A novel MN2+-oxidizing enzyme system in a freshwater bacterium.

Abstract

Manganese oxidation by cell suspensions and cell extracts of a freshwater bacterium, designated strain FMn 1, was investigated. Manganese appeared to be oxidized in the periplasmic space. A conventional, membrane-bound-electron transport system was not utilized. An enzyme or enzyme complex and a cofactor, each of different molecular size, were located in different parts of the cell envelope. Results suggest that the cofactor reacts with manganese in the periplasmic space and that in the presence of oxygen it is reoxidized by the enzyme. The enzyme is probably loosely bound to the membrane. A combination of enzyme and cofactor in a crude preparation exhibited a pH optimum at around 7.0. The enzyme exhibited a temperature optimum at around 30 degrees C. No temperature optimum was found for the cofactor. The enzyme was heat-stable and could oxidize manganese under anaerobic conditions. The enzyme system appears to be different from others so far described.