Abstract: The thermal denaturation of the small iron protein, rubredoxin, has been previously shown to exhibit unusual kinetics (Elkins,1995) characterized by nearly constant rate of change and a reaction time independent of the starting amount of the protein. Recently, Wampler and Bradley (1997) have described a kinetic model that explains these data and a variety of other thermal denaturation data for various rubredoxins as well as other proteins. This presentation describes the features of the model and offers additional data that supports a working hypothesis where in rubredoxin thermal denaturation in the presense of oxygen leads to formation of an iron containing species that catalyzes further breakdown of the protein. In the absense of oxygen the kinetics are much slower and fit a more normal exponential decay model. Work is in progress to identify the products of this reaction (Neuhaus, 1997). This work was supported by NIH grants GM41482 and GM50736.
Table of ContentsThe Unusual Kinetics of Rubredoxin Thermal Denaturation Characteristics of simple models Lysozyme irreversible thermal denaturation at 100 degrees Ferredoxin and Carbonic Anhydrase thermal denaturation. WHY'S RD THERMAL DECAY UNUSUAL? Chris Elkin’s data (1995) for Clostridium pasteurianum rubredoxin. Another look at the C. p. rubredoxin decays Can you get Michaelis-Menten kinetics with an irreversible reaction? ...model can vary from exponential to very cooperative Therefore, Chris’s data shows characteristics of all aspects of the model mechanism. Spectra taken during aerobic Desulfovibrio vulgaris rubredoxin denaturation. Pyrococus furiosus rubredoxin decays are also fit. Some fits to the Clostridium pasteurianum rubredoxin decays How do you interpret these fits... Reality is always more complex. |
Author:
J. E. Wampler
Home Page: this server References Cited: Ahern, T. J. , and Klibanov, Y A. M. (1985). Science 228 , 1280-1284. |