Professor Quentin Gibson
Born
Quentin Howieson Gibson

(1918-12-09)9 December 1918
Aberdeen, Scotland
Died6 March 2011(2011-03-06) (aged 92)
CitizenshipBritish, American
EducationQueen's University Belfast
SpouseAudrey Jane Pinsent
Children4
AwardsFellow of the Royal Society (1969)[1]
Scientific career
FieldsBiochemistry of heme proteins
InstitutionsUniversity of Sheffield
Cornell University
University of Pennsylvania
Notable studentsKeith Moffat[2]

Quentin Howieson Gibson FRS[1] (9 December 1918 – 16 March 2011) was a Scottish American physiologist, and professor at the University of Sheffield,[3] and Cornell University.[4]

Education

Gibson earned a Doctor of Medicine degree in 1944 and a Ph.D. in 1946, from Queen's University Belfast.

Life

Gibson taught at the University of Sheffield from 1947. Whilst at the University of Sheffield Gibson met Audrey Jane Pinsent in 1951. They married, started a family, and eventually had four children. Jane Gibson continued working part-time whilst raising her family. In 1963 they emigrated to the United States, where she took up positions, first at the University of Pennsylvania.[5] He succeeded (Sir) Hans Krebs as the Head of the Department of Biochemistry in 1955. In 1963 he left Sheffield to become a professor at the University of Pennsylvania. He was the Greater Philadelphia Professor at Cornell University, from 1965 to 1996. In 1982, he became a U.S. citizen.[6]

Research

Hemoglobin

Gibson started his career with studies of hemoglobin,[7] [8] and continued with much other work on heme proteins.

Medical and physiological work

In keeping with his medical qualifications, much of Gibson's early work[9] [10] had medical or physiological relevance.[11]

Cooperativity

During the period when protein and enzyme cooperativity was at the center of biochemical interest Gibson studied it in the context of abnormal hemoglobins.[12] [13]

Rapid reactions

Gibson made major contributions to the development of methods for studying rapid reactions,[14] and their application to hemoglobin.[15]

Other proteins

Other work concerned enzymes such as "diaphorase",[16][17] glucose oxidase,[18] cytochrome oxidase[19][20] and peroxidase.[21]

Thermodynamics

Much of Gibson's work concerned questions of thermodynamics and equilibria, and in that context he participated in discussions about how to present thermodynamic data.[22]

Awards and honours

Gibson was elected a Fellow of the Royal Society in 1969.[1] He was also a member of the National Academy of Sciences, and an associate editor of the Journal of Biological Chemistry from 1975 to 1994.[23]

References

  1. 1 2 3 Olson, J. S.; Gutfreund, H. (2013). "Quentin Howieson Gibson 9 December 1918 -- 16 March 2011". Biographical Memoirs of Fellows of the Royal Society. 60: 169–210. doi:10.1098/rsbm.2013.0018.
  2. ↑ "Quentin H. Gibson's Profile on Academic Tree".
  3. ↑ "Quentin H. Gibson". Cf.ac.uk. Retrieved 21 December 2011.
  4. ↑ "Notices 2011". Royal Society. Retrieved 21 December 2011.
  5. ↑ Bretscher, Anthony. "Audrey Jane Gibson" (PDF). ecommons.cornell.edu. Cornell University. Retrieved 27 March 2017.
  6. ↑ Olson, John. "Retrospective: Quentin H. Gibson". Asbmb.org. Retrieved 21 December 2011.
  7. ↑ Gibson, Q. H. (1943). "The reduction of methaemoglobin by ascorbic acid". Biochemical Journal. 37 (5): 615–618. doi:10.1042/bj0370615. PMC 1257979. PMID 16747706.
  8. ↑ Gibson, Q. H. (1948). "The reduction of methaemoglobin in red blood cells and studies on the cause of idiopathic methaemoglobinaemia". Biochemical Journal. 42 (1): 13–23. doi:10.1042/bj0420013. PMC 1258588. PMID 16748235.
  9. ↑ Gibson, Q. H.; Harrison, D. C.; Montgomery, D. A. D. (1950). "Case of Acute Porphyria". BMJ. 1 (4648): 275–277. doi:10.1136/bmj.1.4648.275. PMC 2036737. PMID 15410128.
  10. ↑ Gibson, Q. H.; Wiseman, G. (1951). "Selective absorption of stereo-isomers of amino-acids from loops of the small intestine of the rat". Biochemical Journal. 48 (4): 426–429. doi:10.1042/bj0480426. PMC 1275345. PMID 14838861.
  11. ↑ Carey, Francis G.; Gibson, Quentin H. (1987). "Blood Flow in the Muscle of Free-Swimming Fish". Physiological Zoology. 60: 138–148. doi:10.1086/physzool.60.1.30158635. S2CID 87448894.
  12. ↑ Cassoly, Robert; Gibson, Quentin H. (1975). "Conformation, co-operativity and ligand binding in human hemoglobin". Journal of Molecular Biology. 91 (3): 301–313. doi:10.1016/0022-2836(75)90382-4. PMID 171411.
  13. ↑ Gibson, Q. H.; Roughton, F. J. W. (1957). "The kinetics and equilibria of the reactions of nitric oxide with sheep haemoglobin". The Journal of Physiology. 136 (3): 507–526. doi:10.1113/jphysiol.1957.sp005777. PMC 1358871. PMID 13429517.
  14. ↑ Gibson, QH; Milnes, L. (1964). "Apparatus for rapid and sensitive spectrophotometry". Biochemical Journal. 91 (1): 161–171. doi:10.1042/bj0910161. PMC 1202828. PMID 5833381.
  15. ↑ Gibson, Q. H. (1959). "The photochemical formation of a quickly reacting form of haemoglobin". Biochemical Journal. 71 (2): 293–303. doi:10.1042/bj0710293. PMC 1196788. PMID 13628568.
  16. ↑ Massey, V.; Gibson, Q. H.; Veeger, C. (1960). "Intermediates in the catalytic action of lipoyl dehydrogenase (Diaphorase)". Biochemical Journal. 77 (2): 341–351. doi:10.1042/bj0770341. PMC 1204990. PMID 13767908.
  17. ↑ Gibson, Q. H. (1954). "Stopped-flow apparatus for the study of rapid reactions". Discussions of the Faraday Society. 17: 137. doi:10.1039/df9541700137.
  18. ↑ Gibson, Q H; Massey, V; Swoboda, B E P J (1964). "Kinetics and mechanism of action of glucose oxidase". J. Biol. Chem. 239 (11): 3927–3934. doi:10.1016/S0021-9258(18)91224-X. PMID 14257628.
  19. ↑ Gibson, Q H; Greenwood, C; Wharton, D C; Palmer, G (1965). "Reaction of cytochrome oxidase with cytochrome C". J. Biol. Chem. 240 (2): 888–894. doi:10.1016/S0021-9258(17)45258-6. PMID 14275150.
  20. ↑ Brunori, M.; Gibson, Q.H. (1983). "Oxygen activation by cytochrome oxidase: A new spectral intermediate observed by flow-flash". The EMBO Journal. 2 (11): 2025–2026. doi:10.1002/j.1460-2075.1983.tb01695.x. PMC 555404. PMID 6315412.
  21. ↑ Noble, R W; Gibson, Q H (1970). "Reaction of ferrous horseradish peroxidase with hydrogen peroxide". J. Biol. Chem. 245 (9): 2409–2413. doi:10.1016/S0021-9258(18)63167-9. PMID 5442280.
  22. ↑ Alberty, Robert A. (1994). "Recommendations for nomenclature and tables in biochemical thermodynamics (IUPAC Recommendations 1994)". Pure and Applied Chemistry. 66 (8): 1641–1666. doi:10.1351/pac199466081641. S2CID 96307963.
  23. ↑ "Volume 250 Issue 24 pages 9215-9438 (J. Biol. Chem.)". 1975. Retrieved 14 April 2021.
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