Events
Date 01 Dec 2023
Time 5:00 pm - 6:00 pm (HKT)
Venue Lecture theatre T3, Ming Wah Complex
Speaker Prof. Fraser Armstrong
Institution Emeritus Research Fellow of St John’s College, University of Oxford

Self Photos / Files - 20231201_Protein film electrochemistry – an overview of advances inTitle:

Protein film electrochemistry – an overview of advances in bioinorganic chemistry, biocatalysis and fundamental enzymology

 

Schedule:

Date: 1st December, 2023 (Friday)

Time: 5 - 6 pm (HKT)

 

Venue: Lecture Theatre T3, Ming Wah Complex

 

Speaker:

Prof. Fraser Armstrong

Emeritus Research Fellow of St John’s College

University of Oxford

 

Biography:

Fraser Armstrong received his PhD from Leeds University in 1975. In 1983 he become one of the first Royal Society University Research Fellows. In 1989 he moved to the University of California, Irvine where he remained until taking up a position at Oxford in 1993 where he remains as Emeritus Research Fellow of St John’s College. He has led a group that has developed Protein Film Electrochemistry, a powerful suite of techniques for unravelling the complex world of electron transfer and redox-based processes in biology. He is also co-author of a leading international textbook on Inorganic Chemistry.He was elected a Fellow of the Royal Society in 2008. His awards include the Eurobic Medal (1998), the Joseph Chatt Medal (2010), The Barker Medal (2012), the Davy Medal (2012), the Earnest Swift Lectureship (Caltech, 2014), the Bailar Medal and Lectureship (Univ. Illinois,2015), the Glenn Seaborg Lectureship (UC Berkeley, 2022). He is currently the Mok Hing-Yiu Distinguished Visiting Professor in Chemistry at HKU.

 

Abstract:

For over 30 years, protein film electrochemistry (PFE), a powerful suite of dynamic electrochemical techniques, has been used to investigate and reveal the properties of proteins containing redox cofactors, ranging from small electron-transferring metalloproteins to some of the most complex enzymes known. Important insight has been gained into the bioinorganic chemistry of Fe, Cu and Ni. Despite their giant nature (where electron tunnelling was once believed to be an insurmountable challenge) many enzymes are now recognised as the most efficient electrocatalysts known; moreover, the ‘overpotential’, a term familiar to all electrochemists, would have been a driver in early evolution. By using an electrode featuring a conductive nanoporous network, multiple enzymes of a cascade can be trapped, resulting in the ‘electrochemical Leaf’ (e-Leaf). Here, local NAD(P)(H) recycling, driven electrochemically by a flavoenzyme, is used to drive and control biocatalysis by enzymes of all major classes, all from a laptop keyboard. Highlights along the path leading us into ‘cascade-tronics’ will be outlined.

 

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