Professor Williams received his B.S. degree from the University of Maryland in 1956 and his Ph.D. degree from Duke University in 1961. From 1961–63, he pursued postdoctoral studies at the University of Sheffield, England. He joined the University of Michigan faculty as an instructor in 1963 and was promoted to assistant professor in 1966, associate professor in 1970, and professor in 1979. He was appointed a research chemist at the Ann Arbor Veterans Administration Hospital in 1963 and was promoted to supervisory research chemist in 1974 and research career scientist in 1978. He retired from active faculty status in 2005.
Professor Williams' entire career has been dedicated to the study of one family of flavoenzymes, which are enzymes containing the B-vitamin riboflavin. For many years he applied his vast knowledge of this enzyme family to the development of a much needed new malaria prophylactic. This incredible effort required Professor Williams to coordinate six laboratories, both in this country and abroad. His work has resulted in the publication of more than 110 papers in prestigious peer-reviewed journals.
In addition to his research, Professor Williams taught the biochemistry course for medical students for thirty years as well as several courses in the graduate program. He trained twelve graduate students and twenty postdoctoral fellows, many of whom have gone on to distinguished positions in academia. Professor Williams has served on numerous advisory groups, including the Research and Development Committee at the Veterans Affairs Medical Center and the Biomedical Research Council of the Medical School. He served as coordinator for research at the Veterans Administration Medical Center from 1977–79. Professor Williams received the Distinguished Faculty Achievement Award in 1992 and the Council's Choice Award for outstanding contributions to the Inteflex Program in 1993.
Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase.
Cheng Z, Zhang J, Ballou DP, Williams CH Jr.
Chem Rev. 2011; 111: 5768–83.
Investigations of the catalytic mechanism of thioredoxin glutathione reductase from Schistosoma mansoni.
Huang HH, Day L, Cass CL, Ballou DP, Williams CH Jr, Williams DL.
Biochemistry. 2011; 50: 5870–82.
Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster.
Huang HH, Arscott LD, Ballou DP, Williams CH.
Biochemistry. 2008; 47: 12769–76.
Acid-base catalysis in the mechanism of thioredoxin reductase from Drosophila melanogaster.
Huang HH, Arscott LD, Ballou DP, Williams CH Jr.
Biochemistry. 2008; 47: 1721–31.
The relationship of the redox potentials of thioredoxin and thioredoxin reductase from Drosophila melanogaster to the enzymatic mechanism: reduced thioredoxin is the reductant of glutathione in Drosophila.
Cheng Z, Arscott LD, Ballou DP, Williams CH Jr.
Biochemistry. 2007; 46: 7875–85.
Identification of acid-base catalytic residues of high-Mr thioredoxin reductase from Plasmodium falciparum.
McMillan PJ, Arscott LD, Ballou DP, Becker K, Williams CH Jr, Müller S.
J Biol Chem. 2006; 281: 32967–77.
For a list of publications from PubMed, click HERE