Abstract
The reaction mechanism of old yellow enzyme (NADPH:(acceptor) oxidoreductase, EC 1.6.99.1) was kinetically investigated using NADH as substrate. The enzyme was reduced by NADH via a reaction intermediate which has a specific absorption spectrum. This intermediate decomposed to yield a reduced enzyme and NAD + through an irreversible first-order reaction step. The reduced enzyme was reoxidized by oxygen through a second-order reaction process. Individual values of elementary rate constants were measured and a computer simulation of the reaction process was carried out. No involvement of free radical of flavin semiquinone in the reaction process could be shown.
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