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The respiratory arsenate reductase from Bacillus selenitireducens strain MLS10

FEMS Microbiology Letters

By:
, , , , , and
DOI: 10.1016/S0378-1097(03)00609-8

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Abstract

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 ??M and Vmax of 2.5 ??mol 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 for which was cloned and sequenced) indicate it is a member of the DMSO reductase family of molybdoproteins. ?? 2003 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.

Additional Publication Details

Publication type:
Article
Publication Subtype:
Journal Article
Title:
The respiratory arsenate reductase from Bacillus selenitireducens strain MLS10
Series title:
FEMS Microbiology Letters
DOI:
10.1016/S0378-1097(03)00609-8
Volume
226
Issue:
1
Year Published:
2003
Language:
English
Larger Work Type:
Article
Larger Work Subtype:
Journal Article
Larger Work Title:
FEMS Microbiology Letters
First page:
107
Last page:
112
Number of Pages:
6