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
Toxicity of Arsenic to Photobacterium phosphoreum, Daphnia magna, and Danio rerio at Different pH Levels
TL;DR: Three kinds of aquatic organisms including Photobacterium phosphoreum, Daphnia magna, and Danio rerio were used to study the effects of pH on the toxicity of arsenic, finding that As(III) is more toxic to the tested organisms than As(V), and P. phosphorum was more sensitive to theoxicity of arsenic than D. rerio.
Book ChapterDOI
Current Aspects of Metal Resistant Bacteria in Bioremediation: From Genes to Ecosystem
Farhana Masood,Abdul Malik +1 more
TL;DR: This chapter summarizes the recent progress in the field of molecular microbial ecology of metal resistant bacteria with emphasis that how the genetic capacity of the organisms can be exploited for the remediation of heavy metal pollution.
Journal ArticleDOI
Did nature also choose arsenic
TL;DR: It is hypothesized that ancient biochemical systems, analogous to but distinct from those known today, could have utilized arsenate in the equivalent biological role as phosphate and may have supported a ‘shadow biosphere’ at the time of the origin and early evolution of life on Earth or on other planets.
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Analysis of As- and Hg-Species in Metal-Resistant Oral Bacteria, by Imaging ToF-SIMS
TL;DR: To elucidate how bacteria take up and transform toxic metals inside the cells, ion imaging and depth profiling with time‐of‐flight secondary ion mass spectrometry (ToF‐SIMS) was performed and mercury ions were found transformed to methylmercury preferably in the periplasmic space.
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Integrated environmental factor-dependent growth and arsenic biotransformation by aquatic microalgae: A review.
TL;DR: In this paper , a review scrutinizes the available literature on the As biotransformation potentials of various marine and freshwater microalgae under individual and integrated stresses of such factors.
References
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Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.
TL;DR: Related sequences in both alpha and beta and in other enzymes that bind ATP or ADP in catalysis help to identify regions contributing to an adenine nucleotide binding fold in both ATP synthase subunits.
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CLUSTAL: A package for performing multiple sequence alignment on a microcomputer
Desmond G. Higgins,Paul M. Sharp +1 more
TL;DR: An approach for performing multiple alignments of large numbers of amino acid or nucleotide sequences is described, based on first deriving a phylogenetic tree from a matrix of all pairwise sequence similarity scores obtained using a fast pairwise alignment algorithm.
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Classification and evolution of P-loop GTPases and related ATPases.
TL;DR: In this article, the authors compared sequences and available structures for all the widely distributed representatives of the P-loop GTPases and GTPase-related proteins with the aim of constructing an evolutionary classification for this superclass of proteins and reconstructing the principal events in their evolution.
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Comparative toxicity of trivalent and pentavalent inorganic and methylated arsenicals in rat and human cells.
Miroslav Styblo,L.M. Del Razo,Libia Vega,Dori R. Germolec,Edward L. LeCluyse,G. Hamilton,W Reed,Changqing Wang,William R. Cullen,David J. Thomas +9 more
TL;DR: It is suggested that trivalent methylated arsenicals, intermediary products of arsenic methylation, may significantly contribute to the adverse effects associated with exposure to iAs, and high methylation capacity does not protect cells from the acute toxicity of triavalent arsenicals.
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The MRP gene encodes an ATP-dependent export pump for leukotriene C4 and structurally related conjugates.
Inka Leier,Gabriele Jedlitschky,Ulrike Buchholz,Susan P.C. Cole,Roger G. Deeley,Dietrich Keppler +5 more
TL;DR: It is concluded that the biosynthetic release of LTC4 from cells is mediated by the 190-kDa product of the MRP gene, a primary-active ATP-dependent export pump for conjugates of lipophilic compounds with glutathione and several other anionic residues.