Over the past two decades, 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. 35+ 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.

I was awarded a Royal Society University Fellowship “Investigating Photosynthetic Complexes” in late 2001. This was gratefully extended to 2012 due to medical circumstances (I have been 0.5/0.65 FTE since 2008). My 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 often observed in light-sensitive samples. This resulted in an output of over 25 primary papers, but further to this, 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 at that time, I noted for two years; with diffraction spots out to 1.1 Å). Other projects have used Atomic Force Microscopy to investigate molecular dynamics within membranes. I have contributed to/designed 8 front covers of books and journals.

During the earliest stages of my career, I was fortunate to isolate the first ever membrane-bound “photosynthetic supercomplex” (PNAS, 1995) whilst working in the laboratory of Professor James Barber at Imperial College, together with Ben Hankamer (now Professor, University of Queensland, Australia). This has opened up a large field of international investigation. At that time, for my Ph.D. studies, I probed this (relatively huge, 33 nm diameter, elongated >1.2 megaDalton) PSII-LHCII supercomplex using 14 biochemical/biophysical techniques, gaining a Ph.D. in 1997, then followed this by its structural elucidation to 17 Å via TEM during two post-doctoral positions (refs: Nature/Nature Structural Biology). The use at that time of (relatively novel) 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 cryo-TEM and 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 (01/2005 to 12/2009; www.rsc.org/pps). I have aided in the revision of the IBID (Biology) 3rd ed. textbooks for the International Baccalaureate (2014). I have been, concurrently, Staff Representative on Faculty and GM-safety committees, as well as organising a seminar series (26 lectures in 18 months), while sitting on Departmental IT provision committees. For the past five years, these skills have turned to being the Careers Liaison Officer for my School's (Department's) biology-degree students (1,650+ individuals) and a management committee member for QMUL's NanoVision TEM/SEM Centre (on the Mile End campus, E1 4NS, London, UK).

Funding has been gratefully received from The Royal Society, BBSRC/UK government and Japan's JST/CREST initiative.

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.