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Reza Razeghifard, Ph.D.

Reza Razeghifard
Professor and Department Chair
Dept. of Chemistry and Physics
(954) 262-7930

Previous Academic Experiences

  • University of Michigan  October 2005-July 2007. Research Lab Specialist-Department of Anesthesiology.
  • Australian National University   January 2001-August 2004. Academic Level B Research Fellow-Research School of Biological Sciences.
  • University of Texas Medical Branch   August 1999-January 2001. Postdoctoral Research Associate-Department of Human Biological Chemistry & Genetics.
  • University of Minnesota  March 1997-January 1999. Postdoctoral Research Associate-Department of Biochemistry.

Area(s) of Research

Protein Engineering

The goal of this project is to design and synthesize photoactive peptides inspired by natural photosynthetic systems.  Learning from photosynthetic reaction centers, we plan to synthesize chlorin pigments through organic chemistry and introduce them into peptides.  Compounds such as quinones will be used as electron acceptors to allow repetitive light oxidations of the chlorin pigment.  This will provide us with a powerful tool to exploit not only the significance of the local protein environment but also the significance of dimerization on the photo-activity of chlorin.  The key advantage of this synthetic approach is that the peptide scaffold can be readily modified. Such photoactive peptides can then be incorporated into membranes and coupled to redox-requiring processes for biotechnological applications, such as artificial photosynthesis. 

P450 Enzyme

Cytochrome P450 enzymes are ubiquitous superfamily of multi-functional oxidases with important catalytic roles including the metabolism of xenobiotics such as drugs and environmental pollutants, and biosynthesis of steroids and fat-soluble vitamins. The P450 catalytic mechanism is typically described by four steps based on the state of heme iron and oxygen.  However, the detailed catalytic mechanism is not knownreactive intermediates are very unstableIn the first step, oxygen binds to the reduced heme iron forming oxyferrous complex. This is followed by one-electron reduction of the oxyferrous complex to a ferric peroxo which is easily protonated to form the hydroperoxo species.  The second protonation causes the formation a Fe-OOH2 intermediate that undergoes heterolytic scission of the O-O bond and as a result a water molecule is released. The remaining so-called ferryl-oxo p-cation porphyrin radical complex referred to as “Compound I” is responsible for hydroxylation of substrate to form a product complex.  Our goal is to find efficient substrates for this enzyme in terms of high coupling and binding affinity.  


The world is facing an energy crisis and environmental issues due to the depletion of fossil fuels and increasing levels of CO2 in the atmosphere. Growing algae offers one practical solution for these global issues because they capture CO2 and store it in high energy biomass compounds using photosynthesis. Their biomass contains a large percentage of oils that can be converted into biofuel. This oil producing ability of algae can be controlled to maximize biofuel production by changing their growth conditions. Our goal is to generate new strains of microalgae capable of producing high amounts of lipids (oil) under extreme growth conditions. These conditions are needed to avoid contamination from bacteria and fungi when algae are grown in open systems for mass production.

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