Michael Smith (chemist)

For other people by this name, see Michael Smith.

Michael Smith, CC, OBC (April 26, 1932 – October 4, 2000) was a British-born Canadian biochemist who was the 1993 Nobel Prize winner in Chemistry.

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Smith received the Prize for his fundamental contributions to the establishment of oligonucleotide-based, site-directed mutagenesis and its development for protein studies.

Born in Blackpool, England, he received his PhD in 1956 from the University of Manchester. He went on to do post-doctoral work in Gobind Khorana's Laboratory at the University of British Columbia, Vancouver, Canada. He remained at the University of British Columbia from 1956 until his death in 2000.

In 1987 he became the Director of the University of British Columbia Biotechnology Laboratory.

Honors

In 1994 Michael Smith was made a Companion of the Order of Canada.

In 2001 the Michael Smith Foundation for Health Research was founded and named after him.

In 2004 the UBC Biotechnology Laboratories were renamed the Michael Smith Laboratories in his honor.

Also in 2004 the new biological sciences research centre at The University of Manchester was named the Michael Smith Building.

Selected publications

• Ferrer, J.C., Turano, P., Banci, L., Bertini, I., Morris, I.K., Smith, K.M., Smith, M., Mauk, A.G. (1994). Active site coordination chemistry of the cytochrome c peroxidase Asp235Ala variant: Spectroscopic and functional characterization. Biochem. 33: (25) 7819-7829.
• Guillemette, J.G., Barker, P.D., Eltis, L.D., Lo, T.P., Smith, M., Brayer, G.D., Mauk, A.G. (1994). Analysis of the biomolecular reducation of ferricytochrome c by ferrocytochrome b5 through mutagenesis and molecular modelling. Biochimie 76: 592-604.
• Berghuis, A.M., Guillemette, J.G., Smith, M., and Brayer, G.D. (1994). Mutation of tyrosine-67 to phenylamaine in cytochrome c significantly alters the local heme environment. J. Mol. Biol. 235: 1326-1341.
• Rafferty, S.P., Guillemette, J.G., Smith, M., and Mauk, A.G. (1996). Azide binding and active site dynamics of position-82 variants of ferricytochrome c. Inorg. Chem. Acta.242: 171-177.
• Woods, A.C., Guillemette, J.G., Parraish, J.C., Smith, M., Wallace, C.J.A. (1996). Synergy in Protein Engineering. Mutagenic manipulation of protein structure to simplify semisynthesis. J. Biol. Chem. 271: (50) 32008-32015.
• Hildebrand, D.P., Ferrer, J.C., Tang, H.-L., Smith, M., and Mauk, A.G. (1996). Trans effects on cysteine ligation in the proximal His93Cys variant of horse heart myoglobin. Biocchemistry 34: 11598-11605.
• Hildebrand, D.P., Ferrer, J.C., Tang, H.-L., Luo, Y., Hunter, C.L., Brayer, G.D., Smith, M. and Mauk, A.G. (1996). Efficient coupled oxidation of heme by an active site variant of horse heart myoglobin. J. Am. Chem. Soc. 118: (51) 12909-12915.
• Maurus, R., Overall, C.M., Bogumil, R., Luo, Y., Mauk, A.G., Smith, M., and Brayer, G.D. (1997). Thermal stabilization of horse heart myoglobin through modification of ahydrophobic cluster in the proximal heme pocket. Biochem. Acta. 1341: 1-13.