Rowena Green Matthews, born on 1938, is the G. Robert Greenberg Distinguished University professor emeritus at the University of Michigan, Ann Arbor. Her research focuses on the role of organic cofactors as partners of enzymes catalyzing difficult biochemical reactions, especially folic acid and cobalamin. Among other honors, she was elected to the National Academy of Sciences in 2002 and the Institute of Medicine in 2004.
Early life and education
Matthews was born in Cambridge, England while her father, biochemist David E. Green, was on sabbatical there. Matthews earned her B.A. in biology summa cum laude from Radcliffe College in 1960. As an undergraduate, and for three years thereafter, she worked with George Wald studying a new intermediate in the bleaching of the visual pigment rhodopsin that temporally coincided with initiation of visual excitation. She then went to graduate school in biophysics at the University of Michigan, where she did her dissertation research in the laboratory of Vincent Massey. She received her Ph.D. in 1969.
Academic career
After finishing her Ph.D., Matthews remained at the University of Michigan as a postdoctoral fellow in the laboratory of Charles Williams in the department of Biological Chemistry and Assistant Research Scientist in the Biophysics Research Division in 1978. She was promoted to Associate Professor in 1981 became a full professor in 1986, and became the G. Robert Greenberg Distinguished University Professor in 1995. In 2002, she assumed the position of Senior Research Professor and Charter Faculty Member of the Life Sciences Institute. She retired in 2007, assuming professor emeritus status.
Dr. Matthew's research focused on one-carbon metabolism, with particular emphasis on the enzymes that catalyze the de novo generation of methyl groups: methionine synthase, a B-12 dependent enzyme in humans, and methylenetetrahydrofolate reductase. Her collaboration with geneticist Rima Rozen at McGill University led to the cloning of human methylenetetrahydrofolate reductase and the characterization of the C677T polymorphism associated with hyperhomocysteinemia in humans. The polymorphism can lead to a high amount of homocysteine in the bloodstream. High concentrations of homocysteine in the plasma can increase the risk for cardiovascular diseases and the use of folic acid have been shown to decrease the amounts in humans. In collaboration with Prof. Martha Ludwig they elucidated the first X-ray structure of vitamin B12 bound to a protein, cobalamin-dependent methionine synthase.