Mechanisms of bacterial resistance to chromium compounds View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-10-13

AUTHORS

Martha I. Ramírez-Díaz, César Díaz-Pérez, Eréndira Vargas, Héctor Riveros-Rosas, Jesús Campos-García, Carlos Cervantes

ABSTRACT

Chromium is a non-essential and well-known toxic metal for microorganisms and plants. The widespread industrial use of this heavy metal has caused it to be considered as a serious environmental pollutant. Chromium exists in nature as two main species, the trivalent form, Cr(III), which is relatively innocuous, and the hexavalent form, Cr(VI), considered a more toxic species. At the intracellular level, however, Cr(III) seems to be responsible for most toxic effects of chromium. Cr(VI) is usually present as the oxyanion chromate. Inhibition of sulfate membrane transport and oxidative damage to biomolecules are associated with the toxic effects of chromate in bacteria. Several bacterial mechanisms of resistance to chromate have been reported. The best characterized mechanisms comprise efflux of chromate ions from the cell cytoplasm and reduction of Cr(VI) to Cr(III). Chromate efflux by the ChrA transporter has been established in Pseudomonas aeruginosa and Cupriavidusmetallidurans (formerly Alcaligenes eutrophus) and consists of an energy-dependent process driven by the membrane potential. The CHR protein family, which includes putative ChrA orthologs, currently contains about 135 sequences from all three domains of life. Chromate reduction is carried out by chromate reductases from diverse bacterial species generating Cr(III) that may be detoxified by other mechanisms. Most characterized enzymes belong to the widespread NAD(P)H-dependent flavoprotein family of reductases. Several examples of bacterial systems protecting from the oxidative stress caused by chromate have been described. Other mechanisms of bacterial resistance to chromate involve the expression of components of the machinery for repair of DNA damage, and systems related to the homeostasis of iron and sulfur. More... »

PAGES

321-332

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10534-007-9121-8

DOI

http://dx.doi.org/10.1007/s10534-007-9121-8

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1045942389

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17934697


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