The incorporation of nitrosocyanin copper binding loop into azurin.

Thumbnail Image

Persistent link to this item

View Statistics

Journal Title

Journal ISSN

Volume Title


The incorporation of nitrosocyanin copper binding loop into azurin.

Published Date




Thesis or Dissertation


Metalloprotein design and engineering can be used to probe our understanding of active site structure and function. Loop-directed mutagenesis has been used in the metalloprotein field to change the copper binding loops from a number of members of the cupredoxin family into other protein scaffolds. We report the replacement of a ten amino acid loop that supports the copper binding site in the blue copper protein azurin with the red copper binding loop from the protein nitrosocyanin. Azurin is an electron transfer protein while the role of nitrosocyanin is unknown, yet believed to be catalytic. In addition to the loop, we added a carboxylic acid residue into the copper binding site which fully models the site of nitrosocyanin. Synthesis, expression, and UV-visible absorption and EPR spectra for this series of azurin variants will be reported.


University of Minnesota M.S. thesis. July 2010. Major: Chemistry. Advisor: Dr. Steven M. Berry. 1 computer file (PDF); v, 56 pages. Ill. (some col.)

Related to



Series/Report Number

Funding information

Isbn identifier

Doi identifier

Previously Published Citation

Suggested citation

Schenewerk, Audrey Rose. (2010). The incorporation of nitrosocyanin copper binding loop into azurin.. Retrieved from the University Digital Conservancy,

Content distributed via the University Digital Conservancy may be subject to additional license and use restrictions applied by the depositor. By using these files, users agree to the Terms of Use. Materials in the UDC may contain content that is disturbing and/or harmful. For more information, please see our statement on harmful content in digital repositories.