FEBS Letters
Volume 583, Issue 8 , Pages 1281-1286, 17 April 2009

Interaction between Sox proteins of two physiologically distinct bacteria and a new protein involved in thiosulfate oxidation

Edited by Stuart Ferguson

  • Cornelia Welte

      Affiliations

    • Institut für Mikrobiologie & Biotechnologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Meckenheimer Allee 168, D-53115 Bonn, Germany
  • ,
  • Swetlana Hafner

      Affiliations

    • Institut für Mikrobiologie & Biotechnologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Meckenheimer Allee 168, D-53115 Bonn, Germany
  • ,
  • Christian Krätzer

      Affiliations

    • Institut für Mikrobiologie & Biotechnologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Meckenheimer Allee 168, D-53115 Bonn, Germany
  • ,
  • Armin Quentmeier

      Affiliations

    • Lehrstuhl für Technische Mikrobiologie, Fachbereich Chemietechnik, Technische Universität Dortmund, Germany
  • ,
  • Cornelius G. Friedrich

      Affiliations

    • Lehrstuhl für Technische Mikrobiologie, Fachbereich Chemietechnik, Technische Universität Dortmund, Germany
  • ,
  • Christiane Dahl

      Affiliations

    • Institut für Mikrobiologie & Biotechnologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Meckenheimer Allee 168, D-53115 Bonn, Germany
    • Corresponding Author InformationCorresponding author. Fax: +49 228 737576.

Received 22 December 2008; received in revised form 2 March 2009; accepted 11 March 2009. published online 19 March 2009.

Abstract 

Organisms using the thiosulfate-oxidizing Sox enzyme system fall into two groups: group 1 forms sulfur globules as intermediates (Allochromatium vinosum), group 2 does not (Paracoccus pantotrophus). While several components of their Sox systems are quite similar, i.e. the proteins SoxXA, SoxYZ and SoxB, they differ by Sox(CD)2 which is absent in sulfur globule-forming organisms. Still, the respective enzymes are partly exchangeable in vitro: P. pantotrophus Sox enzymes work productively with A. vinosum SoxYZ whereas A. vinosum SoxB does not cooperate with the P. pantotrophus enzymes. Furthermore, A. vinosum SoxL, a rhodanese-like protein encoded immediately downstream of soxXAK, appears to play an important role in recycling SoxYZ as it increases thiosulfate depletion velocity in vitro without increasing the electron yield.

Abbreviations: DTT, dithiothreitol, Sox, sulfur oxidizing

Keywords: Sox proteins, Thiosulfate oxidation, Purple sulfur bacteria, Allochromatium vinosum, Paracoccus pantotrophus

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

PII: S0014-5793(09)00204-X

doi:10.1016/j.febslet.2009.03.020

FEBS Letters
Volume 583, Issue 8 , Pages 1281-1286, 17 April 2009