Heme nitric oxide and/or oxygen binding (H-NOX) proteins are involved in signaling pathways in a variety of bacteria, including functioning as O2-binding signaling proteins in the anaerobic bacterium, Thermoanaerobacter tengcongensis. Studies on the H-NOX domain from T. tengcongensis have shown that this protein can bind O2, NO, and CO gasses as ligands to the heme cofactor and that this protein is very amenable to both site-directed mutagenesis as well as incorporation of non-iron porphyrin cofactors. To further examine and tune the gas binding affinities of this protein, unnatural amino acids have been site-directly incorporated into the protein framework.

Exploring new avenues to tune gas ligand affinity in a sturdy heme binding protein

248th National Meeting (2014)

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