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Low-potential cytochromebas an essential electron-transport component of menaquinone reduction by formate inVibrio succinogenes

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Bioenergetics
0005-2728
Publisher
Elsevier
Publication Date
Volume
725
Issue
2
Identifiers
DOI: 10.1016/0005-2728(83)90206-2
Keywords
  • Cytochromeb
  • Formate Dehydrogenase
  • Electron Transport
  • Liposome
  • Menaquinone
  • (Vibrio Succinogenes)
Disciplines
  • Biology

Abstract

Abstract Incorporation of the electron-transport enzymes of Vibrio succinogenes into liposomes was used to investigate the question of whether, in this organism, a cytochrome b is involved in electron transport from formate to fumarate on the formate side of menaquinone. (1) Formate dehydrogenase lacking cytochrome b was prepared by splitting the cytochrome from the formate dehydrogenase complex. The enzyme consisted of two different subunits ( M r 110 000 and 20 000), catalyzed the reduction of 2,3-dimethyl-1,4-naphthoquinone by formate, and could be incorporated into liposomes. (2) The modified enzyme did not restore electron transport from formate to fumarate when incorporated into liposomes together with vitamin K-1 (instead of menaquinone) and fumarate reductase complex. In contrast, restoration was observed in liposomes that contained formate dehydrogenase with cytochrome b ( E m = −224 mV), in addition to the subunits mentioned above (formate dehydrogenase complex). (3) In the liposomes containing formate dehydrogenase complex and fumarate reductase complex, the response of the cytochrome b of the formate dehydrogenase complex was consistent with its interaction on the formate side of menaquinone in a linear sequence of the components. The low-potential cytochrome b associated with fumarate reductase complex was not reducible by formate under any condition. It is concluded that the low-potential cytochrome b of the formate dehydrogenase complex is an essential component in the electron transport from formate to menaquinone. The low-potential cytochrome b of the fumarate reductase complex could not replace the former cytochrome in restoring electron-transport activity.

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