The work and contribution of fifteen eminent bioscientists, outstanding educators and exceptional early career researchers has been acknowledged in the annual Biochemical Society Awards following a record year of nominations.

Each recipient has been recognised for excellence in their field as well as a strong commitment to build, support, and nurture future talent. Winners of the 2025 Awards represent a cross-section of the molecular biosciences ranging from redox biology and plant-microbe interactions to mechanochemistry and virology.

Professor Steve Busby, Professor of Biochemistry at the University of Birmingham, and Chair of the Biochemical Society’s Awards Committee, says: "The list of the 2025 Biochemical Society award winners is impressive and, of course, we have a wonderful mix of awardees, since each prize is targeted to a different section of our community. This is due to great foresight by the Society’s managers and funders, over many many years. As well as congratulating the winners, I want to say thanks for all the hard work put in by nominators, supporters, Biochemical Society staff and the Awards Panel during the current round, this scheme could not work without you and your efforts made my job easy!”

Professor Cross 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."

Professor Cross 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 colleagues Professor Andrew McAinsh and Professor Anne Straube, to Warwick Medical School, 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.

Find out more about the Awards here and find out more about Professor Rob Cross and his research here.