BY JOHN OLSON AND WILLIAM ROYER 

Gibson was born on Dec. 9, 1918 in Aberdeen, Scotland. In 1926, his father was appointed director of the Linen Industry Research Association, and the family moved to Glenmore House, Lambeg, Northern Ireland, about 10 miles south of Belfast, where Quentin spent his youth among the research laboratories and the elaborate grounds. He enrolled in Queen’s University Belfast, receiving an M.D. in 1944 and a Ph.D. in 1946. Gibson’s graduate research was based on studies of the reaction of methemoglobin with ascorbate, which reverses methemoglobinanemia (1, 2). His work with D.C. Harrison on familial idiopathic methemoglobinanemia was the first to show a genetic disorder to be due to an enzyme defect. In the Belfast cases, the anemia was due to the loss of diaphorase I activity, which now is known as NADH methemoglobin reductase or cytochrome-b5 reductase.

From 1947 to 1956, Gibson was successively appointed a lecturer, senior lecturer, and reader in the department of physiology in the school of medicine at the University of Sheffield. During this time, he began close collaborations with F. J. W. Roughton, who in 1923 built the first rapid mixing device with H. Hartridge to examine the rates of O₂ and CO binding to hemoglobin and red cells. Gibson, who was a skilled machinist, designed and built a stopped-flow, rapid mixing spectrometer (3) and a flash photolysis apparatus (4, 5) to re-examine these reactions and, with Roughton, showed for the first time that the major increase in iron reactivity during cooperative ligand binding does not occur until roughly three ligands have been bound. Gibson and his colleagues then used these instruments to examine a variety of enzymatic and globin reactions. The stopped-flow spectrometer was commercialized by Durrum (later Dionex) Instruments, Inc. and sold as the “Durrum-Gibson” instrument until approximately 1990. 

While at the University of Sheffield, Gibson married and started a family. His wife, Audrey Jane (Pinsent) Gibson, obtained a doctorate from the University of London in 1949, where she discovered that selenite is required for the production of formate dehydrogenase in coliforms. After a year of study with C.B. Van Niel in California, she took a position in Sidney Elsden laboratory in Sheffield to characterize c-type cytochromes from photosynthetic bacteria. Like her husband, she had a long and distinguished career before her death on June 10, 2008.

In 1957, Gibson was awarded a professorship and the chair of the department of biochemistry at the University of Sheffield, replacing Hans Krebs, who took a position at the University of Oxford. Gibson brought together a remarkable group of biophysicists and enzymologists, including Gregorio Weber, Vincent Massey and Keith Dalziel, who each were elected either fellows of the London Royal Society or members of the U.S. National Academy of Sciences.

In 1963, Gibson moved to the United States to take a joint professorship of biophysics and physical biochemistry at the Johnson Research Foundation and of physiology in the graduate school of medicine at the University of Pennsylvania. While in Philadelphia, Gibson expanded his own work to studies of a variety of enzymes and, with Colin Greenwood, made the first measurements of bimolecular O₂ binding to cytochrome c oxidase using a newly constructed flow flash apparatus, which set the standard for these types of measurements for more than 30 years.

In 1965, Gibson became the Greater Philadelphia Professor in the Section of Biochemistry, Molecular and Cell Biology at Cornell University, where he remained until his retirement in 1996. While at Cornell, Gibson was elected a fellow of the London Royal Society in 1969, became a member of the U.S. National Academy of Sciences immediately after becoming a U.S. citizen in 1982, served as an associate editor of the Journal of Biological Chemistry from 1975 to 1994, and received the Keilin Memorial Medalist Award and Lectureship in 1990.