BLUE COPPER PROTEINS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 铜蛋白在自然界中很常见，参与了多种生物过程，如呼吸作用、光合作用和对新陈代谢至关重要的氧化还原反应。根据其光谱性质，铜中心被分为类型1、类型2或类型3。类型1存在于广泛的电子转移(ET)蛋白中，包括细菌中的氨基青素和天青素，植物中的质蓝蛋白，以及多铜氧化酶，如真菌漆酶和人类铜蓝蛋白。 氨基花青素含有单一的铜位置，在某些甲基化细菌的呼吸链中起着关键作用。它是甲胺脱氢酶向细胞色素c-551I传递电子的媒介。将对氨基花青素的突变体进行研究，以找出它们在电子转移中的作用。

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.