Protein scaffold of a heart11/10/2022 ![]() 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. 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. 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. 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.ĪB - The role of π-stacking in controlling redox and ligand binding properties of porphyrins has been of interest for many years. N2 - The role of π-stacking in controlling redox and ligand binding properties of porphyrins has been of interest for many years. Michael Winter for helpful discussions and members of the Marletta laboratory for discussions and critical reading of this manuscript. 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. Passariello, Marjorie Gayanilo, Hrishikesh Thakur, Joseph Dayan, Kimberly Dodge-Kafka, Michael S. ![]() Charlotte Whited, Professor Harry Gray, Dr. The scaffold protein muscle a-kinase anchoring protein orchestrates cardiac myocyte hypertrophic signaling required for the development of heart failure Michael D. T1 - Porphyrin π-stacking in a heme protein scaffold tunes gas ligand affinityįunding 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.). ![]()
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