During his early years at Cornell, Gibson and Richard DeSa automated the collection of data from all his rapid kinetic instruments, using minicomputers to provide the first millisecond digital readouts of kinetic data in enzymology. This technology was applied to a complete analysis of O2 binding. Both equilibrium curve and time course data were analyzed by combined analog and digital computing. Next, Gibson turned his attention to the problems associated with naturally occurring hemoglobinopathies, the properties of globins from a variety of plant and animal species, the differences between the alpha and beta subunits of human hemoglobin, and the rate of the R to T quaternary transition.
After developing a stomach ulcer in 1969, Gibson decided to spend his summers at Woods Hole, which he did from 1970 to approximately 1990. He and his wife Jane bought a house there and a sailboat, which he used every summer until Hurricane Gloria destroyed it in 1985. Jane taught in the summer microbiology course at the Marine Biological Laboratory, and Quentin went out on expeditions to collect fish blood with Frank Carey. After he returned to Cornell in the fall, his students studied ligand binding to fish Hbs, which showed unusual pH and temperature effects (6).
In the 1980s, Gibson’s group constructed laser photolysis systems to examine internal (geminate) rebinding within the globin molecules at room temperature. These experiments then were used to determine pathways for ligand movement into and out of the protein matrix using site-directed mutagenesis in collaboration with a variety of laboratories. In the 1990s, Ron Elber helped Gibson implement the use of molecular dynamics simulations for interpreting the ultrafast picosecond and nanosecond recombination processes that were being measured in his laboratory with both native and mutant proteins.
In 1996, Gibson and his wife retired from Cornell University and moved permanently to Etna, N.H. They spent the winter months of 1996 to 2001 in Houston, Texas. There, Quentin worked in a kinetics laboratory set up for him at Rice University, continuing his collaborative studies with John Olson and George Phillips, while Jane worked in the microbiology department at the University of Texas Medical School Houston. This time period was highly productive and led to a detailed map of the pathway for O2 migration into and out of Mb. In 2002, Gibson decided to stay year-round in New Hampshire, but a small kinetics laboratory in William Royer’s laboratory at the University of Massachusetts Medical School allowed him to keep doing experiments on hemoglobins until 2009, the year his last research article appeared in print. Even after he was unable to make the trip to Worcester, Gibson continued to advise the Royer lab on both experimental techniques and interpretations of kinetic data well into the last year of his life.
Gibson’s career truly was remarkable. He published papers from 1943 to 2009, a span of almost seven decades. When he began his studies of hemoglobin in the 1940s, its structure was completely unknown, but when he ended his career, his papers described detailed movements of diatomic oxygen through a gate opened by rotation of the distal histidine and then its capture in well-specified cavities in the protein that were engineered by recombinant DNA technology, visualized by time-resolved X-ray crystallography, and analyzed by molecular dynamics simulations. In 2004, he wrote a detailed and amusing history of these changes in our understanding of hemoglobin kinetics (7).
A few months before his death, the regents of the University of Sheffield recognized Gibson’s contributions to science and to the reputation of their institution by granting him an honorary Doctorate of Science and establishing an eponymous lectureship. In January of 2011, he reflected peacefully and with contentment that this honor had brought his academic career full circle.
1. Gibson, Q. H. (1993) Historical note: methemoglobinemia – long ago and far away. Am. J. Hematol. 42, 3 – 6.
2. Gibson, Q. (2002) Introduction: congenital methemoglobinemia revisited. Blood 100, 3445 – 3446.
3. Gibson, Q. H. (1954) Stopped-Flow Apparatus for the Study of Rapid Reactions, Discuss. Faraday Soc. 137 – 139.
4. Gibson, Q. H., and Milnes, L. (1964) Apparatus for rapid and sensitive spectrophotometry. Biochem. J. 91, 161 – 171.
5. Gibson, Q. H. (1956) An apparatus for flash photolysis and its application to the reactions of myoglobin with gases. J. Physiol. 134, 112 – 122.
6. Andersen, M. E., Olson, J. S., Gibson, Q. H., and Carey, F. G. (1973) Studies on ligand binding to hemoglobins from teleosts and elasmobranchs. J. Biol. Chem. 248, 331 – 341.
7. Gibson, Q. H. (2004) Hemoglobin Kinetics – A Retrospect. Comprehensive Biochemistry (G. Semenza and A. J. Turner, Volume Eds.) 43, 101 – 197.
John Olson (firstname.lastname@example.org) is the Ralph and Dorothy Looney professor of biochemistry and cell biology at Rice University. William Royer (William.Royer@umassmed.edu) is a professor of Biochemistry and Molecular Pharmacology at the University of Massachusetts Medical School.
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