Mechanistic studies and properties of galactose oxidase

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Project objective

Research objectives and content Galactose Oxidase is a single copper enzyme from the Canadian woodrot fungus Fusarium dendroides. It oxidises/degrades primary alcohol, sugar/polysaccharide substrates to aldehydes, and is re-oxidised by oxygen with release of hydrogen peroxide. The structure has recently been determined and mechanistic studies are timely. To better understand substrate binding to copper, reactions with azide, thiocyanate and phenols will be studied. The copper will be replaced by other metals enabling the second redox component (a tyrosyl radical) and other features to be studied in what is a unique active site. Interesting thermochromic changes for Galactose Oxidase, an auto-redox interconversion taking 3h, the determination of reduction potentials by direct electrochemistry, and reduction of Galactose Oxidase with phenylhydrazine will also be investigated. Training content (objective. benefit and expected impact) Previous research has been in generating and studying phenol ate radicals in metal complexes as models for enzymes. There have been no opportunities to work on enzymes. Professor Sykes' group has extensive experience with metalloproteins, Galactose Oxidase being a recent additional interest. This is an excellent opportunity to gain experience isolating and handling a free-radical containing enzyme in an important developing research area. Links with industry / industrial relevance (22) Professor Sykes' group has Ph.D. student support/collaborations with Unilever Research for work on Galactose Oxidase.

Original text from CORDIS.

Participants

• UNIVERSITY OF NEWCASTLE UPON TYNE · NEWCASTLE UPON TYNECoordinatorUnited Kingdom
• Not availableCity levelGermany

Links

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