，计算（例如Monte Carlo模拟）、蛋白质化学和重组DNA技术。 所处理的具体问题是： 来自光合细菌Rb的天然和突变体RC。球形细胞 细胞色素c2、RC-cyt c2复合物、来自光系统的RC的结构 绿色植物. RC中的电子转移.静电的计算 RC中的能量和生物结晶的机制 大分子