BLUE COPPER PROTEINS

蓝铜蛋白

• 批准号: 8169299
• 负责人: NATARAJAN SUKUMAR
• 金额: $ 0.35万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-04-01 至 2011-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169299
• 关键词: Azurin; Bacteria; Biological Process; Ceruloplasmin; Computer Retrieval of Information on Scientific Projects Database; Copper; Electron Transport; Funding; Grant; Human; Institution; Laccase; Mediator of activation protein; Metabolism; Nature; Oxidases; Oxidation-Reduction; Photosynthesis; Plants; Plastocyanin; Play; Property; Proteins; Reaction; Research; Research Personnel; Resources; Respiration; Respiratory Chain; Role; Site; Source; United States National Institutes of Health; cytochrome c; methylamine dehydrogenase; mutant

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. Copper proteins are common in nature and involved in a variety of biological processes such as respiration, photosynthesis, and redox reactions critical to metabolism. The copper centers are classified according to their spectroscopic properties as type 1, type 2 or type 3. Type 1 copper sites are found in a wide range of electron transfer (ET) proteins, including amicyanin and azurin in bacteria, plastocyanin in plants, and multicopper oxidases such as fungal laccase and human ceruloplasmin. Amicyanin contain a single copper site and plays a critical role in the respiratory chain of certain methylotropic bacteria. It serves as a mediator of electron transfer between methylamine dehydrogenase to cytochrome c-551i. The mutants of amicyanin will be studied to find their role in the electron transfer.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 铜蛋白在自然界中很常见，参与多种生物过程，如呼吸、光合作用和对新陈代谢至关重要的氧化还原反应。铜中心根据其光谱特性分为 1 型、2 型或 3 型。1 型铜位点存在于多种电子转移 (ET) 蛋白中，包括细菌中的阿米青蛋白和天青蛋白、植物中的质体蓝蛋白和多铜氧化酶，例如真菌漆酶和人铜蓝蛋白。 阿米青蛋白含有单个铜位点，在某些甲基化细菌的呼吸链中发挥着关键作用。它充当甲胺脱氢酶与细胞色素 c-551i 之间电子转移的介体。 将研究阿米青蛋白的突变体以发现它们在电子转移中的作用。