Iron-Mediated NOX Chemistry: Relevance to the Global Nitrogen Cycle

Friday, April 5, 2019

Prof. George B. Richter-Addo

Department of Chemistry & Biochemistry

The University of Oklahoma

Reception: 3:00PM Hand 1135

Seminar: 3:30PM Hand 1144

Abstract: The simple nitrogen oxides (NOx) are employed in biology to serve many functions in human health, and some of these functions are enabled by heme proteins.  Heme proteins have evolved to select combinations of (i) distal pocket amino acids, (ii) metal, and (iii) macrocycle (e.g., porphyrin vs chlorin) to help achieve specific interactions with incoming NOx ligands that promote their metabolic activation.  NO is a known vasodilator that requires a heme protein for its function, and the small molecule HNO is biologically relevant in its interactions with heme proteins. Similarly, the alkyl/aryl nitroso compounds (RNO) are biologically relevant species that interact with heme to inhibit protein function.  Our recent findings on the role of the heme proteins such as Mb and Hb in directing their interactions with various NOx species will be presented. In addition, our findings on the generation and reactivity of heme model–HNO/RNO compounds, as well as their roles in N–N bond forming reactions to generate N2O of relevance to the global N cycle will be presented for discussion.

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