Answers are grounded in this paper and cite their sources.
An alcohol dehydrogenase isolated from Zymomonas mobilis was found to be activated by ferrous ions but not by zinc, after inactivation with metal-complexing agents. Cobaltous ions also re-activated to a lesser extent. It is suggested that in this species the alcohol dehydrogenase naturally contains iron. Kinetic studies on the iron-treated enzyme indicate an 'alcohol activation' phenomenon, which may have physiological relevance in overcoming product inhibition during fermentation.
No takes yet. Share an insight, caveat, or question.
R.K. Scopes (1983) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: