Bettie Sue Masters, PhD

Professor Emeritus (Retired, UT Health San Antonio)


Ph.D. Biochemistry Duke University 1963
Post Doctoral: Department of Biochemistry Duke University
Other Faculty Positions: July 1990-January 2016 - The Robert A. Welch Distinguished Professor in Chemistry, Dept of Biochemistry - The University of Texas Health Science Center at San Antonio

1982-1990 Professor & Chairman, Dept of Biochemistry, Medical College of Wisconsin, Milwaukee, WI

1979-1982 Research Professor of Surgery, Director of Biochemical Burn Research, UT Southwestern Medical School, Dallas, TX

1968-1982 Assistant, Associate and Full Professor of Biochemistry
UT Southwestern Medical School, Dallas, TX

1968-1973 American Heart Assn, Established Investigator, UT Southwestern Medical School, Dallas, TX


1. 1. Structural/Functional Modularity in Nitric Oxide Synthase; Principal Investigator: Bettie Sue Masters, Ph.D.; Agency: National Institute of General Medical Sciences; Type: R01 (GM52419, Years 13-16) Period: 4/1/2009-3/31/2013. Score 122; 2.5%ile

Original aims of this grant activity featured a modular approach to the structural aspects of neuronal nitric oxide synthase (nNOS) but have been extended to include inducible and endothelial NOS isoforms and have permitted the expression of isolated modules and domains of all three isoforms in E. coli. NOS isoforms have been purified in their full-length forms, also, for study using a variety of biophysical approaches, including x-ray crystallography. The hypothesis is that the NOS isoforms, sharing common prosthetic groups, cofactors and mechanisms, are structurally unique in order to perform specific functions in the cell types in which they occur. These enzymes are involved in neurotransmission, immune responses (cytotoxicity) and vasodilation, among other physiologically important signaling functions.

2. Molecular and Cellular Effects of Human Mutations in Cytochrome P450 Reductase; Principal Investigator: Bettie Sue Masters, Ph.D.; Agency: National Institute of General Medical Sciences; Type: 1-R01 (GM81568-01) Period: 04/01/2008-03/31/2012. Score 137; 3.1%ile.

This proposal addresses the effects of the human polymorphisms on the structure and function of NADPH-cytochrome P450 reductase in vitro and in vivo (cellular level). These mutations, depending upon their location in the reductase molecule, cause severe phenotypic characteristics in human patients, including craniofacial dysmorphogenesis and steroidogenic abnormalities resulting in sexual dimorphisms. The proposed studies will address the developmental consequences of these mutations in human cells and attempt to determine the signaling pathways affected, as well as the structural consequences to the reductase itself and the compromises in function that result. Preliminary data show that rescue of several of the human variants can be rescued by the addition of FAD, derived from riboflavin, suggesting a therapeutic approach to reversing the consequences of these devastating mutations if addressed in a timely manner prenatally.