Imperial College London

Professor Bill Rutherford FRS

Faculty of Natural SciencesDepartment of Life Sciences

Chair in Biochemistry of Solar Energy



+44 (0)20 7594 5329a.rutherford Website




702Sir Ernst Chain BuildingSouth Kensington Campus





My career aim is to understand the water oxidising enzyme Photosystem II in terms of its mechanism, its assembly and its evolutionary relationships with other photosynthetic reaction centres. This enzyme has become the focus of attention because cheap water splitting catalysts are urgently needed in the energy sector for solar fuel production, electrolysis of water and the reverse reaction in fuel cells. My research has made major contributions to understanding this enzyme before it was either popular or profitable. Now that it is finally becoming both of those, I hope to continue to do more of the same. Not just because it might contribute to solving aspects of the energy crisis but also because understanding the enzyme, which put the energy into the biosphere, the oxygen into the atmosphere and thence changed the planet, is one of the greatest challenges in biology and chemistry. It is also a fun enzyme to work on.



Zamzam N, Rakowski R, Kaucikas M, et al., 2020, Femtosecond visible transient absorption spectroscopy of chlorophyll f- containing Photosystem II, Proceedings of the National Academy of Sciences of Usa, ISSN:0027-8424

Sjodin M, Hjelm J, Rutherford AW, et al., 2020, Proton-coupled electron transfer from an interfacial phenol monolayer, Journal of Electroanalytical Chemistry, Vol:859, ISSN:1572-6657

Cardona Londono T, Rutherford AW, 2019, Evolution of photochemical reaction centres: more twists?, Trends in Plant Science, Vol:24, ISSN:1878-4372, Pages:1008-1021

De Causmaecker S, Douglass J, Fantuzzi A, et al., 2019, Energetics of the exchangeable quinone, QB, in Photosystem II, Proceedings of the National Academy of Sciences of Usa, Vol:116, ISSN:0027-8424, Pages:19458-19463

Varghese F, Kabasakal BV, Cotton CA, et al., 2019, A low-potential terminal oxidase associated with the iron-only nitrogenase from the nitrogen-fixing bacterium Azotobacter vinelandii, Journal of Biological Chemistry, Vol:294, ISSN:0021-9258, Pages:9367-9376

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