The subatomic resolution study of laccase inhibition by chloride and fluoride anions using single-crystal serial crystallography: Insights into the...
Polyakov K. M., Gavryushov S. A., Fedorov T. V., Glazunova O. A., Popov A. N.
Acta Crystallographica Section D: Structural Biology
Vol.75, P. 804-816
Опубликовано: 2019
Тип ресурса: Статья
DOI:10.1107/S2059798319010684
Аннотация:
Laccases are enzymes that catalyze the oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of molecular oxygen to water. Here, a subatomic resolution X-ray crystallographic study of the mechanism of inhibition of the laccase from the basidiomycete fungus Steccherinum murashkinskyi by chloride and fluoride ions is presented. Three series of X-ray diffraction data sets were collected with increasing doses of absorbed X-ray radiation from a native S. murashkinskyi laccase crystal and from crystals of complexes of the laccase with chloride and fluoride ions. The data for the native laccase crystal confirmed the previously deduced enzymatic mechanism of molecular oxygen reduction. The structures of the complexes allowed the localization of chloride and fluoride ions in the channel near the T2 copper ion. These ions replace the oxygen ligand of the T2 copper ion in this channel and can play the role of this ligand in the enzymatic reaction. As follows f
Ключевые слова:
enzymatic oxygen reduction; laccase inhibition; laccase inhibition; reaction mechanisms; single-crystal serial crystallography
chloride; copper; fluoride; laccase; ligand; oxygen; Basidiomycetes; chemistry; enzyme active site; enzymology; metabolism; molecular model; oxidation reduction reaction; procedures; protein conformation; single molecule imaging; X ray crystallography; Basidiomycota; Catalytic Domain; Chlorides; Copper; Crystallography, X-Ray; Fluorides; Laccase; Ligands; Models, Molecular; Oxidation-Reduction; Oxygen; Protein Conformation; Single Molecule Imaging
Язык текста: Английский
ISSN: 2059-7983
Polyakov K. M.
Gavryushov S. A. Sergej Aleksandrovich 1964-
Fedorov T. V.
Glazunova O. A.
Popov A. N.
Поляков К. М.
Гаврюшов С. А. Сергей Александрович 1964-
Федоров Т. В.
Глазунова О. А.
Попов А. Н.
The subatomic resolution study of laccase inhibition by chloride and fluoride anions using single-crystal serial crystallography: Insights into the enzymatic reaction mechanism
The subatomic resolution study of laccase inhibition by chloride and fluoride anions using single-crystal serial crystallography: Insights into the...
Текст визуальный непосредственный
Acta Crystallographica Section D: Structural Biology
John Wiley & Sons
Vol.75 P. 804-816
2019
Статья
enzymatic oxygen reduction laccase inhibition laccase inhibition reaction mechanisms single-crystal serial crystallography
chloride copper fluoride laccase ligand oxygen Basidiomycetes chemistry enzyme active site enzymology metabolism molecular model oxidation reduction reaction procedures protein conformation single molecule imaging X ray crystallography Basidiomycota Catalytic Domain Chlorides Copper Crystallography, X-Ray Fluorides Laccase Ligands Models, Molecular Oxidation-Reduction Oxygen Protein Conformation Single Molecule Imaging
Laccases are enzymes that catalyze the oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of molecular oxygen to water. Here, a subatomic resolution X-ray crystallographic study of the mechanism of inhibition of the laccase from the basidiomycete fungus Steccherinum murashkinskyi by chloride and fluoride ions is presented. Three series of X-ray diffraction data sets were collected with increasing doses of absorbed X-ray radiation from a native S. murashkinskyi laccase crystal and from crystals of complexes of the laccase with chloride and fluoride ions. The data for the native laccase crystal confirmed the previously deduced enzymatic mechanism of molecular oxygen reduction. The structures of the complexes allowed the localization of chloride and fluoride ions in the channel near the T2 copper ion. These ions replace the oxygen ligand of the T2 copper ion in this channel and can play the role of this ligand in the enzymatic reaction. As follows f