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

Emily Weinert, Christine M. Phillips-Piro, Michael A. Marletta

Research output: Contribution to journalArticle

8 Citations (Scopus)

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 (~ 40 mV) 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.

Original languageEnglish (US)
Pages (from-to)7-12
Number of pages6
JournalJournal of Inorganic Biochemistry
Volume127
DOIs
StatePublished - Jul 11 2013

Fingerprint

Hemeproteins
Porphyrins
Scaffolds
Oxidation-Reduction
Gases
Ligands
Carbon Monoxide
Phenylalanine
Engineers

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Inorganic Chemistry

Cite this

Weinert, Emily ; Phillips-Piro, Christine M. ; Marletta, Michael A. / Porphyrin π-stacking in a heme protein scaffold tunes gas ligand affinity. In: Journal of Inorganic Biochemistry. 2013 ; Vol. 127. pp. 7-12.
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Porphyrin π-stacking in a heme protein scaffold tunes gas ligand affinity. / Weinert, Emily; Phillips-Piro, Christine M.; Marletta, Michael A.

In: Journal of Inorganic Biochemistry, Vol. 127, 11.07.2013, p. 7-12.

Research output: Contribution to journalArticle

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