3NVU

Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion

3NVU の概要

• エントリーDOI: 10.2210/pdb3nvu/pdb
• 関連するPDBエントリー: 1U55 3NVR
• 分子名称: Methyl-accepting chemotaxis protein, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (5 entities in total)
• 機能のキーワード: h-nox, hemoprotein, heme, signaling protein
• 由来する生物種: Thermoanaerobacter tengcongensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45375.36

構造登録者

Olea Jr., C.,Kuriyan, J.,Marletta, M.A. (登録日: 2010-07-08, 公開日: 2010-09-08, 最終更新日: 2024-02-21)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.038 Å)