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Review
. 2013 Oct 9;113(10):7769-92.
doi: 10.1021/cr300015c. Epub 2013 Jun 28.

Arsenic binding to proteins

Shengwen Shen  1 , Xing-Fang Li, William R Cullen, Michael Weinfeld, X Chris Le
Affiliations
Review

Arsenic binding to proteins

Shengwen Shen et al. Chem Rev. .
No abstract available

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Figures

Figure 1
Figure 1
Binding of inorganic arsenite (iAsIII), monomethylarsonous acid (MMAIII), and dimethylarsinous acid (DMAIII) to cysteines in a protein.
Figure 2
Figure 2
Binding of iAsIII to the ArsR repressor from E. coli plasmid R773 (P15905) results in conformational change of the repressor. iAsIII binds to Cys32, Cys34, and Cys37 of the ArsR repressor. Unwinding the helix disrupts DNA binding, resulting in dissociation of the repressor from the operator site. Dissociation of the repressor induces gene expression. (Adapted from ref (65).)
Figure 3
Figure 3
Ribbon representation of ligand-free AS3MT (CmArsM) from the thermophilic eukaryotic alga C. merolae. N and C indicate the N- and C-terminal domains and are colored blue and red, respectively. Cysteine residues are shown as balls and sticks and colored green (carbon) and yellow (sulfur). Three cysteine residues, C72, C174, and C224, are believed to be involved in arsenic binding. (Reprinted with permission from ref (75). Copyright 2012 American Chemical Society.)
Figure 4
Figure 4
A model depicting six arsenic atoms bound to 18 cysteines in metallothionein. (Reprinted with permission from ref (155). Copyright 2008 American Chemical Society.)
Figure 5
Figure 5
Mass spectra showing the number of monomethylarsonous acid (MMAIII) molecules bound to metallothionein (MT). The solutions contained 7 μM metallothionein (rMT-IIa) and increasing concentrations of MMAIII. The concentration ratios of MMAIII to MT in the solutions were (a) 1:5, (b) 1:1, (c) 5:1, and (d) 50:1. The ions carrying 5+ and 4+ charges are shown. The numbers on the peaks represent the number of MMAIII bound to the MT molecule. For example, peak 6 represents MT-(CH3As)6. A maximum of 10 MMAIII molecules were bound to a single MT that contained 20 cysteines. (Adapted from ref (151).)
Figure 6
Figure 6
Schematic representation of arsenic interaction with the arsRDABC operon and related enzymes in E. coli. ArsR is an AsIII-responsive transcriptional repressor that binds to the ars promoter, repressing transcription. Binding of iAsIII to ArsR results in dissociation of the repressor from the DNA and hence gene expression. iAsV is taken up by the phosphate transporter, while iAsIII is taken up by the aquaglyceroporin GlpF. iAsV is reduced to iAsIII by ArsC. Intracellular iAsIII is extruded from the cells by ArsB alone or by the ArsAB ATPase. (Modified from ref (163).)
Figure 7
Figure 7
Comparison of rat hemoblobin (rHb) and human hemoblobin (hHb) binding to three trivalent arsenicals (iAsIII, MMAIII, and DMAIII). Higher percentages of the trivalent arsenicals are bound to rHb than to hHb. (Reprinted with permission from ref (169). Copyright 2004 American Chemical Society.)
Figure 8
Figure 8
A proposed mechanism for the treatment of acute promyelocytic leukemia (APL) using inorgaic arsenic. Binding of arsenic to the promyelocytic leukemia (PML) retinoic acid receptor alpha (RARα) fusion protein triggers SUMOylation and ubiquitination and ultimately leads to the degradation of the oncoprotein and cell death. (Reprinted with permission from ref (66) and Kogan, S.C. 10.1126/science.1189198. Copyright 2010 American Association for the Advancement of Science.)
Figure 9
Figure 9
Toxicity of six arsenic compounds to HL-60 cells after a 48-h incubation. (Adapted from ref (200).)
Figure 10
Figure 10
A comparison of binding affinity of trivalent and pentavalent arsenicals to proteins.
Figure 11
Figure 11
Kinetic data showing the relative abundance of the various arsenic–metallothionein species detected using electrospray mass spectrometry. The solution was analyzed following reaction of 9 μM apo-rfMT with 108 μM arsenite at 23.5 °C. The experimental data have a relative standard error of 7%. (Reprinted with permission from ref (153).)
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