OXIDATION OF REDUCED DIPHOSPHOPYRIDINE NUCLEOTIDE BY CLOSTRIDIUM PERFRINGENS : II. Purification of the Oxidase; Relation to Cytochrome c Reductase
Abstract
Updated information and services can be found at: http://jb.asm.org/content/77/4/393.citation These include: CONTENT ALERTS Receive: RSS Feeds, eTOCs, free email alerts (when new articles cite this article), more» Information about commercial reprint orders: http://jb.asm.org/site/misc/reprints.xhtml To subscribe to to another ASM Journal go to: http://journals.asm.org/site/subscriptions/ M. I. Biology Division, Oak Ridge National Laboratory,' Oak Ridge, Tennessee Received for publication August 27, 1958 The first paper of this series (, 1959) was concerned with the DPNH2 oxidation reactions catalyzed by extracts of Clostridium perfringens and the relation of these reactions to the problem of anaerobiosis. A four-electron DPNH oxidase that catalyzes reaction 1 was described. In addition, these extracts catalyze the reduction of (reaction 2). 2DPNH + 2H+ + 02 -- 2DPN+ + 2H20 (1) DPNH + 2 (Fe++) -* DPN+ (2) + 2 (Fe++) + H+ In the present paper, the partial purification of the oxidase and the evidence for its flavoprotein nature will be described. Evidence will be presented that indicates a close relation exists between DPNH oxidase and two molecular species of cytochrome reductase. One cytochrome reductase component may be identical with the oxidase; the formation of the other appears to be linked to loss of the four-electron