Prestigious Award for University Chemist.
Dr. Michael Blackburn was awarded the International Arbusovs Prize at the Butlerov 150th Anniversary Congress in Kazan, sponsored by the Russian Academy of Science.
Kazan is historically a unique city connecting East and West. In 1804 the third University in Russia was established there, and its alumni include Tolstoy and Lenin. The element ruthenium was discovered there, and thiscity has been described as “the cradle of Russian organic chemistry”. Most notably, Vladimir Markovnikov, Alexander Arbuzov (father), and Boris Arbuzov (son) established a golden era for organic chemistry in Kazan.
The International Arbuzovs Award was created in 1997 to commemorate the great achievements of the two Arbuzovs. It is awarded every two years by the President of the Republic of Tatarstan, now Rustam Minnikhanov, to an outstanding chemist who has made significant international contributions to phosphorus chemistry, this year being the first award to a British chemist.
The presentation ceremony took place in the Concert Great Hall of KazanUniversity on September 19th. The award of the Medal and Certificate to Professor Blackburn was made by the Prime Minister of Tatarstan, Ildar Khalikov (see photo) in the unavoidable absence of the President. His Laureate Lecture was delivered at the close of the Butlerov Congress in the presence of distinguished guests including many international chemists celebrating the sesquicentenary of Alexander Butlerov’s theory of the chemical structure of organic compounds.
Professor Blackburn graduated from Cambridge University, did his Ph.D. studies on Vitamin B12 in Nottingham, and returned to Cambridge as a Rockefeller Fellow and University Demonstrator in Organic Chemistry.
Working with Lord Todd, he was initiated into phosphorus chemistry and the synthesis of nucleic acids just 50 years ago. Collaborations within the youthful Cambridge Laboratory for Molecular Biology led to his use of carrier-free 32P-phosphate to establish the role of puromycin in ribosomal peptide synthesis, to the structure of thymine photodimer in bacteria, and to the mechanism of phosphate diester formation by the reagents then used for oligonucleotide synthesis. He became an active member of the international phosphorus community, beginning with the Georg Wittig Symposium in Heidelberg in 1964 and culminating in his organizational role in the 16th ICPC Meeting in Birmingham in 2004.
Moving to Sheffield University in 1965, Mike Blackburn bridged thegap between the chemistry and biochemistry departments, using chemical synthesis and reaction kinetics to explore phosphoryl transfer processes catalysed by a range of enzymes, including kinases and mutases. His quantitative analysis of the relatively disappointing performance of methylenephosphonates as stable analogues of biological phosphate esters stimulated his novel proposal to introduce fluorine onto the proximate carbon as an a-fluorophosphonate, thereby bringing the properties of the phosphonate group into closer alignment with those of the parent phosphate ester. That signature called for the invention of new methods for the synthesis of both a-fluoro- and a,a-difluorophosphonates, initially involving very hazardous reagents, and over the last 25 years has become an internationally-used device across many areas of chemical biology, particularly in nucleotides and phosphopeptides, where some 500 publications now describe its deployment. In his own work, Mike Blackburn focused on its application to the master nucleotide, adenosine triphosphate (ATP) and its relatives and their use by receptors and enzymes such as kinases, polymerases, and mutases. Through the 90’s, those studies produced structural and quantitative analyses of a variety of phosphoryl transfer processes but the very nature of stable, ground state analogues precluded the analysis of transition states for enzyme mechanisms. That problem was made more acute by investigations into catalytic antibodies that were finally frustrated by the limitations of the Periodic Table precluding delivery of stable analogues of transition states for phosphoryl transfer reactions.
Mike therefore turned to the burgeoning deployment of metal fluorides capable of forming stable transition state complexes with a range of kinases, mutases, and phosphatases. Juxtaposing protein crystallography and 19F NMR spectroscopy to deliver accurate, and sometimes critical, analyses of these complexes, he has rationalized major features of enzymatic phosphoryl transfer in terms of the “anionic shield” of phosphate esters and “charge balance” as a hypothesis explaining how enzymes respond to it. These studies are now demonstrating the relative simplicity of enzyme catalysis of kinases, phosphatases, and mutases even though these processes include some of the most remarkable accelerations of any enzymatic reactions. In conclusion, these investigations lead to the conclusion that phosphorus is the unique element whose oxyacids are capable of fulfilling the multiple roles of phosphate esters in terrestrial life and fully justify Lord Todd’s 1981 prediction that phosphorus (sic) will play the same roles in life wherever it is found in the universe.