The dehydrogenation of 1-indanol by a soluble oxidoreductase from bovine liver.

A soluble enzyme that catalyzes the dehydrogenation of l-indanol to indanone has been partially purified from bovine liver. The enzyme has a narrow substrate specificity, and only very closely related carbinols such as ltetralol, fluorenol, acenaphthenol, and acenaphthene-1,8diol are oxidized. trans-Acenaphthene-l , 8-diol is converted to a mixture of acenaphthenequinone and 1,8-naphthalic acid. Indanol dehydrogenase, which has a molecular weight of 30,000, is clearly distinct from liver alcohol dehydrogenase. NADP+ is the preferred cofactor, but NAD+ is also utilized. The role of indanol dehydrogenase in the intact organism is presently unknown.