UV Resonance Raman Characterization of a Substrate Bound to Human Indoleamine 2,3-Dioxygenase 1.

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ID: 42701
2019
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Abstract
Human indoleamine 2,3-dioxygenase 1 (IDO) is a heme enzyme that catalyzes the first reaction of the main metabolic pathway of L-tryptophan (Trp) to produce N-formylkynurenin. The reaction involves cleavage of the C=C bond in the Trp indole ring and insertion of two atomic oxygens from the iron-bound O into the indole 2 and 3 position. For establishment of the chemical mechanism of this unique enzymatic reaction, it is necessary to determine the conformation and electronic state of the substrate Trp bound to IDO. In this study, we measured the ultraviolet resonance Raman spectra of IDO in the presence of Trp to detect the vibrational modes of the substrate Trp. We compared the ultraviolet resonace Raman spectra of Trp in a ternary complex (Trp-bound cyanide enzyme) and a binary complex (Trp-bound reduced enzyme) of IDO with that of free Trp in solution and found that binding to IDO influences the conformation of Trp, resulting in similar changes in the two complexes, especially around the C-C bond. However, the presence of the diatomic ligand at the heme sixth coordination site in the ternary complex significantly alters the mobility and electronic structure of Trp, most likely resulting in the C=C bond cleavage in the enzymatic reaction.
Reference Key
yanagisawa2019uvbiophysical Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Yanagisawa, Sachiko;Kayama, Kure'e;Hara, Masayuki;Sugimoto, Hiroshi;Shiro, Yoshitsugu;Ogura, Takashi;
Journal Biophysical journal
Year 2019
DOI
S0006-3495(19)30585-5
URL
Keywords Keywords not found

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