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Open AccessJournal ArticleDOI

Biochemistry of arsenic detoxification

Barry P. Rosen
- 02 Oct 2002 - 
- Vol. 529, Iss: 1, pp 86-92
TLDR
While the overall schemes for arsenic resistance are similar in prokaryotes and eukaryotes, some of the specific proteins are the products of separate evolutionary pathways.
About
This article is published in FEBS Letters.The article was published on 2002-10-02 and is currently open access. It has received 726 citations till now. The article focuses on the topics: Arsenate reductase activity & Arsenate reductase.

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Citations
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Journal ArticleDOI

The Ecology of Arsenic

TL;DR: This work reviews what is known about arsenic-metabolizing bacteria and their potential impact on speciation and mobilization of arsenic in nature and investigates their role in aquifers.
Journal ArticleDOI

Wound healing - A literature review.

TL;DR: The purpose of this review is to describe the various cellular and molecular aspects involved in the skin healing process.
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Arsenic hazards: strategies for tolerance and remediation by plants

TL;DR: Recent advances in arsenic tolerance are discussed and their potential applications, particularly in the context of multigenic engineering approaches, are discussed.
Journal ArticleDOI

Arsenic binding to proteins.

TL;DR: Although the adverse health effects arising from exposure to arsenic have been well-recognized, the mechanism(s) of action responsible for the diverse range of health effects are complicated and poorly understood.
Journal ArticleDOI

Occurrence of arsenic contamination in Canada: sources, behavior and distribution.

TL;DR: An analysis of the currently available information on recognized problem areas, and an overview of current knowledge of the principal hydrogeochemical processes of arsenic transportation and transformation are provided, however, a more detailed understanding of local sources of arsenic and mechanisms of arsenic release is required.
References
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Journal ArticleDOI

Asp45 Is a Mg2+ Ligand in the ArsA ATPase

TL;DR: Results indicate that Asp45 is a Mg2+-responsive residue, consistent with its function as a M g2+ ligand in ArsA, which is allosterically activated by arsenite or antimonite.
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The anion-stimulated atpase arsa shows unisite and multisite catalytic activity

TL;DR: It is demonstrated that the A1 domain is capable of carrying out unisite catalysis in the absence of antimonite, and the linker region, where ADP binds under both unisite and multisite catalytic conditions, may play an important role in the energy transduction process.
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Role of conserved histidine residues in metalloactivation of the ArsA ATPase.

TL;DR: Results suggest that the histidine residues play a role in transmission of the signal between the catalytic and allosteric sites to activate ATP hydrolysis.
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