Resonance Raman study on the oxygenated and the ferryl-oxo species of indoleamine 2,3-dioxygenase during catalytic turnover
Abstract
Resonance Raman (RR) O
O 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
- This article is part of the themed collection: Spectroscopy, Theory and Mechanism in Bioinorganic Chemistry