![]() BIOLOGICAL SCIENCE FACULTY MEMBER Dr. Betty Jean Gaffney
Personal Home Page Lipids and arachidonic acid mediators; molecular redox mechanisms; magnetic resonance. We study the roles of unsaturated fatty acids in cells from several views. Recent studies focus on structure-function relationships of enzymes in arachidonic acid/oxylipin cascades, including iron and manganese lipoxygenases from several species and a novel allene oxide synthase from Plexaura homomalla. Oxidation and reduction of metal centers are key events in the mechanisms of these enzymes. We also specialize in studying redox-active enzymes by high- and low-frequency electron paramagnetic resonance (EPR). The instrumentation for the high-field studies operates at 94 GHz and is equipped for magnetic-field scans from 0 to 6 tesla. Computer simulation of EPR spectra has been developed for multielectron centers. A high frequency might be chosen in EPR studies, for example, because extremely small samples are used, magnetic-field-independent effects such as zero-field splitting become less important so resolution is improved, the contributions of multicomponent samples can be resolved, or a fast-motional process is involved. We aim to explore redox reactions in new enzymes as they are discovered. If you've got a favorite, let us know.
Selected Recent Publications: Gaffney, B. J. 1996. Lipoxygenases: structural principles. Annual Review of Biophysics and Biomolecular Structure 25: 431-459. PMID: 8800477. Full text, PDF Bowers, C. R., V. Storhaug, C. E. Webster, J. Bharatam, A. Cottone III, R. Gianna, K. Betsey, and B.J. Gaffney. 1999. Exploring protein surfaces and cavities in lipoxygenase and other proteins by hyperpolarized xenon-129 NMR. Journal of the American Chemical Society 121: 9370-9377. PMID: 16429610. Full text, PDF Abraham, B., M. Sono, O. Boutaud, A. Shriner, J. H. Dawson, A. R. Brash, and B. J. Gaffney. 2001. Characterization of the coral allene oxide synthase active site with magnetic circular dichroism and electron paramagnetic resonance spectroscopy: evidence for tyrosinate-ligation to the ferric enzyme heme iron. Biochemistry 40: 2251-2259. PMID: 11329294. Full text, PDF Gaffney, B. J., C. Su, and E. H. Oliw. 2001. Assignment of EPR transitions in a manganese-containing lipoxygenase and prediction of local structure. Applied Magnetic Resonance 21: 413-424. PMID: 16518455. Full text, PDF Wu, F., L. J. Katsir, M. Seavy, B. J. Gaffney. 2003. Role of radical formation at Y193 in the allene oxide synthase domain of a lipoxygenase-AOS fusion protein from coral. Biochemistry 42: 6871-6880. PMID: 12779342. Full text, PDF Agarwalla, S., R. M. Stroud, and B. J. Gaffney. 2004. Redox reactions in the iron-sulfur cluster in a ribosomal RNA methyltransferase, RumA: optical and EPR studies. Journal of Biological Chemistry 279:34123-34129. PMID: 15181002. Full text, PDF Coffa, G., A. N. Imber, B. C. Maguire, G. Laxmikanthan, C. Schneider, B. J. Gaffney, and A. R. Brash. 2005. On the relationships of substrate orientation, hydrogen abstraction and product stereochemistry in single and double dioxygenations by soybean lipoxygenase-1 and its Ala542Gly mutant. Journal of Biological Chemistry 280: 38756-38766. PMID: 16157595. Full text, PDF Youn, B. Y., G. E. Sellhorn, R. J. Mirchel, B. J. Gaffney, H. D. Grimes, and C. H. Kang. 2006. Crystal structures of vegetative soybean lipoxygenase VLX-B and VLX-D, and comparisons with seed isoforms, LOX-1 and LOX-3. PROTEINS: Structure, Function, and Bioinformatics 65: 1008-1020. PMID: 17022084. Wu, F. Y., and B. J. Gaffney. 2006. Dynamic behavior of fatty acid spin labels within a binding site of soybean Lipoxygenase-1. Biochemistry 45:12510-12518. PMID: 17029406. Gaffney, B. J. 2007. Anethesia, analgesia and euphoria. Biophysical Journal 92: 1-2. PMID: 17028147. Gaffney, B. J. 2009. High resolution EPR of mononuclear iron proteins. Pages 233-268 in Biological Magnetic Resonance, Vol 28. High Resolution EPR: Applications to Metalloenzymes and Metals in Medicine, G. Hanson and L. J. Berliner, eds. Springer Verlag. ISBN 978-0-64655-6. Click here for author preprint.
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