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Appears in Collections:Biological and Environmental Sciences Journal Articles
Peer Review Status: Refereed
Title: Hemocyanin conformational changes associated with SDS-induced phenol oxidase activation
Author(s): Baird, Sharon
Kelly, Sharon M
Price, Nicholas C
Jaenicke, Elmar
Meesters, Christian
Nillius, Dorothea
Decker, Heinz
Nairn, Jacqueline
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Keywords: Hemocyanin
Biochemistry Research
Issue Date: Nov-2007
Date Deposited: 23-Feb-2009
Citation: Baird S, Kelly SM, Price NC, Jaenicke E, Meesters C, Nillius D, Decker H & Nairn J (2007) Hemocyanin conformational changes associated with SDS-induced phenol oxidase activation. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1774 (11), pp. 1380-1394.;
Abstract: The enzymatic activity of phenoloxidase is assayed routinely in the presence of SDS. Similar assay conditions elicit phenoloxidase activity in another type 3 copper protein, namely hemocyanin, which normally functions as an oxygen carrier. The nature of the conformational changes induced in type 3 copper proteins by the denaturant SDS is unknown. This comparative study demonstrates that arthropod hemocyanins can be converted from being an oxygen carrier to a form which exhibits phenoloxidase activity by incubation with SDS, with accompanying changes in secondary and tertiary structure. Structural characterisation, using various biophysical methods, suggests that the micellar form of SDS is required to induce optimal conformational transitions in the protein which may result in opening a channel to the di-copper centre allowing bulky phenolic substrates access to the catalytic site.
DOI Link: 10.1016/j.bbapap.2007.08.019
Rights: Published in Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics by Elsevier.

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