Stellacyanin is a small blue copper protein of unknown biological function. It contains a copper binding domain at the amino terminus which creates a noticeable blue color upon the addition of copper. We propose to study the electrochemistry of copper bound up by the protein. Stellacyanin is ideal for this purpose as it interacts with electrodes without intermediates and has its copper binding domain located at a terminus where it can be easily modified. We will alter the binding domain by the addition of bases to the gene that codes for the protein. This should create a weaker bond to copper and give measurable electrochemical effects
University of Minnesota M.S. thesis. July 2010. Major: Chemistry. Advisor: Dr. Steven M. Berry. 1 co...
Direct electrochemistry of a series of blue copper proteins: azurin, pseudoazurin, umecyanin, stella...
The metal sites of electron transfer proteins are tuned for function. The type 1 copper site is one ...
Stellacyanin is a blue copper-binding protein of unknown biological function. We propose to combine ...
It is conceivable that eukaryotes posses DNA proof-reading proteins that sense the difference in con...
It has been observed in azurin [1], plastocyanin, and stellacyanin (unpublished work) that a redox p...
Cofactors extend the chemistry of life. Redox reactions in photosynthesis, nitrogen fixation, and ot...
The cupredoxin domain of a putative type 1 blue copper protein (BCB) from Arabidopsis thaliana was o...
Detailed electronic and geometric structural descriptions of the blue copper sites in wild-type (WT)...
Azurin belongs to a family of small blue copper proteins or cupredoxins which participate in electro...
Blue Copper Binding (BCB) Proteins are an important family of proteins found in every kingdom of lif...
Blue copper binding proteins are prevalent in all forms of life, yet most of them have not been func...
Stellacyanin is a mucoprotein of molecular weight approximately 20,000 containing one copper atom in...
International audienceBlue copper proteins have a constrained Cu(II) geometry that has proven diffic...
Blue copper proteins are type-I copper containing redox proteins whose role is to shuttle electrons ...
University of Minnesota M.S. thesis. July 2010. Major: Chemistry. Advisor: Dr. Steven M. Berry. 1 co...
Direct electrochemistry of a series of blue copper proteins: azurin, pseudoazurin, umecyanin, stella...
The metal sites of electron transfer proteins are tuned for function. The type 1 copper site is one ...
Stellacyanin is a blue copper-binding protein of unknown biological function. We propose to combine ...
It is conceivable that eukaryotes posses DNA proof-reading proteins that sense the difference in con...
It has been observed in azurin [1], plastocyanin, and stellacyanin (unpublished work) that a redox p...
Cofactors extend the chemistry of life. Redox reactions in photosynthesis, nitrogen fixation, and ot...
The cupredoxin domain of a putative type 1 blue copper protein (BCB) from Arabidopsis thaliana was o...
Detailed electronic and geometric structural descriptions of the blue copper sites in wild-type (WT)...
Azurin belongs to a family of small blue copper proteins or cupredoxins which participate in electro...
Blue Copper Binding (BCB) Proteins are an important family of proteins found in every kingdom of lif...
Blue copper binding proteins are prevalent in all forms of life, yet most of them have not been func...
Stellacyanin is a mucoprotein of molecular weight approximately 20,000 containing one copper atom in...
International audienceBlue copper proteins have a constrained Cu(II) geometry that has proven diffic...
Blue copper proteins are type-I copper containing redox proteins whose role is to shuttle electrons ...
University of Minnesota M.S. thesis. July 2010. Major: Chemistry. Advisor: Dr. Steven M. Berry. 1 co...
Direct electrochemistry of a series of blue copper proteins: azurin, pseudoazurin, umecyanin, stella...
The metal sites of electron transfer proteins are tuned for function. The type 1 copper site is one ...