Structure and function relationships in hemeproteins, like the unique hemoglobin I from Lucina pectinata. For example, using “site directed mutagenesis” we tailor the structure of this hemoglobin. Its chemical structure is then studied by Fourier Transform infrared, resonance Raman vibrational analysis, and NMR spectroscopies. This is followed by the kinetic study of the reaction between hemoglobin and ligands (for example, O2, CO, NO, and H2S) using time – resolved (pump and probe) infrared and resonance Raman techniques. Ultrafast geminate chemical dynamics are studied also in our laboratory using time - resolved (pump and probe) picosecond and femtosecond spectroscopy.
Research Project
The project involves the use of the unusual hemoglobin from the tropical clam L. pectinata as a model system to study the relationship between chemical structure, reactivity and function of heme proteins with hydrogen peroxide
Selected Publications:
Evidence for nonhydrogen bonded compound II in cyclic reaction of hemoglobin I from Lucina pectinata with hydrogen peroxide. De Jesus-Bonilla, Walleska; Ramirez-Melendez, Eunice; Cerda, Jose; Lopez-Garriga, Juan. Chemistry Department, University of Puerto Rico, Mayaguez, P. R. Biopolymers (2002), 67(3), 178-185.
Expression and purification of recombinant hemoglobin I from Lucina pectinata. Rosado-Ruiz, Tanya; Antommattei-Perez, Frances M.; Cadilla, Carmen L.; Lopez-Garriga, Juan. Chemistry Department, University of Puerto Rico, Mayaguez, P. R. Journal of Protein Chemistry (2001), 20(4), 311-315.
Formation of Compound I and Compound II Ferryl Species in the Reaction of Hemoglobin I from Lucina pectinata with Hydrogen Peroxide. De Jesus-Bonilla, Walleska; Cortes-Figueroa, Jose E.; Souto-Bachiller, Fernando A.; Rodriguez, Lolita; Lopez-Garriga, Juan. Chemistry Department, University of Puerto Rico, Mayaguez, P. R. Archives of Biochemistry and Biophysics (2001), 390(2), 304-308
