The Biochemical Society Award for Significant Breakthrough or Achievement will be presented to Dr Zhao-Qing Luo in 2025. Zhao-Qing is a professor at the Department of Biological Sciences, Purdue University. His research focuses on biochemical basis of bacterial infection using Legionella pneumophila as a model. One hallmark of L. pneumophila pathogenicity is its hundreds of virulence factors that function to modulate host processes to create an intracellular niche permissive for bacterial growth. His group has contributed significantly not only the identification but also functional characterization of many of these factors by revealing their unique biochemical activities and targets within host cells. He identified enzymes that catalyze reversible AMPylation and phosphorylcholination to regulate Rab1, a key signaling protein involved in vesicle trafficking. More notably, his group discovered a ubiquitination mechanism in which ubiquitin is activated by ADP-ribosylation using NAD as the energy source. These reactions are chemically distinct from the canonical three-enzyme cascade powered by ATP. He also found that these bacterial ubiquitin ligases are regulated by glutamylation catalyzed by pseudokinase-induced protein AMPylation. Work from the Luo group has revealed host function modulation by a wide variety of protein posttranslational modifications catalyzed by bacterial virulence factors, which have greatly expanded our understanding of cell signaling and the biochemical mechanisms underlying such modifications.

Zhao-Qing said: “I feel thrilled to be recognized by the prestigious Award from the Biochemical Society. It is a great honor for myself and for the many outstanding people with whom I have been fortunate to work with over the years. It reminds me of the many moments when we gained a glimpse of the activity of these cryptic proteins often after years of pursuit. I wish to thank my mentors at different stages of my career, my department, Purdue University, the funding agencies and my family for the support that enables my research."

The Biochemical Society Award for Sustained Excellence will be presented to Professor Robert Cross in 2025. Rob is a molecular motors enthusiast. Motors are fundamental to eukaryotic life, because they allow cells to self-organise. How molecular motors work has fascinated him all his working life.

Rob obtained his PhD in 1983 from the University of Nottingham and then won an EMBO long-term fellowship to work with J. Victor Small and Apolinary Sobieszek in Salzburg on the structure and mechanisms of smooth muscle myosin filaments. In 1986, he moved to MRC-LMB as an MDA fellow and alongside John Kendrick Jones, Clive Bagshaw and Mike Geeves, Rob was ultimately able to propose an explicit mechanism for myosin II self-assembly.

In 1991, he moved to the Marie Curie Research Institute (MCRI) and began work on kinesin, then newly-discovered. In 2005, Rob and Nick Carter found that kinesin can step processively backwards under load. This turned out to be key to its mechanochemical coupling, which, as they recently (2020) showed, combines tight-coupled forwards steps with loose-coupled backslips.

In 2009, the MCRI closed and Rob moved, with his friends Andrew McAinsh and Anne Straube, to the University of Warwick. At Warwick, Rob continues to interrogate the kinesin mechanism, but with an important paradigm shift, whereby the interlock between the mechanochemical mechanisms of kinesin and tubulin is paramount.

Rob said: "The Biochemical Society is a national treasure and I am grateful for this recognition of my work. I like the idea of an award for sustained progress - for me, science is about finding a good problem, splitting it into smaller problems, and working to solve those, as best one can, for as long as it takes."

The Biochemical Society Award for Significant Breakthrough or Achievement will be presented to Professor Cees Dekker in 2026. Cees is a Distinguished University Professor at TU Delft. Trained as a physicist, he pioneered nanotechnology with many discoveries on carbon nanotubes in the 1990s. Since 2000, he moved to single-molecule biophysics and nanobiology.

Dekker is an elected member of the Royal Netherlands Academy of Arts and Sciences (KNAW) and fellow to the American Physical Society (APS) and the Institute of Physics (IOP). Dekker was Director of the prestigious Kavli Institute of Nanoscience Delft, initiated an entirely new Department of Bionanoscience at Delft, and leads large national research consortia. He received an honorary doctorate and many prizes such as the 2001 Agilent Europhysics Prize, 2003 Spinoza Prize, 2012 ISNSCE Nanoscience Prize, 2017 NANOSMAT Prize, 2021 Nano Research Award, and the 2024 Sackler Prize. Dekker was knighted as Knight in the Order of the Netherlands Lion, and he received ERC Advanced Grants in 2009, 2015 and 2020. Dekker published over 400 peer-reviewed papers that got cited >90.000 times (H-index 128).

His current research focuses on (i) nanopores for protein sequencing; (ii) chromosome structure, in particular SMC motor proteins; and (iii) building a living synthetic cell from lifeless molecules. On the latter subject, he initiated efforts to build a synthetic cell from the bottom up already 2 decades ago. He was one of the pioneers triggering the Dutch BaSyC consortium and the European Synthetic Cell Initiative, and currently leads the large (46M€) Dutch consortium EVOLF. His lab’s research on synthetic cells ranges from facilitating microfluidics lab-on-a-chip technology for generating liposomes, to biophysical studies of synthetic cell division, to synthetic genomes.

Cees said: “I am really greatly honoured by this 2026 Award from the Biochemical Society. It is wonderful that they acknowledge our contributions to nanobiology and single-molecule biophysics in this way, and it is a further motivation to continue this research in the forthcoming years.”

The Biochemical Society Award for Sustained Excellence will be presented to Professor Christine Foyer in 2026. Christine is a Professor of Plant Sciences at the University of Birmingham, a Member of the Environmental Sustainability Board of the FERRERO group and the Editor in Chief of Plant, Cell and Environment. She has over 480 published papers and ranked as a Highly Cited Researcher™ list from Clarivate™. She is listed in the 2023 Edition of the Ranking of Top 1000 Female Scientists in the World. Ranked 15 in United Kingdom, and 192 in the world. She is ranked 7th in the list of the world's Best Scientists in Plant Sciences. Christine is an expert in plant biochemistry and metabolism. With a strong focus on reduction/oxidation (redox) processes and signals that regulate plant growth and stress tolerance, her lab studies how primary processes such as photosynthesis regulate plant, growth development and defence, particularly through effects on the redox status of cells and cell signalling under optimal and stress conditions. Using model (Arabidopsis), crop plants and trees, her lab investigates the responses of photosynthesis and associated processes to abiotic stresses including elevated carbon dioxide.

Christine said: "I am honoured and delighted to receive this award, which means a great deal to me, not least because I undertook my PhD in the Department of Biochemistry in Kings College at the University of London. While the Department of Biochemistry evolved into a new structure long ago, I have remained a biochemist at heart and I encourage early stage researchers to continue to embrace this important topic, which remains a fundamental basis for understanding cell functions.”

The 2023 Centenary Award was presented to Professor Matthias Hentze. Matthias is the Director of the European Molecular Biology Laboratory (EMBL) and Co-Director of the Molecular Medicine Partnership Unit (MMPU). Following medical training in Germany and the UK, he codiscovered “iron-responsive elements” as the first mammalian regulatory elements in mature mRNAs during his postdoctoral research at NIH. After two decades of elucidating mechanisms of RNA regulation by RNA binding proteins, the Hentze group recently uncovered hundreds of new RNA-binding proteins, including many metabolic enzymes. Their current work focuses on riboregulation in metabolism and cell biology.

Matthias is a co-founder of the MMPU, an interdisciplinary and translational research unit between EMBL and Heidelberg University. His work has been widely recognized, including Germany’s most prestigious Gottfried Wilhelm Leibniz Prize and the Lifetime Achievement Award of the RNA Society. He is an elected member of the European Molecular Biology Organisation, the German Academy of Sciences Leopoldina, the Academia Europaea, the Australian Academy of Science, and the American Academy of Arts and Sciences. Matthias serves on numerous scientific advisory and editorial boards, and in 2020 initiated the Environmental Research Initiative and Fund.

Matthias says: “I feel deeply honoured to receive this prestigious award which I want to share with the many outstanding team members whom I had the pleasure to mentor. RNA science holds so many more exciting secrets and I hope that the award helps to draw attention to this.” 

Matthias presented his Award lecture at RNA Granules on 10 October 2023.

The 2020 Centenary Award was presented to Professor Dame Kay E Davies of the University of Oxford, UK.

Kay completed her D.Phil studies at the Department of Biochemistry, University of Oxford. After a Royal Society Fellowship in France she moved back to St Mary’s Hospital Medical School to study Duchenne muscular dystrophy (DMD), a progressive muscle wasting disease. In 1984, as a MRC Senior Fellow, she moved back to Oxford to work on the molecular analysis of neurological disorders. She was appointed Professor of Genetics and then Dr Lee’s Professor of Anatomy and set up the MRC Functional Genomics Unit to apply genomics to genetic disease analysis. Her own group focuses on the development of therapeutic strategies for DMD. Kay’s earlier work paved the way for the use of mini dystrophin gene delivery using AAV and contributed to the exon skipping approach to therapy. She also discovered the dystrophin related protein, utrophin, and demonstrated that increased levels of utrophin can compensate for the lack of dystrophin in the mdx mouse model of the disease. This has led to the identification of small molecules which increase utrophin in adult mdx muscle and prevent pathology. Kay co-founded Summit Therapeutics to translate her work into the clinic. She is a founding fellow of the UK Academy of Medical Sciences and was elected a Fellow of the Royal Society in 2003. She was a Governor of the Wellcome Trust from 2008-17 and Deputy Chairman from 2013-2017. Kay was made Dame Commander of the British Empire for services to science in 2008.

Kay said: “I am very honoured and delighted to have my work recognised in this way by the Biochemical Society. I am also very grateful to all the talented researchers I have had the privilege to work with over the years.”

Kay presented her Award lecture on Wednesday 29 July 2020 as part of the Biochemistry Focus webinar series. View the recording.

The 2019 Centenary Award was presented to R. John Ellis from the University of Warwick, UK. John has made fundamental discoveries through the study of the mechanism of protein folding essential for light harvesting and photosynthesis. His work focused on the pathway by which the key enzyme of photosynthesis (RUBISCO) – the most abundant protein on earth – is made and assembled in plant cells. From this specific case, John developed key concepts which have revolutionized thinking about how proteins assemble and fold in all cells. John termed these other proteins that assist in protein folding and assembly ‘molecular chaperones’ and his key insight showed that these chaperones are not restricted to the protein assembly pathway that he studied, but exist universally in all cells.

The 2018 Centenary Award was presented to Professor Frank McCormick from the University of California San Francisco Helen Diller Family Comprehensive Cancer Center. Frank has been a leader in the field of RAS oncogene function and regulation for over 30 years, having made a large number of seminal discoveries about the signalling pathway regulated by the RAS protein. His identification of RAS GAP marked the start of the rush to understand the regulation of RAS proteins and their normal role within the cell. With the identification of the NF1 protein as a member of the GAP family this led to fundamental understanding of Neurofibromatosis type I. Frank has also contributed very important observations about the downstream pathways regulated by RAS, including the RAF/MAPK pathway and PI3K signaling. Frank has also been hugely influential outside of his own lab, he founded ONYX Pharmaceuticals, a company dedicated to developing new cancer therapies. In addition to all this, Frank has also been President of the AACR and made many other contributions to the cancer research community at the highest level. 

Of winning the Centenary Award, Frank said “I am absolutely thrilled to receive this award.  It means a great deal to me to be recognized by my peers, especially as I was trained as a biochemist in the UK and attended many outstanding Biochemical Society meetings in which I made connections and gained new insights that have affected my entire career.”

Read his review article 'Progress in targeting RAS with small molecule drugs' published in the Biochemical Journal. 

The 2016 Centenary Award was presented to Patrick Cramer from Max Planck Institute for Biophysical Chemistry, Germany.  The award is made in recognition of Patrick’s successful systems biology approach to uncovering the importance of and mechanisms in transcriptome surveillance and RNA degradation in the balanced production of mRNAs.  Furthermore, two important crystal structures were published in 2013.

Patrick Cramer received his award at the 80th Harden Conference: Machines on Genes IV – Mechanisms of Actions of Large Macromolecular Machines on Genes Across Biological Scales at Shrigley Hall Hotel, Macclesfield, UK, 31 July—4 August 2016.

Read his review article published in Biochemical Society Transactions here: Structure determination of transient transcription complexes.