Hemeteam Research Overview

Hemeteam Research involves, exclusively, Heme Proteins. At present we focus our efforts on Heme-containing Oxygen Sensing and Signalling proteins and the Cytochrome c Peroxidase from S. cerevisiae

Heme Oxygen Sensing Protein

Dr. Satterlee’s group produces isolates recombinant Heme-containing oxygen sensing and signalling proteins that govern important biological processes. Members of this multi-domain group of proteins are: (a) FixLs from two members of the genus rhizobi a (abbreviated Bj and Sm), (b) Dos from E. coli, and (c) HemeAT from B. subtilis . Depending on the development of each of these on-going projects we produce variants, or constructs that are tailored specifically to answer the question of how these combined sensing and signalling proteins function.

All of these proteins function similarly and all are multi-domain proteins, possessing similar primary sequence structures of the 2-3 domains. The multidomain structure of these oxygen sensors is illustrated using SmFixL as an example in the figure below.

Yeast Cytochrome c Peroxidase

The cytochrome c peroxidase (CcP) from the yeast s. cerevisiae is a monomer Heme enzyme that catalyzes the oxidation of ferrocytochrome c via the decomposition of of hydrogen peroxide. CcP is found in yeast mitochondria, the cell's powerhouse, where the "mitochondrial electron transport chain" ultimately reduces oxygen to water. The precise details of the CcP peroxidase mechanism is being studied using recombinant CcP mutants. Since CcP functions via electron-transfer complexes with ferrocytochrome c, we also study the dynamics and stoichiometry of these protein-protein complexes.