COMPONENTS OF THE ELECTRON-TRANSFERRING SYSTEM IN ACETOBACTER SUBOXYDANS AND RECONSTRUCTION OF THE LACTATE OXIDATION SYSTEM

概要

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1. Cytochromes a_1^<590>, b^<560>, c_1^<554>, and c_1^<552> were isolated and purified from a strain of Aceiobacter suboxydans. The procedures used were described in detail. 2. The main cytochrome band at 550-560mμ in intact cells splitted at liquid air temperature into two bands, 551mμ (strong) and 559mμ (weak). 3. Optical and physiological properties of the four cytochromes were investigated. Lactic dehydrogenase activity was found to be associated with cytochrome c_1^<554>. The two c_1-type cytochromes, especially cytochrome c_1^<554>, persisted in their reduced form after the purification through many steps. 4. By some combinations of isolated components reconstruction of the oxygen uptake system could be realized. 5. The oxygen-consuming activity of purified oxidase prepara-tions was accelerated by a-tocopherol but not by Emasoll 4130 and Tween 80. 6. Some discussions were made on the nature of terminal oxidase, the role of cytochrome c_1^<552> in the electron-transport system, and persistence of reduced state of c_1-type cytochromes. 7. A possible scheme of the electron-transferring system of Acetobacter suboxydans was presented.
日本植物生理学会の論文