POWRE: Heteronuclear NMR Studies on a Soluble Heme Oxygenase

University Of Maryland At Baltimore, Baltimore

Investigators

Abstract

0074609 Wilks The objective of this POWRE grant is for the PI to develop expertise in triple resonance multidimensional nuclear magnetic resonance (NMR) methods to answer fundamental questions on the role of protein structure and dynamics in heme reactivity. She will learn these techniques in the laboratory of a colleague at her institution. Heteronuclear NMR will enable her to determine the three dimensional structure of the protein as well as changes in atomic resolution dynamics and its role in redox based heme reactivity. This laboratory is investigating the mechanism of iron release from heme by heme oxygenase. This enzyme uses heme as the substrate and the prosthetic group. This lab is particularly interested in determining the role the protein environment has in modulating the reactivity of the heme. The information obtained from using heteronuclear NMR will expand knowledge in the protein structure as it relates to heme reactivity.