US-Switzerland Cooperative Research: Photosynthetic Electron Transfer Reactions

该奖项为大卫B博士提供了适度的支持。克纳夫 技术大学，以促进长期的研究访问， 瑞士苏黎世大学。 在那里，他将与 与汉斯·R教授的两条研究路线。波斯哈德 生物化学研究所和工厂的Reinhard Bachofen教授 生物研究所。 这两个合作项目都代表了逻辑 Knaff博士目前研究的扩展;然而，他的实验室 没有足够的设备来执行某些方面的工作 一个人 与Bosshard教授的合作集中在阐明 两个之间的静电稳定复合物的细节 植物电子传递蛋白，铁氧还蛋白和铁氧还蛋白：NADP+ 氧化还原酶（FNR）。 FNR是植物光合作用的关键酶 光合放氧电子传递链 有机体 特定氨基酸基团的化学修饰 将被用来识别涉及的带电基团 将两种蛋白质结合在一起。 制备的抗体 将使用FNR上的不同站点来确定特定的角色 FNR上不同结构域在催化电子转移中的作用 铁氧还蛋白到NADP+。 的详细几何特征 铁氧还蛋白：FNR复合物可能提供线索， 其他铁氧还蛋白：酶复合物的构型。 它也可以 提供有关蛋白质复合物功能的见解 在哺乳动物的新陈代谢中。 博夏德教授拥有最先进的 他是一个公认的 世界领先的微分化学技术 修饰以鉴定参与的特定氨基酸残基 蛋白质复合物的形成。 与巴霍芬教授的合作将集中在确定 在一个区域中携带电子的蛋白质成分的变化 绿色红球藻的电子转移链 当细菌在需氧条件下生长时， 条件 这种光合作用的电子传递链 紫色无硫菌越来越好 近年来了解。 然而，人们对它的了解要少得多。 呼吸链比它的光合电子传递 链 光合紫中电子流之间的相似性 在线粒体、叶绿体和蓝细菌中 增加这项工作的潜在相关性和重要性。 巴霍芬教授的团队提供了宝贵的最先进的 计算机控制的光合细菌生长装置 以及这种细菌的分子生物学方面的专业知识。

This award provides modest support to Dr. David B. Knaff of Texas Tech University to facilitate a long term research visit to the University of Zurich, Switzerland. There he will collaborate in two lines of research with Professor Hans R. Bosshard of the Biochemistry Institute and Professor Reinhard Bachofen of the Plant Biology Institute. Both collaborative projects represent logical extensions of Dr. Knaff's current research; however, his laboratory is not adequately equipped to carry out certain aspects of the work alone. Collaboration with Professor Bosshard centers on elucidating the details of an electrostatically stabilized complex between two plant electron transfer proteins, ferredoxin and ferredoxin:NADP+ oxidoreductase (FNR). FNR is a key enzyme of the photosynthetic electron transfer chain of all oxygen-evolving photosynthetic organisms. Chemical modification of specific amino acid groups will be employed to identify the charged groups that are involved in holding the two proteins together. Antibodies prepared against different sites on FNR will be used to identify the specific roles of different domains on FNR in catalyzing electron transfer from ferredoxin to NADP+. Characterization of the detailed geometry of the ferrodoxin:FNR complex may provide clues to the likely configuration of other ferrodoxin:enzyme complexes. It may also provide insights into the functioning of related protein complexes in mammalian metabolism. Professor Bosshard has state-of-the-art facilities for protein sequencing and he is an acknowledged world-leader in using the technique of differential chemical modification to identify specific amino acid residues involved in the formation of protein complexes. Collaboration with Professor Bachofen will focus on identifying changes in electron-carrying protein constituents in one region of the electron transfer chain of Rhodopseudomonas viridis that occur when the bacterium is grown under aerobic versus photosynthetic conditions. The electron transfer chains of such photosynthetic purple non-sulfur bacteria have become increasingly better understood in recent years. However, much less is known about the respiratory chain than about its photosynthetic electron transfer chain. Resemblances between electron flow in photosynthetic purple bacteria and in mitochondria, chloroplasts and cyanobacteria increase the potential relevance and significance of this work. Professor Bachofen's group offers valuable state-of-the-art computer-controlled apparatus for growing photosynthetic bacteria and expertise in the molecular biology of such bacteria.