Based on previous results which showed that quinohemo-protein alcohol dehydrogenase (QH-ADH) entrapped within polypyrrole is able to directly transfer electrons via the conducting polymer to the electrode surface, the electron-transfer properties of this multi-cofactor enzyme adsorbed and covalently-bound to self-assembled thiol monolayers and bare electrode surfaces has been investigated more closely. While the dissolved enzyme is able to transfer electrons to the electrode via heme c as well as via the more deeply buried PQQ (fast adsorption-chemical reaction-desorption mechanism), an orientation of adsorbed QH-ADH on hydrophobic electrode surfaces, as well as of adsorbed and covalently bound QH-ADH on negatively-charged thiol monolayers could be observed. In these cases the heme c units are pointing towards the electrode surfaces resulting in an optimised direct ET rate.