Porphyrin π-stacking in a heme protein scaffold tunes gas ligand affinity.
Porphyrin π-stacking in a heme protein scaffold tunes gas ligand affinity.
复制标题
血红素蛋白支架中的卟啉α-堆积可调节气体配体亲和力。
DOI：
10.1016/j.jinorgbio.2013.06.004
复制
发表时间：
2013
影响因子：
3.9
通讯作者：
Marletta,MichaelA
中科院分区：
文献类型：
--
作者：
Weinert,EmilyE;Phillips-Piro,ChristineM;Marletta,MichaelA
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.
