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Reza Razeghifard, Ph.D.

Reza Razeghifard
Department Chair
Associate Professor 
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.

  1. Razeghifard R., Microalgae for Energy, in: Kirk-Othmer Encyclopedia of Chemical Technology, John Wiley & Sons, Inc., 2016, pp. doi: 10.1002/0471238961.koe0471200019.
  2. Razeghifard R. Photochemistry of free and bound Zn-chlorophyll analogues to synthetic peptides depend on the quinone and pH. J Photochem Photobiol B. 2015 Jul 23. pii: S1011-1344(15)00232-8. doi: 10.1016/j.jphotobiol.2015.07.013.
  3. Razeghifard, Reza; Chiafair, Catherine E.; Giarikos, Dimitrios G. A P450 Metabolism Experiment for Undergraduate Biochemistry Laboratories. J Chem. Edu.  2014 91(1): 141-144
  4. Razeghifard, R. Artificial Photosynthesis. Natural and artificial photosynthesis: solar power as an energy source, 2013 John Wiley & Sons, Ed. Razeghifard, R.
  5. Razeghifard R. Algal biofuels. Photosynth Res. 2013 117(1-3): 207-19
  6. Giarikos, Dimitrios G.; Patel, Sagir; Lister, Andrew; Razeghifard R. Incorporation of Gas Chromatography-Mass Spectrometry into the Undergraduate Organic Chemistry Laboratory Curriculum. J Chem. Edu.  2013 90(1): 106-109
  7. Kim, Eun-Ha; Li, Xiao-Ping; Razeghifard, Reza; et al. The multiple roles of light-harvesting chlorophyll a/b-protein complexes define structure and optimize function of Arabidopsis chloroplasts: A study using two chlorophyll b-less mutants. Biochimica et Biophysica Acta-Bioenergetics 2009 1787(8): 973-984
  8. Razeghifard  R  Artificial Photoactive Proteins. Photosynthesis Research 2008 98: 677-685.
  9. Davydov R, Razeghifard R, Im S-C, Waskell L, Hoffman BM . Characterization of the Microsomal Cytochrome P450 2B4 O2 Activation Intermediates by Cryoreduction and Electron Paramagnetic Resonance. Biochemistry 2008 47(36): 9661-9666.
  10. Razeghifard R, Wallace BB, Pace RJ, Wydrzynski T.  Creating functional artificial proteins. Curr Protein Pept Sci. 2007 8(1): 3-18.  
  11. Kim EH, Razeghifard R, Anderson JM, Chow WS. Multiple sites of retardation of electron transfer in Photosystem II after hydrolysis of phosphatidylglycerol. Photosynth Res. 2007 93(1-3): 149-58.
  12. Hughes JL, Razeghifard R, Logue M, Oakley A, Wydrzynski T, Krausz E. Magneto-optic spectroscopy of a protein tetramer binding two exciton-coupled chlorophylls. J Am Chem Soc. 2006 128(11): 3649-58.  
  13. Razeghifard R, Wydrzynski T . Protein-Based Artificial Photosynthetic Reaction Centers. Photosynthesis: From Basic Biology to Industrial Application 2005 Editors A. Collings & C. Critchley, Wiley Publisher.  Chapter 7, 127-145.
  14. Razeghifard MR, Chen M, Hughes JL, Freeman J, Krausz E, Wydrzynski T. Spectroscopic studies of photosystem II in chlorophyll d-containing Acaryochloris marinaBiochemistry. 2005 44(33): 11178-87.
  15. Razeghifard MR, Kuzek D, Pace RJ. EPR kinetic studies of the S-1 state in spinach thylakoids. Biochim Biophys Acta. 2005 1708(1): 35-41.
  16. Razeghifard MR. On-column refolding of recombinant human interleukin-4 from inclusion bodies. Protein Expr Purif. 2004 37(1): 180-186.
  17. Razeghifard MR, Wydrzynski T. Binding of Zn-chlorin to a synthetic four-helix bundle peptide through histidine ligation. Biochemistry. 2003 42(4): 1024-30.
  18. Whitten ST, Wooll JO, Razeghifard R, García-Moreno E B, Hilser VJ. The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins. J Mol Biol. 2001 309(5): 1165-75.  
  19. Hutchison RS, Steenhuis JJ, Yocum CF, Razeghifard MR, Barry BA. Deprotonation of the 33-kDa, extrinsic, manganese-stabilizing subunit accompanies photooxidation of manganese in photosystem II. J Biol Chem. 1999 274(45): 31987-95.
  20. Kim S, Ayala I, Steenhuis JJ, Gonzalez ET, Razeghifard MR, Barry BA . Infrared Spectroscopic Identification of the C-O Stretching Vibration Associated with the Tyrosyl Z and D Radicals in Photosystem II. Biochim. Biophys. Acta (1998) 1366 (3): 330-354.
  21. Razeghifard MR, Pace RJ. EPR kinetic studies of oxygen release in thylakoids and PSII membranes: a kinetic intermediate in the S3 to S0 transition. Biochemistry. 1999 38(4): 1252-7.
  22. Razeghifard MR, Kim S, Patzlaff JS, Hutchison RS, Krick T, Ayala I, Steenhuis JJ, Boesch SE, Wheeler RA, Barry BA. In vivo, in vitro, and calculated vibrational spectra of plastoquinone and the plastosemiquinone anion radical. J. Phys. Chem B. (1999) 103 (44), 9790-9800.
  23. Razeghifard MR, Pace RJ. Electron paramagnetic resonance kinetic studies of the S states in spinach PSII membranes. Biochim Biophys Acta. 1997 1322 (2-3): 141-150
  24. Razeghifard MR, Wydrzynski T, Pace RJ, Burnap RL. Yz reduction kinetics in the absence of the manganese-stabilizing protein of photosystem II.  Biochemistry 1997 36(47): 14474-8.
  25. Razeghifard MR, Klughammer C, Pace RJ.  Electron paramagnetic resonance kinetic studies of the S states in spinach thylakoids. Biochemistry 1997 36(1): 86-92.
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