Protein Degradation by Peroxide Catalyzed by Chromium (III): Role of Coordinated Ligand

Shrivastava, H. Yamini; Nair, Balachandran Unni

doi:10.1006/bbrc.2000.2492

Cited by 39 publications

(19 citation statements)

References 28 publications

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“…It is known that Cr can bind to proteins and may be associated with enhanced protein degradation (Shrivastava & Nair, 2000, 2004Feng et al, 2003). However, Cr-DNA interactions are also widely reported.…”

Section: Discussionmentioning

confidence: 99%

Oxidative protein damage causes chromium toxicity in yeast

et al. 2005

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Oxidative damage in microbial cells occurs during exposure to the toxic metal chromium, but it is not certain whether such oxidation accounts for the toxicity of Cr. Here, a Saccharomyces cerevisiae sod1D mutant (defective for the Cu,Zn-superoxide dismutase) was found to be hypersensitive to Cr(VI) toxicity under aerobic conditions, but this phenotype was suppressed under anaerobic conditions. Studies with cells expressing a Sod1p variant (Sod1 H46C ) showed that the superoxide dismutase activity rather than the metal-binding function of Sod1p was required for Cr resistance. To help identify the macromolecular target(s) of Cr-dependent oxidative damage, cells deficient for the reduction of phospholipid hydroperoxides (gpx3D and gpx1D/gpx2D/gpx3D) and for the repair of DNA oxidation (ogg1D and rad30D/ogg1D) were tested, but were found not to be Cr-sensitive. In contrast, S. cerevisiae msraD (mxr1D) and msrbD (ycl033cD) mutants defective for peptide methionine sulfoxide reductase (MSR) activity exhibited a Cr sensitivity phenotype, and cells overexpressing these enzymes were Cr-resistant. Overexpression of MSRs also suppressed the Cr sensitivity of sod1D cells. The inference that protein oxidation is a primary mechanism of Cr toxicity was corroborated by an observed~20-fold increase in the cellular levels of protein carbonyls within 30 min of Cr exposure. Carbonylation was not distributed evenly among the expressed proteins of the cells; certain glycolytic enzymes and heat-shock proteins were specifically targeted by Cr-dependent oxidative damage. This study establishes an oxidative mode of Cr toxicity in S. cerevisiae, which primarily involves oxidative damage to cellular proteins.

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Section: Discussionmentioning

confidence: 99%

Oxidative protein damage causes chromium toxicity in yeast

et al. 2005

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“…The chromium in the wastewater exists as highly cationic species. 4 These cationic species are ionically exchanged with the alkali/alkaline earth metal ions and protons present in the seaweeds. This observation was demonstrated through EDAX and flame photometry studies.…”

Section: Correlationmentioning

confidence: 99%

Recovery and reuse of chromium from tannery wastewaters using Turbinaria ornata seaweed

Aravindhan

Madhan

Rao

et al. 2004

J of Chemical Tech & Biotech

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Brown seaweed (Turbinaria spp) was pre-treated with sulfuric acid, calcium chloride and magnesium chloride and tested for its ability to remove chromium from tannery wastewater. Protonated seaweeds gave better uptake of chromium compared with calcium and magnesium treatments. Chromium uptake was optimal at pH 3.5. Turbinaria weed exhibited maximum uptake of about 31 mg of chromium for one gram of seaweed at an initial concentration of 1000 ppm of chromium. Freundlich and Langmuir adsorption isotherm models were used to describe the biosorption of chromium(III) by Turbinaria spp. The chromium-loaded seaweed was reused as a reductant in the preparation of the tanning agent basic chromium sulfate (BCS). Leathers made from this tanning agent had properties comparable to conventionally processed chrome-tanned leathers.

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“…The electronic spectrum of this complex shows an intense charge transfer band at 590 nm. The parent chromium(III) complex of the ligand salen, Cr (salen) (H 2 O) 2 ϩ has been shown to bind with BSA through coordinate bond formation and their proteinmetal complex is stabilized due to extensive hydrophobic interactions (13). The binding constant, K b was found to be 7.6 Ϯ 0.4 ϫ 10 3 M Ϫ1 .…”

Section: Resultsmentioning

confidence: 99%

“…Even though the interaction of chromium(V) with DNA has been well studied, it is surprising that not much attention has been paid to understand the consequence of the interaction of chromium(V) with proteins. The ability of some chromium(III) complexes to bring about protein degradation has however, been recently demonstrated by us (13). Oxidatively modified proteins are rapidly and selectively degraded by intracellular proteolytic systems (14).…”

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confidence: 99%