SAXS OF METHYLAMINE DEHYDROGENASE ELECTRON TRANSFER PROTEIN COMPLEXES

甲胺脱氢酶电子转移蛋白复合物的 SAXS

• 批准号: 7369165
• 负责人: CAROLINE MARY WILMOT
• 金额: $ 0.44万
• 依托单位: ILLINOIS INSTITUTE OF TECHNOLOGY
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-04-01 至 2007-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7369165
• 关键词: SAXS; METHYLAMINE; DEHYDROGENASE; ELECTRON; TRANSFER

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Methylamine dehydrogenase (MADH) is an ancient bacterial metabolic enzyme that evolved in a pre-aerobic world. Its anaerobic origins are attested to by the highly evolved multistep chemistry it catalyzes, and its use of ancillary redox protein partners, rather than molecular oxygen, to remove electrons during catalysis. The energy generated through these types of electron transfer reactions underlies all energy generation in living organisms. Although a product of convergent evolution, the reductive chemistry catalyzed by the enzyme is analogous to that of the copper-containing amine oxidase family, whose human counterparts are linked to late-diabetic complications and vascular changes in congestive heart disease. Using a novel combination of single crystal visible spectroscopy, X-ray crystallography and freeze-trapping, and small-angle X-ray scattering, this project will probe how the protein controls its complex multistep reaction at atomic resolution by trapping catalytic intermediates in Paracoccus denitrificans MADH (PD-MADH) containing crystals, and determining their structures. By studying this highly developed metabolic system, a part of the ancient anaerobic redox chemistries still found in mitochondria and chloroplasts today, we can shed light on the fundamental processes of harnessing energy and materials that evolved complex life on earth.

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。甲胺脱氢酶(MADH)是一种古老的细菌代谢酶，在有氧前环境中进化而来。它的厌氧起源被证明是由它催化的高度进化的多步骤化学，以及它在催化过程中使用辅助氧化还原蛋白质伙伴，而不是分子氧来移除电子。通过这些类型的电子转移反应产生的能量是生物体所有能量产生的基础。虽然是收敛进化的产物，但该酶催化的还原化学类似于含铜胺氧化酶家族，其人类同行与晚期糖尿病并发症和充血性心脏病的血管变化有关。利用单晶可见光谱、X射线结晶学和冷冻捕获以及小角X射线散射的新组合，本项目将探索蛋白质如何通过捕获含有晶体的催化中间体来控制其复杂的多步骤反应，并确定它们的结构。通过研究这一高度发达的代谢系统，我们可以揭示利用能量和物质的基本过程，这些物质进化出了地球上复杂的生命。