Biosciences News and Events Publication

Obituary: Professor Barbara Banks

21 July 2014

Professor Barbara Banks (24th February 1934 to 10 June 2014) was a staff member in the UCL Chemistry and Physiology Departments until 1999 when she retired as Emeritus Professor of Physiological Chemistry. 

Her obituary, written by Shawn Doonan is posted below.

Professor Barbara Banks PhD, DSc, FRSC

Barbara Banks, born 24th of February 1934, died on the 10th of June 2014. Barbara was a Lancastrian by birth and read chemistry at Royal Holloway College before starting a life-long association with UCL by taking an MSc in biochemistry. Barbara then worked for a PhD under the supervision of Charles Vernon who had recently turned his attention to the mechanism of action of enzymes. Barbara was given the job of purifying the enzyme aspartate aminotransferase which was no mean task given the primitive methods available for protein purification at that time. She then carried out a detailed investigation of the kinetics of the enzyme-catalysed reaction and on the basis of that work was awarded the Ramsay Medal for the session 1961/62.

Barbara continued working on aspartate aminotransferase as a post-doctoral fellow. This is a particularly interesting enzyme because its action requires a bound cofactor, pyridoxal 5’-phosphate, which is itself capable of catalysing the reactions of transamination. By combining kinetic studies of the cofactor-catalysed reaction with some very cunning studies carried out by Tony Lawrence of the enzyme-catalysed reaction using deuterated substrates it was possible to show that the rate enhancements due to the protein part of the enzyme on the rate-limiting steps of the process were of the order of 107 to 109-fold. This was the first time that the catalytic power of an enzyme was put onto a quantitative footing. At that time (the mid-sixties) the first three-dimensional structures of enzymes were determined and it became possible to make conjectures about the physical and chemical bases of their catalytic effects. Barbara co-authored a review on the topic along with Charles Vernon and myself in Progress in Biophysics and Molecular Biology (1970, 20, 247-327) the ideas expressed in which are still largely valid today.

Around this time Barbara was appointed to a lectureship in the Department of Physiology in UCL but still retained links with the Department of Chemistry and in particular with Charles Vernon whom she subsequently married. This collaboration was focused on work at the boundaries of chemistry and biology. One such project involved studies of the structure and function of nerve growth factor, NGF, a molecule critical for the survival and maintenance of sympathetic and sensory neurons. Other work concerned the anti-inflammatory activity of peptide 401 from bee venom and the relationship between this activity and the ability of the peptide to degranulate mast cells.

Apart from these experimental research activities Barbara had a long-standing interest in the misuse by biochemists and biologist of the concepts of free energy changes in biological systems, and in particular about the role of the molecule adenosine 5’-triphosphate (ATP). This molecule is often referred to as ‘high energy phosphate’ on the grounds of its relatively high standard free energy of hydrolysis. The idea had gained ground that the ATP produced during the exergonic reactions of catabolism (degradation of foodstuffs) ‘stored’ this energy, and that energy subsequently liberated by its hydrolysis then ‘drove’ the endergonic reactions of biosynthesis and other processes such as muscular contraction. This wholly mistaken idea served to draw attention away from the true role of ATP as providing a chemical, as opposed to an energetic, link between the processes of catabolism and anabolism. The most detailed criticism of the traditional view was given by Barbara and Charles Vernon in a paper in the Journal of Theoretical Biology (1970, 29, 301-326). In spite of the force of the arguments made in this and other related papers it is regrettable that misconceptions about the role of ATP persist. For example, the Wikipedia entry for ATP still contains statements such as “ATP is consumed in the cell by energy-requiring (endothermic) processes and can be generated by energy-releasing (exothermic) processes. In this way ATP transfers energy between spatially separate metabolic reactions.” Despite this, Barbara’s analysis of the role of ATP in biological processes must still be seen as a major contribution to knowledge. For this and her other scientific work Barbara was awarded a DSc and was promoted to a personal chair of Physiological Chemistry in the Department of Physiology.

Barbara made many other contributions to the life of UCL. She was a fine teacher and much appreciated as a tutor to medical students. She also had a strong interest in the promotion of opportunities in science for women; this she pursued through work with the AUT and also by her involvement in the establishment of a crèche in the college. She was an active member of the Science Society and a contributor to the general intellectual life of UCL. In recognition of these contributions and of her scientific work she was elected as Honorary Fellow of UCL in 1991. In 1994 she instituted the Charles Vernon Prize in memory of her husband.

Shawn Doonan

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