Anions binding to bilirubin oxidase from Trachyderma tsunodae K-2593

Autor:	Tsutomu Morikawa, Junzo Hirose, Hirokuni Sakuragi, Mituru Kikkawa, Keitaro Hiromi, Masayoshi Minakami, Hiroyuki Iwamoto, Kaori Inoue
Rok vydání:	1998
Předmět:	Inorganic chemistry chemistry.chemical_element Substrate (chemistry) Disproportionation Copper Redox Inorganic Chemistry Absorbance chemistry Materials Chemistry Physical and Theoretical Chemistry Absorption (chemistry) Bilirubin oxidase Anion binding
Zdroj:	Inorganica Chimica Acta. 273:204-212
ISSN:	0020-1693
DOI:	10.1016/s0020-1693(97)06183-5
Popis:	Bilirubin oxidase obtained from Trachyderma tsunodae K-2593 is a multi-copper enzyme which has type 1:type 2:type 3 copper atoms in the ratio 1:1:2. Anion binding properties of bilirubin oxidase were investigated to determine the structural and functional properties of bilirubin oxidase. The anions N3−, SCN−, F−, Cl−, and Br− were non-competitive inhibitors against the substrate, bilirubin ditaurate, and the inhibition constants of the anions were in the following order: N3−
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::6396a5b27fb20f9350506135a35d1aea https://doi.org/10.1016/s0020-1693(97)06183-5 Zobrazit plný text záznamu Full Text from ScienceDirect