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Brian Selby Hartley (16 April 1926 – 3 May 2021) FRS was a British biochemist. He was Professor of Biochemistry at Imperial College London from 1974 to 1991.

Education

Hartley was educated at Queens' College, Cambridge graduating with a Bachelor of Arts in 1947 followed by a Master of Arts degree in 1952. He moved to the University of Leeds where he was awarded a PhD in 1952 for research supervised by Malcolm Dixon and Bernard A. Kilby.

Career and research

From 1952 to 1964, Hartley pioneered work on the sequence and mechanism of the enzyme chymotrypsin in Cambridge, and developed the use of paper chromatography to separate amino acids and peptides — an essential part of protein characterisation at that time. In 1965, he became a founding member of the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB), and collaborated with David Mervyn Blow in determining the structure and mechanism of chymotrypsin, as part of extensive work on chymotrypsin and related enzymes. His group also showed that mammalian serine proteases, including the blood clotting cascade, had homologous structures and mechanisms, indicating a common evolutionary origin. Hartley also studied other enzymes, such as aminoacyl tRNA synthetases (with Alan Fersht), xylose isomerase and glucose isomerase.

In 1974, Hartley became Head of the Department of Biochemistry at Imperial College London, converting it into a centre for molecular biology. In 1982, he conceived the need for a discipline – biotechnology – to exploit molecular biology breakthroughs. He left the Department of Biochemistry to set up Imperial's Centre for Biotechnology, and became a founding board member of Biogen – the longest surviving genetic engineering company. Since then, Hartley has founded companies to make cheap bioethanol from waste hemicellulosic biomass, using genetically engineered compost heap microorganisms.

Awards and honours

Hartley was elected a Fellow of the Royal Society (FRS) in 1971. His certificate of election reads:

Distinguished for his studies on the structure and mode of action of the proteolytic enzymes. In particular, he has determined the complete amino acid sequence of chymotrypsinogen, a protein of 253 residues, and has studied the relationship of this structure to enzymic activity. He has developed two important new techniques in protein chemistry: the "dansyl" methods for determining sequences in peptides on a very small scale, and the "diagonal" technique for studying the distribution of disulphide bridges in proteins. His comparative studies on other pancreatic proteolytic enzymes have revealed interesting homologies, which give information about the biological origin of the proteins and their mode of action. His earlier kinetic studies on chymotrypsin demonstrated the formation of an acyl enzyme as an intermediate in the hydrolysis reaction.

References

1. ^ Hartley, Brian (2004). "The First Floor, Department of Biochemistry, University of Cambridge (1952–58)". IUBMB Life. 56 (7): 437–439. doi:10.1080/15216540412331318974. ISSN 1521-6543. PMID 15545222. S2CID 19975592.
2. ^ "Chemistry Tree – Brian S. Hartley Family Tree". academictree.org. Archived from the original on 30 December 2015.
3. Rajewsky, K. (2014). "Michael S. Neuberger 1953-2013". Proceedings of the National Academy of Sciences. 111 (8): 2862–3. Bibcode:2014PNAS..111.2862R. doi:10.1073/pnas.1401334111. PMC 3939883. PMID 24532658.
4. Neuberger, Michael Samuel (1978). Transducing phages for analysis of gene duplications (PhD thesis). University of London. OCLC 500526968.
5. ^ "HARTLEY, Prof. Brian Selby". Who's Who. Vol. 2015 (online Oxford University Press ed.). A & C Black. (Subscription or UK public library membership required.)
6. "Brian Hartley (1926 – 2021)". 7 May 2021.
7. ^ "Professor Brian Hartley FRS". London: Royal Society. Archived from the original on 24 November 2015. One or more of the preceding sentences incorporates text from the royalsociety.org website where:

   "All text published under the heading 'Biography' on Fellow profile pages is available under Creative Commons Attribution 4.0 International License." --"Royal Society Terms, conditions and policies". Archived from the original on 25 September 2015. Retrieved 9 March 2016.{{cite web}}: CS1 maint: bot: original URL status unknown (link)

8. Hartley, Brian Selby (1978). Transducing phages for analysis of gene duplications (PhD thesis). University of London. OCLC 500526968.
9. Richmond, Virginia; Hartley, Brian S. (1959). "A Two-Dimensional System for the Separation of Amino-Acids and Peptides on Paper". Nature. 184 (4702): 1869–1870. Bibcode:1959Natur.184.1869R. doi:10.1038/1841869a0. S2CID 4287417.
10. Brown, JR; Hartley, BS (1966). "Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A". Biochemical Journal. 101 (1): 214–228. doi:10.1042/bj1010214. PMC 1270086. PMID 5971783.
11. Blow, David M.; Birktoft, J. J.; Hartley, Brian S. (1969). "Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin". Nature. 221 (5178): 337–340. Bibcode:1969Natur.221..337B. doi:10.1038/221337a0. ISSN 0028-0836. PMID 5764436. S2CID 4214520.
12. Naughton, M. A.; Sanger, F.; Hartley, B. S.; Shaw, D. C. (1960). "The amino acid sequence around the reactive serine residue of some proteolytic enzymes". Biochemical Journal. 77 (1): 149–163. doi:10.1042/bj0770149. PMC 1204911. PMID 13727969.
13. Hartley, B. S. (1960). "Proteolytic Enzymes". Annual Review of Biochemistry. 29: 45–72. doi:10.1146/annurev.bi.29.070160.000401. PMID 14400122.
14. Hartley, B.S.; Naughton, M.A.; Sanger, F. (1959). "The amino acid sequence around the reactive serine of elastase". Biochimica et Biophysica Acta. 34: 243–244. doi:10.1016/0006-3002(59)90254-9. PMID 14400120.
15. Hartley, B. S.; Brown, J. R.; Kauffman, Dorothy L.; Smillie, L. B. (1965). "Evolutionary Similarities between Pancreatic Proteolytic Enzymes". Nature. 207 (5002): 1157–1159. Bibcode:1965Natur.207.1157H. doi:10.1038/2071157a0. PMID 5882362. S2CID 4216808.
16. Hartley, B. S. (1964). "Amino-Acid Sequence of Bovine Chymotrypsinogen-A". Nature. 201 (4926): 1284–1287. Bibcode:1964Natur.201.1284H. doi:10.1038/2011284a0. PMID 14151403. S2CID 11398820.
17. Hartley, B. S. (1979). "Evolution of enzyme structure". Proceedings of the Royal Society of London. Series B. Biological Sciences. 205 (1161): 443–452. Bibcode:1979RSPSB.205..443H. doi:10.1098/rspb.1979.0078. PMID 42054. S2CID 32023040.
18. Winter, G.P.; Hartley, B.S. (1977). "The amino acid sequence of tryptophanyl tRNA Synthetase from Bacillus stearothermophilus". FEBS Letters. 80 (2): 340–342. Bibcode:1977FEBSL..80..340W. doi:10.1016/0014-5793(77)80471-7. PMID 891985.
19. Fersht, Alan R.; Ashford, Jeremy S.; Bruton, Christopher J.; Jakes, Ross; Koch, Gordon L. E.; Hartley, Brian S. (1975). "Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases". Biochemistry. 14 (1): 1–4. doi:10.1021/bi00672a001. PMID 1109585.
20. Siddiqui, K. S.; Rangarajan, M.; Hartley, B. S.; Kitmitto, A.; Panico, M.; Blench, I. P.; Morris, H. R. (1993). "Arthrobacter D-xylose isomerase: Partial proteolysis with thermolysin". Biochemical Journal. 289 (Pt 1): 201–208. doi:10.1042/bj2890201. PMC 1132150. PMID 8424759.
21. Hartley, Brian S.; Hanlon, Neil; Jackson, Robin J.; Rangarajan, Minnie (2000). "Glucose isomerase: Insights into protein engineering for increased thermostability". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1543 (2): 294–335. doi:10.1016/S0167-4838(00)00246-6. PMID 11150612.
22. "Certificate of election EC/1971/10: EC/1971/10". London: Royal Society. Archived from the original on 5 August 2014.

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