4MXL

X-ray structure of ZnPFeBMb1

4MXL の概要

• エントリーDOI: 10.2210/pdb4mxl/pdb
• 関連するPDBエントリー: 4MXK
• 分子名称: Myoglobin, PROTOPORPHYRIN IX CONTAINING ZN (3 entities in total)
• 機能のキーワード: globin fold, oxygen transport
• 由来する生物種: Physeter catodon (Sperm whale)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17906.95

構造登録者

Chakraborty, S.,Lu, Y.,Petrik, I. (登録日: 2013-09-26, 公開日: 2014-02-12, 最終更新日: 2024-02-28)

主引用文献

Chakraborty, S.,Reed, J.,Ross, M.,Nilges, M.J.,Petrik, I.D.,Ghosh, S.,Hammes-Schiffer, S.,Sage, J.T.,Zhang, Y.,Schulz, C.E.,Lu, Y.
Spectroscopic and computational study of a nonheme iron nitrosyl center in a biosynthetic model of nitric oxide reductase.
Angew.Chem.Int.Ed.Engl., 53:2417-2421, 2014

PubMed Abstract: A major barrier to understanding the mechanism of nitric oxide reductases (NORs) is the lack of a selective probe of NO binding to the nonheme FeB center. By replacing the heme in a biosynthetic model of NORs, which structurally and functionally mimics NORs, with isostructural ZnPP, the electronic structure and functional properties of the FeB nitrosyl complex was probed. This approach allowed observation of the first S=3/2 nonheme {FeNO}(7) complex in a protein-based model system of NOR. Detailed spectroscopic and computational studies show that the electronic state of the {FeNO}(7) complex is best described as a high spin ferrous iron (S=2) antiferromagnetically coupled to an NO radical (S=1/2) [Fe(2+)-NO(.)]. The radical nature of the FeB -bound NO would facilitate N-N bond formation by radical coupling with the heme-bound NO. This finding, therefore, supports the proposed trans mechanism of NO reduction by NORs.

PubMed: 24481708
DOI: 10.1002/anie.201308431

実験手法

X-RAY DIFFRACTION (1.5 Å)