Awardee OrganizationNEW MEXICO STATE UNIVERSITY LAS CRUCES
Description
Abstract Text
Fatty acids ar a class of poorly soluble, hydrophobic metabolites that are
used as building blocks for complex membrane lipids, energy storage and
energy production. Under normal circumstances, the total concentration of
fatty acids in the cell are kept within strict limits. During certain
pathological conditions (ischemia/reperfusion, diabetes) total fatty acid
concentrations can increase dramatically (80%) in some experiments). It
is thought that such concentrations of fatty acids will outstrip the
capacity of the cell to remove them from the cytoplasm. The effects of
these elevated fatty acids levels however is not well understood.
Preliminary experiments in this laboratory have demonstrated that
cytochromes c are affected by the presence of fatty acids at physiological
levels. The UV-VIS spectrum of the protein changes dramatically upon
binding. It was originally thought that this must involve specific
rearrangement of the protein structure around the heme ring. Subsequent
1/H-NMR experiments have demonstrated that the methionine sulfur atom
(bonded directly the iron) is shifted away from the heme ring upon the
binding of fatty acids. Cyclic voltammetric experiments have shown that
the redox potential of cytochrome c is shifted when fatty acids bind to
the protein. These observations indicate that fatty acids may have an
important role in controlling the electron transport function of
cytochrome c. Structural implications also suggest that cytochromes may
be an important component fatty acid metabolism as well. Specific
research aims, based on this hypothesis, are to rigorously investigate the
affects of fatty acids on the structure, function, and reactivity of
cytochromes c.
The interactions of cytochromes c from mammalian, plant, and microbial
sources with fatty acids of varied structural features will be studied.
Most studies will be with native cytochromes buy site-specific variants,
supplied by other researchers, will also be investigated in order to
provide a more detailed of the binding process through structural
modifications of the proposed site.
A variety of instrumental techniques will be used to this hypothesis.
These include stopped-flow and temperature jump kinetic
spectrophotometers, a rapid-scanning spectrophotometer, 1/H and 19/F NMR
spectrometers (250MHz and 400MHz), HPLC, conventional diode array
spectrophotometers, cyclic voltammetry, and oxygen sensitive electrodes.
Public Health Relevance Statement
Data not available.
NIH Spending Category
No NIH Spending Category available.
Project Terms
chemical bindingcytochrome celectrodeselectron transportenzyme activityenzyme structurefatty acidshigh performance liquid chromatographynuclear magnetic resonance spectroscopyprotein structure functionspectrometry
No Sub Projects information available for 5S06GM008136-24 0034
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