Joan Selverstone Valentine graduated from Smith College in Northampton, Massachusetts in 1967 with an A.B. in Chemistry. Four years later, she was the first woman to receive a Ph.D. in Chemistry from Princeton University. After a year as an Instructor at Princeton, she was appointed Assistant Professor of Chemistry at Rutgers University in New Brunswick in 1972. In 1980, she moved to UCLA, where she is now Professor of Chemistry and Biochemistry.
In addition to her research and teaching activities at UCLA, Professor Valentine served as Associate Editor of the journal Inorganic Chemistry from 1989 to 1995 and has served as Editor-in-Chief of the journal Accounts of Chemical Research since September 1994. She was the recipient of a Research Career Development Award from the National Institutes of Health from 1976 to 1981. She also received the Alpha Chi Sigma Faculty Research Award at UCLA in 1985 and the Smith Medal (awarded to distinguished Smith College Alumnae) in 1991. In 2006, Dr. Valentine was elected to the National Academy of Science and in 2007 to the American Academy of Arts and Sciences.
Professor Valentine’s research has focused on the role of metal ions in biological oxidation and in naturally occurring biological antioxidant systems. It has had three central themes: (1) studies of isolated copper-zinc superoxide dismutase (CuZnSOD) proteins, (2) biological studies of CuZnSOD in vivo, and (3) coordination complexes as models for catalysts involved in biological oxidation. Since the 1970’s, her laboratory has played a major role in characterizing the properties of CuZnSOD and in the last few years has broadened to include studies of the role of mutations in CuZnSOD in causing familial amyotrophic lateral sclerosis (ALS, Lou Gehrig’s Disease). In parallel with studies of isolated CuZnSOD proteins themselves, her laboratory cloned the CuZnSOD gene from S. cerevisiae and characterized the highly oxygen-sensitive phenotype of yeast strains lacking this gene and/or other antioxidant genes such as MnSOD, catalase, and others.
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