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.

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子弹和调查员（PI）可能已经从其他NIH来源获得了主要资金，因此可以在其他清晰的条目中代表。列出的机构适用于该中心，这不一定是调查员的机构。甲胺脱氢酶（MADH）是一种古老的细菌代谢酶，它在1herobic的世界中进化。它的厌氧起源得到了催化的高度进化的多步进化学的证明，以及在催化过程中使用辅助氧化还原蛋白伴侣而不是分子氧来去除电子。通过这些类型的电子传递反应产生的能量是活生物体中所有能量产生的基础。尽管是收敛进化的产物，但用酶催化的还原性化学类似于含铜胺氧化酶家族的化学，其人类的人类与晚期糖尿病并发症和充血性心脏病的血管变化有关。 该项目结合了单晶体可见光谱，X射线晶体学和冻结术以及小角度X射线散射，该项目将如何通过捕获催化性催化中间的催化性中间的蛋白质在原子分辨率下控制其复杂的多步反应，并在Denitrificans Madh（pd-Madh）（PD-Madh）（PD-MADH）中含有结构的结构，并确定其结构的结构。通过研究这种高度发达的代谢系统，这是当今线粒体和叶绿体中仍然发现的古代厌氧氧化还原化学物质的一部分，我们可以阐明利用能量和材料在地球上发展复杂寿命的基本过程。