Imperial College London

Professor Bill Rutherford FRS

Faculty of Natural SciencesDepartment of Life Sciences

Chair in Biochemistry of Solar Energy
 
 
 
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Contact

 

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

 
 
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Location

 

702Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Summary

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.

Publications

Journals

Murray JW, Rutherford AW, Nixon PJ, 2020, Photosystem II in a State of Disassembly, Joule, ISSN:2542-4351

Judd M, Morton J, Nurnberg D, et al., 2020, The primary donor of far-red photosystem II: Chl(D1) or P-D2?, Biochimica Et Biophysica Acta-bioenergetics, Vol:1861, ISSN:0005-2728

Babacan O, De Causmaecker S, Gambhir A, et al., 2020, Assessing the feasibility of carbon dioxide mitigation options in terms of energy usage, Nature Energy, Vol:5, ISSN:2058-7546, Pages:720-728

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, Vol:117, ISSN:0027-8424, Pages:1-7

Shevela D, Do H-N, Fantuzzi A, et al., 2020, Bicarbonate-Mediated CO2 Formation on Both Sides of Photosystem II., Biochemistry, Vol:59, ISSN:0006-2960, Pages:2442-2449

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