We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
A mechanistic study on SMOB-ADP1: an NADH:flavin oxidoreductase of the two-component styrene monooxygenase of Acinetobacter baylyi ADP1.
- Authors
Gröning, Janosch; Kaschabek, Stefan; Schlömann, Michael; Tischler, Dirk
- Abstract
Two styrene monooxygenase types, StyA/StyB and StyA1/StyA2B, have been described each consisting of an epoxidase and a reductase. A gene fusion which led to the chimeric reductase StyA2B and the occurrence in different phyla are major differences. Identification of SMOA/SMOB-ADP1 of Acinetobacter baylyi ADP1 may enlighten the gene fusion event since phylogenetic analysis indicated both proteins to be more related to StyA2B than to StyA/StyB. SMOB-ADP1 is classified like StyB and StyA2B as HpaC-like reductase. Substrate affinity and turnover number of the homo-dimer SMOB-ADP1 were determined for NADH (24 µM, 64 s) and FAD (4.4 µM, 56 s). SMOB-ADP1 catalysis follows a random sequential mechanism, and FAD fluorescence is quenched upon binding to SMOB-ADP1 ( K = 1.8 µM), which clearly distinguishes that reductase from StyB of Pseudomonas. In summary, this study confirmes made assumptions and provides phylogenetic and biochemical data for the differentiation of styrene monooxygenase-related flavin reductases.
- Subjects
ACINETOBACTER baylyi; STYRENE; MONOOXYGENASES; OXIDOREDUCTASES; FLAVIN reductase; ADENOSINE diphosphate
- Publication
Archives of Microbiology, 2014, Vol 196, Issue 12, p829
- ISSN
0302-8933
- Publication type
Article
- DOI
10.1007/s00203-014-1022-y