The respiratory arsenate reductase from the Gram-positive, haloalkaliphile, Bacillus selenitireducens strain MLS10 was purified and characterized. It is a membrane bound heterodimer (150 kDa) composed of two subunits ArrA (110 kDa) and ArrB (34 kDa), with an apparent Km for arsenate of 34 µM and Vmax of 2.5 µmol min−1 mg−1. Optimal activity occurred at pH 9.5 and 150 g l−1 of NaCl. Metal analysis (inductively coupled plasma mass spectrometry) of the holoenzyme and sequence analysis of the catalytic subunit (ArrA; the gene fr which was cloned and sequenced) indicate it is a member of the DMSO reductase family of molybdoproteins.
Additional publication details
|Publication Subtype||Journal Article|
|Title||The respiratory arsenate reductase from Bacillus selenitireducens strain MLS10|
|Series title||FEMS Microbiology Letters|
|Contributing office(s)||Toxic Substances Hydrology Program|
|Google Analytic Metrics||Metrics page|