首页> 外文会议>Symposium on Structures and Mechanisms: from Ashes to Enzymes, May 12-14, 2000 >Metalloproteins to Membrane Proteins: Biological Energy Transduction Mechanisms
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Metalloproteins to Membrane Proteins: Biological Energy Transduction Mechanisms

机译:从金属蛋白到膜蛋白的生物能传导机制

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Structural analyses of two macromolecular systems, the metalloprotein nitrogenase and the integral membrane protein MscL (mechanosensitive channel of large conductance), are discussed within the context of energy transduction mechanisms. Nitrogenase catalyzes the ATP dependent reduction of dinitrogen to ammonia during the process of biological nitrogen fixation, while MscL is a stretch activated (mechanosensitive) channel that opens and closes in response to changes in lateral tension applied to membranes. Although nitrogenase and MscL have very different structures and functions, they both mediate the coupling of two energetic processes. From these studies, it is suggested that effective coupling of two processes by transduction proteins occurs through conformational states common to each process.
机译:在能量传导机制的背景下,讨论了两个大分子系统的结构分析,即金属蛋白固氮酶和完整膜蛋白MscL(大电导的机械敏感通道)。固氮过程中,固氮酶催化ATP依赖的二氮还原为氨,而MscL是拉伸激活的(机械敏感)通道,可响应施加在膜上的侧向张力变化而打开和关闭。尽管固氮酶和MscL具有非常不同的结构和功能,但它们都介导了两个高能过程的耦合。从这些研究表明,转导蛋白通过两个过程共有的构象状态发生了两个过程的有效偶联。

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