Welcome to the website of the Richter-Addo laboratory at the University of Oklahoma. Our work focuses on the biological inorganic chemistry of the simple nitrogen oxides NOx, and we pay special attention to the interactions of these NOx species with heme proteins and model hemes. We combine classical inorganic chemistry with complex protein biochemistry to examine how the iron center in proteins directs the physiological effects of nitrogen oxides. We welcome you to this site!
We are part of the Price Family Foundation Institute of Structural Biology.
Structural Biology of Heme Proteins
We utilize single-crystal macromolecular X-ray diffraction techniques to elucidate the role that Fe plays in the biological chemistry of NOx species. The proteins we normally use are myoglobin (Mb) and hemoglobin (Hb). We have demonstrated unique binding modes for both nitric oxide (NO) and nitrite to these proteins that helps to explain the physiological chemistry that these NOx species display. We use both in-house X-ray diffraction equipment and synchrotron-based (Brookhaven National Laboratory) techniques. More...
Electrochemistry and Spectroelectrochemistry
Electrochemistry is an excellent tool to study the generation and behavior of redox intermediates in chemical reactions. We have developed new methodology to make infrared and UV-vis spectroelectrochemistry more readily available to synthetic chemists. More...
Gas-phase Biomarker Detection
In collaboration with the McCann group in Electrical Engineering, we are developing new TDLAS methodology for the specific and simultaneous detection of nitric oxide (NO), 15-NO, and nitrous oxide (N2O; a nitroxyl dimerization product) from complex biochemical mixtures. More...
We are located in the Stephenson Life Sciences Research Center on the southeast side of the city of Norman.
The Richter-Addo laboratory, Department of Chemistry and Biochemistry, Stephenson Life Sciences Research Center, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019. Tel: +1-405-325-2378.