Over the past decade, co-authored discoveries of novel, photosynthetically active, protein macromolecular structures (20 to 40 nm in size) have been elucidated by the structural biology techniques of Transmission Electron Microscopy (TEM) and single particle analysis. This body of work has resulted in primary publications in Nature (3), Proceedings of the National Academy of Sciences USA (2), The Plant Cell (2), The Plant Journal and over 40 others in leading journals. More than 30 invited talks have been presented internationally and nationally. The protein structures observed involve a central photosystem ‘reaction centre’ coupled to peripheral light-harvesting components. These are now termed in the literature “photosynthetic supercomplexes”. It is anticipated that renewable energy technologies, such as those involving solar capture and biohydrogen, will benefit from this knowledge of nature.

A Royal Society University Fellowship “Investigating Photosynthetic Complexes” was awarded in late 2001. This was (gratefully) serially extended to 2012 due to medical circumstances (I have been 0.5/0.65 FTE since 2008). The Fellowship’s central remit was to probe more evolutionarily diverse organisms and mutants for light-harvesting photosynthetic proteins, and to drive forward a combinatorial approach of TEM and computer purification to overcome the structural heterogeneity that is often observed in light-sensitive samples. Separate structural breakthroughs were made for proteins involved in bacterial pathogenesis, PspA, and for antibiotic resistance, the emrAB complex. Photosystem assembly (Ycf4 protein; ref: The Plant Cell, 2009) and red algal light harvesting (Lhcr proteins) were also reported upon. X-ray diffraction was used to probe a cyanobacterial light-harvesting protein, subsequently elucidated to a resolution of 1.45 Å in 2003 (the most highly resolved light harvesting protein; for two years). Other projects used Atomic Force Microscopy to investigate molecular dynamics within membranes. I have contributed/designed to 7 invited front covers of books and journals.

During the earliest stages of my career, the first ever membrane-bound “photosynthetic supercomplex” was isolated whilst in the laboratory of Professor James Barber at Imperial College (PNAS, 1995). This has opened up a large field of international investigation. At that time I probed it with 14 biochemical/biophysical techniques to gain a Ph.D., followed by TEM during two post-doctoral positions (refs: Nature/Nature Structural Biology). The use of vitrified samples permitted 3D structures to be calculated from a number of organisms (cyanobacteria, green algae and a diverse range of niche organisms and their mutants) by single particle image analysis (17-20 Å resolution).

The lab engages in many national/international collaborations with emphasis now on the mechanisms and complexes that assemble, repair and regulate these membrane proteins in the first instance, including the first 3D reconstruction of the PSII-affecting protease FtsH (ref: The Plant Cell, 2012). Visiting researchers and/or Ph.D. students are welcome to contact the lab.

I referee publications for many journals, both specialist and well known, for the scientific community. I was an Associate Editor of Photochemical & Photobiological Sciences (2005-2009; www.rsc.org/pps). I have aided in the revision of the IBID (Biology) 3rd ed. textbook for the International Baccalaureate (2014). He has been, concurrently, Staff Representative on Faculty and GM-safety committees, as well as organising a seminar series (26 lectures in 18 months). He has sat on a Departmental IT provision committee.
Funding has been from The Royal Society, BBSRC/UK government and Japan's JST/CREST initiative, for which I am very grateful.

All original scientific content within this website is copyright of myself, the relevant authors, institutions and/or the journals that it is published in, as indicated.