Home
Classes
Research
Publications
Curriculum Vitae

Department of Chemistry & Biochemistry

Florida International University
University Park
11200 SW 8th Street
Miami, Florida 33199

Office: CP 406
Phone: (305) 348-7406
Fax: (305) 348-3772
Email: miksovsk@fiu.edu

It has been widely recognized that fundamental biological processes such as receptor sensing, cell redox respiration, and enzymatic reactions are associated with changes in protein structure that are often propagated over a considerable distance. Unraveling the mechanism of how such conformational changes are generated and transmitted is of major interest for understanding regulatory function, kinetics and recognition properties of proteins. My research project focuses on the application of time-resolved absorption and fluorescence spectroscopy together with novel photothermal techniques (photoacoustic calorimetry and photothermal beam deflection) to unravel signaling mechanisms in calcium-binding proteins as well as to characterize the conformational dynamics associated with ligand or substrate binding to peroxidases and other heme proteins.

i) Mechanism of signal recognition and transduction in calcium binding proteins.

Calcium binding proteins represent an intriguing family of proteins. Despite the highlevel of sequential homology, the structural response to calcium binding varies significantly among the members of this family. Crystallographic and NMR studies have allowed enormous advances to be made in understanding the structural basis of the function of calcium transducers. However, little is known about the kinetics and energetics of conformational changes that are associated with the transition between the ligand-free and ligand-bound forms of calcium transducers. Elucidation of the relationship between protein structure, energetics, and dynamics is crucial not only for a detailed understanding of the signaling mechanism in calcium transducers, but also for the design of novel bio-mimetic calcium signaling systems.

ii) Dynamics of conformational changes associated with ligand and substrate interactions with lactoperoxidase.

Lactoperoxidase is a member of a large family of mammal peroxidases, which catalyze the oxidation of inorganic and organic substrates by peroxide. Despite the fact that conformational dynamics have been shown to play an important role in regulating ligand association to oxygen-binding heme proteins, little is known about the dynamics and energetics of conformational changes associated with the catalytic cycle in peroxidases, including ligand or substrate migration through the protein matrix. Understanding of the mechanism of substrate interaction with lactoperoxidse is of broad interest taking into account that this enzyme can also catalyze peroxidation of substrates that re regarded as important breast cancer risk factors.