4FDK

F78L Tt H-NOX

Summary for 4FDK

• Entry DOI: 10.2210/pdb4fdk/pdb
• Related: 1U4H 1U55 1U56
• Descriptor: Methyl-accepting chemotaxis protein, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (4 entities in total)
• Functional Keywords: o2-sensor, signaling protein
• Biological source: Thermoanaerobacter tengcongensis
• Total number of polymer chains: 2
• Total formula weight: 45323.94

Authors

Weinert, E.E.,Phillips-Piro, C.M.,Marletta, M.A. (deposition date: 2012-05-28, release date: 2013-08-28, Last modification date: 2023-09-13)

Primary citation

Weinert, E.E.,Phillips-Piro, C.M.,Marletta, M.A.
Porphyrin pi-stacking in a heme protein scaffold tunes gas ligand affinity.
J.Inorg.Biochem., 127C:7-12, 2013

PubMed 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.

PubMed: 23831583
DOI: 10.1016/j.jinorgbio.2013.06.004

Experimental method

X-RAY DIFFRACTION (2.1 Å)