8FB0

H64Q Myoglobin in complex with acetamide

8FB0 の概要

• エントリーDOI: 10.2210/pdb8fb0/pdb
• 分子名称: Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, ACETAMIDE, ... (6 entities in total)
• 機能のキーワード: heme protein, oxygen storage
• 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: 18599.14

構造登録者

Powell, S.M.,Thomas, L.M.,Richter-Addo, G.B. (登録日: 2022-11-29, 公開日: 2023-06-21, 最終更新日: 2023-11-01)

主引用文献

Powell, S.M.,Prather, K.Y.,Nguyen, N.,Thomas, L.M.,Richter-Addo, G.B.
Interactions of metronidazole and chloramphenicol with myoglobin: Crystal structure of a Mb-acetamide product.
J Porphyr Phthalocyanines, 27:1142-1147, 2023

PubMed Abstract: Nitroorganics present a general concern for a safe environment due to their health hazards. However, some nitroorganics such as metronidazole (Mtz) and chloramphenicol (CAM) also possess medicinal value. Mtz and CAM can undergo reductive bioactivation presumably via their nitroso derivatives. We show, using UV-vis spectroscopy, that sperm whale myoglobin (swMb) and its distal pocket mutants retaining H-bonding capacity react with Mtz in the presence of dithionite to generate products with spectra suggestive of the Fe-bound nitroso (Fe-RNO; λ ~420 nm) forms. We have crystallized and solved the X-ray crystal structure of an H64Q swMb-acetamide compound to 1.76 Å resolution; formation of this compound results from the serendipitous crystallographic trapping, by the heme center, of acetamide from the reductive decomposition of Mtz. Only one of the swMb proteins, namely H64Q swMb with a relatively flexible Gln64 residue, reacted with CAM presumably due to the bulky nature of CAM that generally may restrict its access to the heme site.

PubMed: 37868702
DOI: 10.1142/s1088424623500700

実験手法

X-RAY DIFFRACTION (1.76 Å)