BLUE COPPER PROTEINS

$3,485P41FY2010RRNIH

Cornell University, Ithaca NY

Investigators

Linked publications, trials & patents

Paper 38508190 Paper 33131423 Paper 32748788 Paper 32581365 Paper 32389689 Paper 30559425 Paper 30289389 Paper 29946027 Paper 28338692 Paper 28045370 Paper 27936128 Paper 27905149 Paper 27463675 Paper 26988700 Paper 26959646 Paper 26745345 Paper 26729507 Paper 26715336 Paper 26707939 Paper 26701219 Paper 26689263 Paper 26644568 Paper 26508639 Paper 26481813 Paper 26472759 Paper 26459562 Paper 26387779 Paper 26349032 Paper 26278175 Paper 26172141 Paper 26130467 Paper 25970265 Paper 25901326 Paper 25831534 Paper 25794619 Paper 25752492 Paper 25728769 Paper 25713376 Paper 25553844 Paper 25484204 Paper 25422158 Paper 25414009 Paper 25372812 Paper 25352689 Paper 25313043 Paper 25231992 Paper 25198768 Paper 25184411 Paper 25136110 Paper 25136092 Paper 25128388 Paper 25102080 Paper 25079952 Paper 25043052 Paper 24948331 Paper 24939935 Paper 24898247 Paper 24820088 Paper 24727379 Paper 24717845 Paper 24692304 Paper 24661065 Paper 24646888 Paper 24599961 Paper 24531000 Paper 24523505 Paper 24523405 Paper 24459150 Paper 24416224 Paper 24362703 Paper 24316823 Paper 24316736 Paper 24257752 Paper 24248594 Paper 24218560 Paper 24185281 Paper 24152548 Paper 24136005 Paper 24130488 Paper 24121512 Paper 24106986 Paper 24099674 Paper 24095061 Paper 24056041 Paper 24048029 Paper 24039739 Paper 24030827 Paper 23999292 Paper 23989139 Paper 23980151 Paper 23937054 Paper 23936628 Paper 23919482 Paper 23891289 Paper 23879525 Paper 23861496 Paper 23808589 Paper 23795296 Paper 23781103 Paper 23713611

Abstract

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.

View original record on NIH RePORTER →