TY - JOUR
T1 - Porphyrin π-stacking in a heme protein scaffold tunes gas ligand affinity
AU - Weinert, Emily E.
AU - Phillips-Piro, Christine M.
AU - Marletta, Michael A.
N1 - Funding Information:
Funding for this research was provided by the National Institutes of Health National Heart, Lung, and Blood Institute Award F32L090174 (E.E.W.), NIH grant GM 070671 (M.A.M.), and a grant from the Rogers Family Foundation (M.A.M.). We are grateful to Dr. Charlotte Whited, Professor Harry Gray, Dr. Jay Winkler and the Beckman Institute Laser Resource Center at the California Institute of Technology for assistance with on-rate measurements, Professor John Kuriyan for use of crystallography equipment, Dr. Michael Winter for helpful discussions and members of the Marletta laboratory for discussions and critical reading of this manuscript.
PY - 2013
Y1 - 2013
N2 - 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.
AB - 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.
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U2 - 10.1016/j.jinorgbio.2013.06.004
DO - 10.1016/j.jinorgbio.2013.06.004
M3 - Article
C2 - 23831583
AN - SCOPUS:84879832467
SN - 0162-0134
VL - 127
SP - 7
EP - 12
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
ER -