Structural highlights
Publication Abstract from PubMed
The role of pi-stacking in controlling redox and ligand binding properties of porphyrins has been of interest for many years. The recent discovery of H-NOX domains has provided a model system to investigate the role of porphyrin pi-stacking within a heme protein scaffold. Removal of a phenylalanine-porphyrin pi-stack dramatically increased O2, NO, and CO affinities and caused changes in redox potential (~40mV) without any structural changes. These results suggest that small changes in redox potential affect ligand affinity and that pi-stacking may provide a novel route to engineer heme protein properties for new functions.
Porphyrin pi-stacking in a heme protein scaffold tunes gas ligand affinity.,Weinert EE, Phillips-Piro CM, Marletta MA J Inorg Biochem. 2013 Jun 15;127C:7-12. doi: 10.1016/j.jinorgbio.2013.06.004. PMID:23831583[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weinert EE, Phillips-Piro CM, Marletta MA. Porphyrin pi-stacking in a heme protein scaffold tunes gas ligand affinity. J Inorg Biochem. 2013 Jun 15;127C:7-12. doi: 10.1016/j.jinorgbio.2013.06.004. PMID:23831583 doi:10.1016/j.jinorgbio.2013.06.004
