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J Inorg Biochem. 2013 Oct;127:7-12. doi: 10.1016/j.jinorgbio.2013.06.004. Epub 2013 Jun 15.

Porphyrin π-stacking in a heme protein scaffold tunes gas ligand affinity.

Author information

1
Department of Chemistry, Emory University, Atlanta, GA 30322, United States.

Abstract

The role of π-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 π-stacking within a heme protein scaffold. Removal of a phenylalanine-porphyrin π-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 π-stacking may provide a novel route to engineer heme protein properties for new functions.

KEYWORDS:

Bioinorganic chemistry; H-NOX; Heme proteins; Pi interactions; Porphyrins; Redox chemistry

PMID:
23831583
PMCID:
PMC3773300
DOI:
10.1016/j.jinorgbio.2013.06.004
[Indexed for MEDLINE]
Free PMC Article

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