3NVR

Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion

Summary for 3NVR

• Entry DOI: 10.2210/pdb3nvr/pdb
• Related: 1U55 3NVU
• Descriptor: Methyl-accepting chemotaxis protein, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (5 entities in total)
• Functional Keywords: h-nox, hemoprotein, heme cofactor, signaling protein
• Biological source: Thermoanaerobacter tengcongensis
• Total number of polymer chains: 2
• Total formula weight: 45462.88

Authors

Olea Jr., C.,Kuriyan, J.,Marletta, M.A. (deposition date: 2010-07-08, release date: 2010-09-08, Last modification date: 2024-02-21)

Primary citation

Olea, C.,Kuriyan, J.,Marletta, M.A.
Modulating heme redox potential through protein-induced porphyrin distortion
J.Am.Chem.Soc., 132:12794-12795, 2010

PubMed Abstract: Hemoproteins are ubiquitous in biology and are commonly involved in critical processes such as electron transfer, oxidative phosphorylation, and signal transduction. Both the protein environment and the heme cofactor contribute to generate the range of chemical properties needed for these diverse functions. Using the heme nitric oxide/oxygen binding (H-NOX) protein from the thermophilic bacterium Thermoanaerobacter tengcongensis, we have shown that heme electronic properties can be modulated by porphyrin distortion within the same protein scaffold without changing the heme ligation state or heme environment. The degree of heme distortion was found to be directly correlated to the electron density at the heme iron, as evidenced by dramatic changes in the heme redox potential and pK(a) of the distal ligand ((-)OH vs H(2)O). Protein-induced porphyrin distortion represents a new strategy to rationally tune the electronic properties of protein-bound porphyrins and could be used to engineer proteins with desired reactivity or functionality.

PubMed: 20735135
DOI: 10.1021/ja106252b

Experimental method

X-RAY DIFFRACTION (2.148 Å)