Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 418, Issue 2, Pages 205-216Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2003.08.008
Keywords
dimethyl sulfoxide reductase; trimethylamine N-oxide reductase; anaerobic respiration; chimeric enzyme; inclusion bodies; hydroxypyridine N-oxide
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The ynJEFGHI operon is a paralogue of the Escherichia coli dmsABC operon. ynfE and ynfF are paralogues of dmsA. ynfG and ynfH are paralogues of dmsB and dinsC, respectively. YnfI (dmsD) has no dms paralogue. YnfE/F and YnfG could be detected by immunoblotting with anti-DmsAB antibodies when expressed under the control of a tac or dms promoter. Cells harbouring ynfFGH on a multicopy plasmid supported anaerobic growth with dimethyl sulfoxide (DMSO) as respiratory oxidant in a dmsA BC deletion, suggesting that YnfFGH forms a heterotimeric enzyme complex similar to DmsABC. Exchange of DmsC by YnfH (DmsAB-YnfH) resulted in membrane localization, anaerobic growth on DMSO, and binding of 2-n-heptyl 4-hydroxyquinoline-N-oxide, indicating that YnfH was a competent anchor. YnfG can also replace DmsB as the electron transfer subunit and assembled [Fe-S] clusters as judged by electron paramagnetic resonance spectroscopy. YnfE and/or YnfF could not form a functional complex with DmsBC and expression of YnfE prevented the accumulation of YnfFGH. (C) 2003 Published by Elsevier Inc.
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