1AJG

CARBONMONOXY MYOGLOBIN AT 40 K

1AJG の概要

• エントリーDOI: 10.2210/pdb1ajg/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 transport, respiratory protein, heme
• 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: 18071.57

構造登録者

Teng, T.Y.,Srajer, V.,Moffat, K. (登録日: 1997-05-02, 公開日: 1997-11-12, 最終更新日: 2024-05-22)

主引用文献

Teng, T.Y.,Srajer, V.,Moffat, K.
Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K.
Nat.Struct.Biol., 1:701-705, 1994

PubMed Abstract: Myoglobin's reversible binding of oxygen is a model for studies of protein control of ligand binding and discrimination. Protein relaxation and geminate ligand rebinding subsequent to ligand photodissociation have been studied extensively by a variety of techniques. The ps to ns time scales for these processes are still much shorter than the ms time resolution of X-ray diffraction experiments, but it may be possible to trap these intermediates at low temperatures. We report here an X-ray diffraction investigation of structural changes induced by photolysis of carbonmonoxy myoglobin crystals at 40 K. Our results provide a structural basis for the interpretation of ambient and low temperature spectroscopic observations and molecular dynamics simulations of the ligand photodissociation and binding processes in haem proteins.

PubMed: 7634074
DOI: 10.1038/nsb1094-701

実験手法

X-RAY DIFFRACTION (1.69 Å)