BLUE COPPER PROTEINS

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH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 中心，不一定是研究者的机构。 铜蛋白质在自然界中很常见，参与多种生物过程，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。铜中心根据它们的光谱性质被分类为1型、2型或3型。1型铜位点存在于广泛的电子转移（ET）蛋白中，包括细菌中的amicyanin和azurin，植物中的plastocyanin，以及真菌漆酶和人血浆铜蓝蛋白等多铜氧化酶。 Amicyanin含有一个单一的铜位点，在某些嗜甲基细菌的呼吸链中起着关键作用。它作为甲胺脱氢酶与细胞色素c-551 i之间电子转移的介体。 将研究amicyanin的突变体，以发现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.