Jose Cerda, Ph.D.
Associate Professor, Director of Chemical Biology
Office: Science Center 306
Phone: (610) 660-1787
Fax: (610) 660-1783
Dr. Cerda earned a B.S. in Chemical Engineering and a M.S. in Chemistry at the University of Puerto Rico at Mayagüez. He continued his education at Michigan State University where he received a Ph.D. in Physical Chemistry. In his graduate research, Dr. Cerda studied the structure of heme proteins by using resonance Raman spectroscopy under the guidance of Dr. Gerald T. Babcock. As a postdoctoral research associate, Dr. Cerda worked with Dr. P. Leslie Dutton at the University of Pennsylvania where he investigated the properties of redox cofactors by using electrochemical techniques. He worked on free natural/synthetic cofactors and measured the effects from the surrounding medium (solvent or synthetic protein) on the electrochemical properties of these redox cofactors. In 2008, Dr. Cerda joined the faculty of Department of Chemistry at Saint Joseph's University. His current research involves the use of electrochemical methods in the study of redox proteins and redox cofactors.
- B.S. University of Puerto Rico at Mayagüez 1994 (Chemical Engineering)
- M.S. University of Puerto Rico at Mayagüez 1997 (Chemistry)
- Ph.D. Michigan State University 2002 (Physical Chemistry)
- CHM 120 General Chemistry I
- CHM 125 General Chemistry II
- CHM 120L General Chemistry Lab I
- CHM 125L General Chemistry Lab II
- CHM 320 Physical Chemistry for Chemical Biology
- CHM 310 Physical Chemistry I
- CHM 315 Physical Chemistry II
- CHM 310L Physical Chemistry Lab I
*SJU undergraduate students in references 2, 3, 4, and 6.
1. “Extended Scope Synthesis of an Artificial Safranin Cofactor” Gheevarghese Raju, Sunaina Singh, Andrew C. Mutter, Bernard Everson, Jose F. Cerda, Ronald L.Koder. Tetrahedron Letters 2014 (55) 2487-2491.
2. “Heme Peripheral Groups Interactions in Extremely Low-Dielectric Constant Media and their Contributions to the Heme Reduction Potential” Jose F. Cerda*, Mary C. Malloy, Brady O. Werkheiser, Alaina T. Stockhausen, Michael F. Gallagher, and Andrew C. Lawler. Inorganic Chemistry 2014, 53 (1), 182–188 .
3. “Electrochemical Determination of Heme-Linked pKas and the Importance of Using Fluoride Binding in Heme Proteins” Jose F. Cerda, Margaret H. Roeder, Danielle N. Houchins, Carmen X. Guzman, Emily J. Amendola, Jacquelyn D. Castorino, and Andrea L. Fritz. Analytical Biochemistry 2013 (443) 75-77.
4. “Spectroelectrochemical measurements of redox proteins by using a simple UV/visisble cell” Jose F. Cerda, Carmen X. Guzman, Haibo Zhang, Emily J. Amendola, Jacquelyn D. Castorino, Nina Millet, Andrea L. Fritz, Danielle N. Houchins, and Margaret H. Roeder. Electrochemistry Communications 2013 (33) 76-79.
5. “A three-dimensional printed cell for rapid, low-volume spectroelectrochemistry” Joseph M. Brisendine, Andrew C. Mutter, Jose F. Cerda, and Ronald L. Koder. Analytical Biochemistry 2013, (439) 1-3.
6. “Manipulating Reduction Potentials in an Artificial Safranin Cofactor” Gheevarghese Raju, Joseph Capo, Bruce R. Lichtenstein, Jose F. Cerda, Ronald L. Koder. Tetrahedron Letters 2012, (53), 1201-1203.
7. “Electrochemical and Structural Coupling of the Naphthoquinone Amino Acid” Bruce R. Lichtenstein, Veronica R. Moorman, José F. Cerda, A. Joshua Wand and P. Leslie Dutton. Chemical Communications 2012,(48) 1997–1999.
8. “Reversible Proton Coupled Electron Transfer in a Peptide-incorporated Naphthoquinone Amino Acid” Bruce R. Lichtenstein, Jose F. Cerda, Ronald L. Koder, P. Leslie Dutton. Chemical Communications 2009, 168–170
9. “Hydrogen Bond-free Flavin Redox Properties: Managing Flavins in Extreme Aprotic solvents” Jose F. Cerda, Ronald L. Koder, Bruce R. Lichtenstein, Christopher C. Moser, Anne F. Miller, P. Leslie Dutton. Organic & Biomolecular Chemistry 2008, 6, 2204-2212.
10. “A Flavin Analogue with Improved Solubility in Organic Solvents” Ronald L. Koder, Bruce R. Lichtenstein, Jose F. Cerda, Anne F. Miller, P. Leslie Dutton. Tetrahedron Letters 2007, 48, 5517-5520.
11. “Structural Specificity in Designed Four -helix Bundles Driven by Buried Polar Interactions” Ronald L. Koder, Kathleen G. Valentine, Jose Cerda, Dror Noy, A. Joshua Wand and P. Leslie Dutton. Journal of the American Chemical Society 2006 (128) 14450-14451.
12. “Hydrogen-bonding conformations of tyrosine B10 tailor the hemeprotein reactivity of ferryl species” Waleska De Jesus-Bonilla, Anthony Cruz, Ariel Lewis, Daniel, E. Barcelo, Jose F. Cerda, Carmen L. Cadilla, Juan Lopez-Garriga. Journal of Biological Inorganic Chemistry 2006 (11) 334-342.
13. “Evidence for Nonhydrogen Bonded compound II in Cyclic Reaction of Hemoglobin I from Lucina pectinata with Hydrogen Peroxide” Waleska De Jesus-Bonilla, Eunice Ramirez-Melendez, Jose F. Cerda, Juan Lopez-Garriga. Biopolymers 2002 (67) 178 -185.
14. “Interaction of Nitric Oxide with Prostaglandin Endoperoxide H Synthase-1: Implications for Fe-His Bond Cleavage in Heme Proteins” Johannes P. M. Schelvis, Steve A. Seibold, Jose F. Cerda, R. Michael Garavito, and Gerald T. Babcock. The Journal of Physical Chemistry B 2000 (104)10844-10850.
15. “Peroxidase Activity in Prostaglandin Endoperoxide H Synthase-1 Occurs with a Neutral Histidine Proximal Heme Ligand” Steve A. Seibold, Jose F. Cerda, Anne M. Mulichak, Inseok Song, R. Micheal Garavito, Toshiya Arakawa, William L. Smith and Gerald T. Babcock. Biochemistry 2000 (39) 6616 – 6624.
16. “Spectroscopic Characterization of the Heme-Binding Sites in Plasmodium faciparum Histidine-Rich Protein 2" Clara Y. H. Choi, Jose F. Cerda, Hsiu-An Chu, Gerald T. Babcock and Michael A. Marletta. Biochemistry 1999 (38) 16916-16924.
17. “Resonance Raman Studies of the Heme-Ligand Active Site of Hemoglobin I from Lucina pectinata” Jose Cerda, Yolanda Echevarria, Erick Morales and Juan Lopez-Garriga. Biospectroscopy 1999 (5) 289-301.
18. “Orientation of the Heme Vinyl Groups in the Hydrogen Sulfide-Binding Hemoglobin I from Lucina pectinata” Eilyn Silfa, Maritza Almeida, Jose Cerda, Shaoxiong Wu and Juand Lopez-Garriga. Biospectroscopy 1998 (4) 311-326.
19. “Unusual Rocking Freedom of the Heme in the Hydrogen Sulfide-Binding Hemoglobin from Lucina pectinata” Jose F. Cerda-Colon, Eilyn Silfa and Juan Lopez-Garriga. Journal of the American Chemical Society 1998 (120) 9312-9317.
20. “Structural characterization and dynamic events in hemoglobin I from Lucina pectinata: Unusual conformation of propionates and vinyl’s peripheral groups” Eilyn Silfa, Maritza Almeida, Jose Cerda, S. Wu, and Juan Lopez-Garriga. Spectroscopy Biology Molecular Trends 1997 79-80.
21. “Resonance Raman Studies of an Unusual Hemoglobin (HbI) from Lucina pectinata” Yolanda Echevarria, Jose Cerda, Jorge Colon and Juan Lopez-Garriga. XVth International Conference on Raman Spectroscopy 1996 456-457.
The main application in my research lab is UV-vis spectroelectrochemistry. The initial design of the electrochemical cell (shown below) was first started at the University of Pennsylvania, when I was a post-doctoral research assistant in the Dutton lab. At SJU, I have been able to optimize the setup into a robust and powerful technique for the study of redox proteins. The UV-vis spectroelectrochemical setup allows the measurement of the midpoint potential (Em) of a redox compound by using UV-vis spectroscopic measurements. The setup is the culmination of both of my research backgrounds in protein spectroscopy and electrochemistry. The technique consists in providing the cell potential (Eapp), via the use of electrodes, and simultaneously measuring the UV-vis absorption of the redox compound. The absorption of the sample is then plotted versus the applied potential (Eapp) and the Nernst equation is used to determine the Em of the compound. Also, with the Nernst fit, the number of electrons that are involved in the redox reaction can be determined. Further details of this setup and its application to redox proteins can be found in reference 4 of the publication list.
Electrochemical studies of heme-bound fluoride proteins
The UV-vis spectroelectrochemical setup has also been used to establish a method to study the heme cofactor and its surrounding protein structure. Fluoride has been known to bind to many heme proteins in their oxidized state (Fe3+). Past studies of heme-bound fluoride complexes have only focused on the spectroscopic properties of the heme protein in the presence of fluoride. In our research, we measure the Em of heme proteins in the presence of heme-bound fluoride complexes. In myoglobin, the oxidized form contains a water molecule in the sixth ligand position. Addition of fluoride results in the substitution of the water ligand for a heme-bound fluoride ion. The advantage of using fluoride is that it has similar electronic properties as the water ligand; both are high spin ligands that cannot bind to the ferrous heme ion. Therefore, upon comparison between the heme protein without fluoride and with fluoride, any changes in Em can mainly be ascribed to changes in the oxidized state.
The study of heme cofactors in aprotic solvents
This research project consists in the study of the electrochemical properties of heme cofactors in aprotic solvent and the effects of proton interactions on the heme reduction potential.
One of the most interesting topics in the field of bioenergetics is the proton pump in enzymes such as cytochrome c oxidase and cytochrome bc1. These enzymes utilize redox energy for proton translocation that results in a proton gradient across the mitochondrial membrane. This stored electrochemical energy is then used to form ATP, the energy currency of metabolism. The functioning of the proton pump in CcO is a source of controversy because of its complexity, but it has been suggested that the heme a peripheral groups are involved in the proton pumping mechanism. Heme peripheral groups have also been shown to be involved in various heme-protein interactions in many other proteins.
However, quantification of theses interactions is difficult because the protein itself is involved in various interactions (hydrogen bonding, electrostatic attraction/repulsion, pi-pi stacking, and hydrophobic stabilization) with the heme. In order to study a particular interaction, a model heme must be devoid of the other interactions. Quantification can be performed on a heme model compound in an aprotic solvent, such as dichloromethane (CH2Cl2) or benzene, with a ligand that can singularly interact with one of its peripheral groups. The low-dielectric constants of these solvents, 8.9 and 2.3 for CH2Cl2 and benzene, respectively, make them ideal media to study hemes in because the interior of proteins can have dielectric constant values as low as 2.5.
The properties of these solvents facilitate the evaluation of hydrogen bonding and electrostatic interactions between ligands and the peripheral groups of hemes. Small heme-ligand interactions, perhaps too small to be measured in commonly-used solvents, can be magnified in benzene and dichloromethane. Using this approach, we recently carried out an electrochemical study on the effects of the ionization of the heme propionates (propionic acids) on the reduction potentials of heme b and heme a in low-dielectric constant media. We also measured the electrochemical contribution of the H-bond to the formyl group on the reduction potential of heme a. Our results show that ionization of the heme propionates in heme b and heme a cause an overall decrease in the heme reduction potential of about -100 mV in CH2Cl2 in the absence of electrolyte. Furthermore, H-bonding between trichloroethanol (TCE) and the heme a formyl group increases the heme reduction potential by about +50 mV in CH2Cl2 without electrolyte. This means that reduction of ionized heme a in CH2Cl2 can lead to an overall change of at least +150 mV.
SJU Summer Scholars Program
Most of the research in our lab has been carried out by students that got their first independent research experience under the sponsorship of the Summer Scholars Program. The following are some of our recent groups.
Jacquelyn Castorino, Michael Gallagher, and Emily Amendola
Victoria Angelucci, Meg Roeder, Kate McGovern, Mary Malloy, Brady Werkheiser, and Danielle Houchins.
Megan Forman, Alaina Stockhausen, Mary Malloy, and Victoria Angelucci
Joshua Middlecamp, Daniel Walz, Kyle Smith, Alaina Stockhausen, and Nicolette Wilkes