Archives of Microbiology

, Volume 149, Issue 6, pp 572–579 | Cite as

Isolation of the sulphur reductase and reconstitution of the sulphur respiration of Wolinella succinogenes

  • I. Schröder
  • A. Kröger
  • J. M. Macy
Original Papers


Wolinella succinogenes can grow at the expense of sulphur reduction by formate. The enzymes involved in the catalysis of this catabolic reaction have been investigated. From the results the following conclusions are drawn: 1. The enzyme isolated as a sulphide dehydrogenase from the cytoplasmic membrane of W. succinogenes is the functional sulphur reductase that operates in the electron transport from formate to sulphur. 2. The enzyme (Mr 200,000) consists essentially of one type of subunit with the Mr 85,000 and contains equal amounts of free iron and sulphide (120 μmol/g protein), but no heme. It represents the first functional sulphur reductase ever isolated. 3. The electron transport chain catalyzing sulphur reduction by formate consists merely of formate dehydrogenase and sulphur reductase. A lipophilic quinone which mediates the transfer of electrons between enzymes in other chains, is apparently not involved. This is the first known example of a phosphorylative electron transport chain that operates without a quinone. 4. The same formate dehydrogenase appears to operate in the electron transport both with sulphur and with fumarate as the terminal electron acceptor in W. succinogenes.

Key words

Sulphur reductase Sulphur respiration Electron transport Reconstitution Wolinella succinogenes 







menaquinone (vitamin K2)


phenylmethane sulfonylfluoride






4-(2-hydroxyethyl)-1-piperazineethane sulfonate


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Copyright information

© Springer-Verlag 1988

Authors and Affiliations

  • I. Schröder
    • 1
  • A. Kröger
    • 1
  • J. M. Macy
    • 1
  1. 1.Institut für Mikrobiologie der J. W. Goethe-Universität Frankfurt am MainFrankfurtGermany

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