Michael J. Barber, D.Phil.
B.Sc. Hons. Chemistry (1972)
University of Kent, Canterbury, Kent, U.K.
M.Sc. Enzyme Chemistry (1973)
University of Kent, Canterbury, Kent, U.K.
D.Phil. Biochemistry (1976)
University of Sussex, Brighton, U.K.
I completed my postdoctoral training at the University of Sussex and in the Department of Biochemistry at Duke University Medical School. I was also a lecturer in Physical Sciences at Britain’s Open University.
I have published over 115 manuscripts in peer-reviewed journals including Biochemistry, Journal of Biological Chemistry, Biochemical Journal, Archives of Biochemistry and Biophysics and Blood. I have published 21 book chapters and reviews in such journals as Annual Reviews and I have published or presented over 200 abstracts at national and international scientific meetings. Examples include:
Marohnic, C.C., Bewley, M.C. & Barber, M.J. (2003), “Engineering and Characterization of a NADPH-Utilizing Cytochrome b5 Reductase”, Biochemistry 42, 11170-11182.
Bewley, M.C., Davis, C.A., Marohnic, C.C, Taormina, D. & Barber, M.J. (2003), “Cytochrome b5 Reductase: The Structure of the S127P Methemoglobinemia Type II Mutant at 1.8 Ao Resolution”, Biochemistry 42, 13145-13151.
Marohnic, C.C., Crowley, L.J., Davis, C.A., Smith, E.T & Barber, M.J. (2005), “Cytochrome b5 Reductase: The Role of the si-Face Residues, Proline 92 and Tyrosine 93, in Structure and Catalysis”, Biochemistry 44, 2449-2461.
Roma, G.W., Crowley, L.J., Davis, C.A. & Barber, M.J. (2005), “Mutagenesis of Glycine 179 Modulates Both Catalytic Efficiency and Reduced Pyridine Nucleotide Specificity in Cytochrome b5 Reductase”, Biochemistry 44, 13467-13476.
Roma, G.W., Crowley, L.J. & Barber, M.J. (2006), “Expression and Characterization of a Functional Canine Variant of Cytochrome b5 Reductase”, Arch. Biochem. Biophys. 452, 69-82.
I have always been fascinated by the complexity of proteins and enzymes and would describe myself as a protein engineer. My students and I use recombinant techniques to examine the structural and functional properties of flavoproteins and metalloenzymes with particular emphasis on those involved in cardiovascular disease. We utilize a broad array of biophysical techniques to explore how amino acid substitutions change the properties of various flavoproteins.
I teach a variety of graduate courses that focus on the subject areas of bioinformatics, (BCH 6888 Bioinformatics & BCH 6889 Bioinformatics II) and biotechnology (BSC 6436 Introduction to Biotechnology), a new on-line course in medical biochemistry (GMS 6210 Basic Medical Biochemistry) and a Clinical Correlations in Molecular Medicine course (BCH 6420). I also teach an Honor’s course that has focused on introducing undergraduates to biotechnology and currently uses case studies to examine current issues in the biomedical sciences (IDH 3350 Science in Action). I also direct our integrated course in the College of Medicine doctoral program (GMS 6001 Foundation in Biomedical Sciences).
While in High School, my favorite subject was chemistry. I continued this theme by majoring in Chemistry as an undergraduate. In my final undergraduate year I took a course in enzymology which exposed me to the complexities of protein structure and function. I chose this field for my Master’s degree, specializing in enzyme chemistry. I found the topic so broad and interesting that I continued the subject for my D.Phil. focusing on metalloenzymes. I have been working in the area of flavoproteins and molybdoenzymes ever since entering graduate school.
As a graduate student, I was responsible for several classes and laboratory sections that were part of the undergraduate curriculum in the biological sciences. I really enjoyed the interaction and the challenges posed by the students in addition to the continued exposure to new ideas and advances in the biological sciences that were integrated into class sessions. I found that I could combine my interest in undergraduate and graduate teaching with my research into the challenges of trying to understand how combinations of twenty amino acids could be transformed into highly efficient biological catalysts. The opportunity to pursue research projects of my choice was a significant contributing factor.
I had collaborated with a USF College of Medicine faculty member while at Duke University and when I heard that a tenure track position in the Department of Biochemistry was available, I applied. I was very interested in continuing my work in the area of molybdoproteins with an established investigator who was an international leader in the field of nitrate assimilation enzymology. I also recognized the opportunity of joining a young and expanding institution while my experiences at Duke had confirmed that I wanted to continue my academic career in a medical school. I was also influenced by my spouse, who is a native Floridian.
I enjoy the breadth of teaching and the training opportunities at USF. One day, I can be involved in teaching an undergraduate course in the Honor’s program that continually challenges me to make modern biomedical science relevant to predominantly non-science majors which will be followed by teaching an advanced graduate course in Bioinformatics as part of a five college interdisciplinary Master’s program. I also enjoy developing new courses, such as those in biotechnology, which provide students with different educational opportunities and contributing to the organization of new graduate programs.
I’ve enjoyed interacting and collaborating with a diverse array of very talented faculty and students and the opportunity to participate in a variety of research projects that have continually motivated me to apply new methods and techniques and expand my academic interests.
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