1GED

A positive charge route for the access of nadh to heme formed in the distal heme pocket of cytochrome p450nor

1GED の概要

• エントリーDOI: 10.2210/pdb1ged/pdb
• 分子名称: CYTOCHROME P450 55A1, BROMIDE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: cytochrome p450nor, nitric oxide reductase, oxidoreductase
• 由来する生物種: Fusarium oxysporum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45196.99

構造登録者

Kudo, T.,Takaya, N.,Park, S.-Y.,Shiro, Y.,Shoun, H. (登録日: 2000-11-02, 公開日: 2000-11-22, 最終更新日: 2023-10-25)

主引用文献

Kudo, T.,Takaya, N.,Park, S.-Y.,Shiro, Y.,Shoun, H.
A positively charged cluster formed in the heme-distal pocket of cytochrome P450nor is essential for interaction with NADH
J.Biol.Chem., 276:5020-5026, 2001

PubMed Abstract: Arg and Lys residues are concentrated on the distal side of cytochrome P450nor (P450nor) to form a positively charged cluster facing from the outside to the inside of the distal heme pocket. We constructed mutant proteins in which the Arg and Lys residues were replaced with Glu, Gln, or Ala. The results showed that this cluster plays crucial roles in NADH interaction. We also showed that some anions such as bromide (Br(-)) perturbed the heme environment along with the reduction step in P450nor-catalyzed reactions, which was similar to the effects caused by the mutations. We determined by x-ray crystallography that a Br(-), termed an anion hole, occupies a key region neighboring heme, which is the terminus of the positively charged cluster and the terminus of the hydrogen bond network that acts as a proton delivery system. A comparison of the predicted mechanisms between the perturbations caused by Br(-) and the mutations suggested that Arg(174) and Arg(64) play a crucial role in binding NADH to the protein. These results indicated that the positively charged cluster is the unique structure of P450nor that responds to direct interaction with NADH.

PubMed: 11076941
DOI: 10.1074/jbc.M007244200

実験手法

X-RAY DIFFRACTION (2 Å)