George Huntly Lorimer

George Lorimer
FRS
George Lorimer FRS
Born	George Huntly Lorimer; October 14, 1942 (age 82)
Education	George Watson's College
Alma mater	University of St Andrews (BSc); University of Illinois (MS); Michigan State University (PhD);
Awards	Humboldt Prize (1997)
	Scientific career
Institutions	University of Maryland
Thesis	The role of oxygen in photorespiration (1972)
Website	www.chem.umd.edu/faculty-staff-directory/facultydirectory/george-lorimer

George Huntly Lorimer (born 1942)^[1] FRS^[2] is a professor in the Department of Chemistry and Biochemistry at the University of Maryland.^[1]^[3]

Career and research

Lorimer is recognized for his work on mechanism of two proteins, RuBisCO and the GroE chaperonins. Rubisco is the enzyme responsible for photosynthetic carbon fixation, and the GroE chaperonins enable the Adenosine triphosphate (ATP)-dependent folding of many other proteins.^[2]

Using Oxygen-18 Lorimer demonstrated the oxygenase activity of RuBisCO, both in vivo and in vitro.^[2] He further established the novel mechanism for the activation of RuBisCO by carbon dioxide, the formation of a lysyl-carbamate in the active site.^[2] With his colleagues at DuPont he employed chemical quench and other techniques to trap and identify the 6-carbon reaction intermediate of the carboxylation reaction and defined the complete stereo-chemical course of the reaction.^[2]

In 1989, using an unequivocally unfolded protein and the purified chaperonin proteins GroEL and GroES, his group was the first to demonstrate the ATP-dependent folding of RuBisCO and many other proteins.^[2] With Devarajan (Dave) Thirumalai he performed a bioinformatic analysis to define the structural elements of the substrate proteins that GroEL recognizes.^[2] Lorimer has also shown that GroEL can perform work on substrate protein during allosteric transitions. He has determined the crystal structure of the functional form, the symmetric GroEL:GroES2 “football” and established that the GroEL rings operate as parallel-processing, iterative annealing machines.^[2]