Biochemistry of arsenic detoxification
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.read more
Citations
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Journal ArticleDOI
The Ecology of Arsenic
Ronald S. Oremland,John F. Stolz +1 more
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.
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Wound healing - A literature review.
Ana Cristina Gonzalez,Tila Fortuna Costa,Zilton A. Andrade,Alena Ribeiro Alves Peixoto Medrado +3 more
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
Rudra Deo Tripathi,Sudhakar Srivastava,Seema Mishra,Nandita Singh,Rakesh Tuli,Dharmendra K. Gupta,Frans J. M. Maathuis +6 more
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.
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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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The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite.
Tsutomu Sato,Y Kobayashi +1 more
TL;DR: Northern hybridization and primer extension analysis showed that synthesis of a full-length ars transcript was induced by arsenate and that the ars promoter contains sequences that resemble the -10 and -35 regions of promoters that are recognized by E sigmaA.
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Insights into the Structure, Solvation, and Mechanism of ArsC Arsenate Reductase, a Novel Arsenic Detoxification Enzyme
Philip D. Martin,Srini DeMel,Jin Shi,Tatiana B. Gladysheva,Domenico L. Gatti,Barry P. Rosen,Brian F.P. Edwards +6 more
TL;DR: The exceptionally well-defined water structure of ArsC indicates that this crystal system has precise long-range order within the crystal and that the upper limit for the number of bound waters in crystal structures is underestimated by the structures in the Protein Data Bank.
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Reactivity of Glutaredoxins 1, 2, and 3 fromEscherichia coli Shows That Glutaredoxin 2 Is the Primary Hydrogen Donor to ArsC-catalyzed Arsenate Reduction
TL;DR: Glutaredoxin 2 is shown to be the most effective hydrogen donor for the reduction of arsenate by ArsC, suggesting that, during the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase.
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Dual mode of energy coupling by the oxyanion-translocating ArsB protein.
Saibal Dey,Barry P. Rosen +1 more
TL;DR: The results suggest that the Ars anion transport system can be either an obligatory ATP-coupled primary pump or a secondary carrier coupled to the proton motive force, depending on the subunit composition of the transport complex.
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Arsenate reductase of Staphylococcus aureus plasmid pI258.
TL;DR: Arsenate reductase encoded by Staphylococcus aureus arsenic-resistance plasmid pI258 was overproduced in Escherichia coli and purified, and the purified enzyme reduced radioactive arsenate to arsenite when coupled to thioredoxin, thiOREDoxin reduct enzyme, and NADPH.