日本語フィールド
著者：Yanagisawa, Sachiko; Horitani, Masaki; Sugimoto, Hiroshi; Shiro, Yoshitsugu; Okada, Norihiro; Ogura, Takashi題名：Resonance Raman study on the oxygenated and the ferryl-oxo species of indoleamine 2,3-dioxygenase during catalytic turnover発表情報：Faraday Discussions 巻: 148 ページ: 239-247キーワード：概要：Resonance Raman (RR) spectra of the oxygenated and FeIVO reaction intermediates of indoleamine 2,3-dioxygenase (IDO) are reported. Absorption and RR spectra reveal that the electronic and geometric structures of the two respective species at pH 6.5 and pH 8.0 are the same, although the enzymatic activity at pH 6.5 is 6 times higher than at pH 8.0. The results thus further support our current understanding that the FeIVO heme species is the active species in the IDO reaction cycle, although its presence was unexpected. The Fe-O2 and the O-O stretching frequencies of the IDO-Trp-O2 ternary complex at Trp concentrations of 50 μM and 8 mM are essentially identical. These results suggest that "substrate inhibition" of enzymatic activity occurs by binding of a second substrate molecule to an unknown binding site and not to the heme pocket. © 2011 The Royal Society of Chemistry.抄録：英語フィールド
Author：Yanagisawa, Sachiko; Horitani, Masaki; Sugimoto, Hiroshi; Shiro, Yoshitsugu; Okada, Norihiro; Ogura, TakashiTitle：Resonance Raman study on the oxygenated and the ferryl-oxo species of indoleamine 2,3-dioxygenase during catalytic turnoverAnnouncement information:Faraday Discussions Vol: 148 Page: 239-247An abstract：Resonance Raman (RR) spectra of the oxygenated and FeIVO reaction intermediates of indoleamine 2,3-dioxygenase (IDO) are reported. Absorption and RR spectra reveal that the electronic and geometric structures of the two respective species at pH 6.5 and pH 8.0 are the same, although the enzymatic activity at pH 6.5 is 6 times higher than at pH 8.0. The results thus further support our current understanding that the FeIVO heme species is the active species in the IDO reaction cycle, although its presence was unexpected. The Fe-O2 and the O-O stretching frequencies of the IDO-Trp-O2 ternary complex at Trp concentrations of 50 μM and 8 mM are essentially identical. These results suggest that "substrate inhibition" of enzymatic activity occurs by binding of a second substrate molecule to an unknown binding site and not to the heme pocket. © 2011 The Royal Society of Chemistry.