Prof. Hagan Bayley.
Awards and Fellowships
Nature utilizes oxidoreductases to cater for its energy needs in respiratory processes.Oxidoreductases are enzymes that catalyze redox reactions relevant to the normal functioning of cell. The active sites of oxidoreductases usually contain transition metal ions and organic cofactors. Amino acid residues in the primary and secondary coordination sphere modulate the redox potential of the metal ions to carry out specific reactions. A recurring theme of the research on redox enzymes is to understand electron/proton transfer processes. Substantial efforts have been made to understand how the insulating protein matrix is capable of conducting electrons/redox equivalents on the ms–μs timescale within (and in between) these enzymes and proteins. The sophisticated experimentation combined with the development of electron-transfer theory has taught us a lot about certain enzyme systems. However, it is important to admit that we are still not able to engineer biomimetic systems which can perform similar tasks in a predictable manner.
The AG group will focus on applying novel single-molecule and ensemble techniques to study electron-transfer and catalysis during enzyme turnover which will be complementary to the customary single-turnover or pre-steady-state kinetics methods to yield a complete picture about catalysis. Further, the group will study transmembrane and interfacial electron-transfer processes which are essential to trap the electrochemical gradient generated by these proteins to perform some external work. This knowledge will be further utilized to engineer proteins for the purpose of harnessing solar energy to drive redox reactions of interest to the industry and society.