2E2Y

Crystal Structure of F43W/H64D/V68I Myoglobin

2E2Y の概要

• エントリーDOI: 10.2210/pdb2e2y/pdb
• 分子名称: Myoglobin, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• 機能のキーワード: oxygen storage/transport, oxygen storage-transport complex
• 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: 18391.94

構造登録者

Ohki, T.,Ueno, T.,Hikage, T.,Suzuki, A.,Yamane, T.,Watanabe, Y. (登録日: 2006-11-18, 公開日: 2007-10-23, 最終更新日: 2023-10-25)

主引用文献

Watanabe, Y.,Nakajima, H.,Ueno, T.
Reactivities of oxo and peroxo intermediates studied by hemoprotein mutants
Acc.Chem.Res., 40:554-562, 2007

PubMed Abstract: A series of myoglobin mutants, in which distal sites are modified by site-directed mutagenesis, are able to catalyze peroxidase, catalase, and P450 reactions even though their proximal histidine ligands are intact. More importantly, reactions of P450, catalase, and peroxidase substrates and compound I of myoglobin mutants can be observed spectroscopically. Thus, detailed oxidation mechanisms were examined. On the basis of these results, we suggest that the different reactivities of P450, catalase, and peroxidase are mainly caused by their active site structures, but not the axial ligand. We have also prepared compound 0 under physiological conditions by employing a mutant of cytochrome c 552. Compound 0 is not able to oxidize ascorbic acid.

PubMed: 17567089
DOI: 10.1021/ar600046a

実験手法

X-RAY DIFFRACTION (1.6 Å)