Premium
Interaction between Sox proteins of two physiologically distinct bacteria and a new protein involved in thiosulfate oxidation
Author(s) -
Welte Cornelia,
Hafner Swetlana,
Krätzer Christian,
Quentmeier Armin,
Friedrich Cornelius G.,
Dahl Christiane
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.03.020
Subject(s) - rhodanese , thiosulfate , chemistry , enzyme , biochemistry , bacteria , sulfur , in vitro , biology , organic chemistry , genetics
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.