Mechanism of hexavalent chromium detoxification by microorganisms and bioremediation application potential: A review

• Published in: International biodeterioration & biodegradation 2007, Vol.59 (1), p.8-15
• Main Authors: Cheung, K.H., Gu, Ji-Dong
• Format: Article
• Language: English
• Subjects: Bacillus megaterium; Bioremediation; Chromium; Detoxification; Escherichia coli; Metal reduction; Proteomics; Pseudomonas maltophilia; Pseudomonas putida
• ISSN: 0964-8305; 1879-0208
• DOI: 10.1016/j.ibiod.2006.05.002

Chromium has been widely used in various industries. Hexavalent chromium (Cr 6+) is a priority toxic, mutagenic and carcinogenic chemical, whereas its reduced trivalent form (Cr 3+) is much less toxic and insoluble. Hence, the basic process for chromium detoxification is the transformation of Cr 6+ to Cr 3+. A number of aerobic and anaerobic microorganisms are capable of reducing Cr 6+. In the presence of oxygen, microbial reduction of Cr 6+ is commonly catalyzed by soluble enzymes, except in Pseudomonas maltophilia O-2 and Bacillus megaterium TKW3, which utilize membrane-associated reductases. Recently, two soluble Cr 6+ reductases, ChrR and YieF, have been purified from Pseudomonas putida MK1 and Escherichia coli, respectively. ChrR catalyzes an initially one-electron shuttle followed by a two-electron transfer to Cr 6+, with the formation of intermediate(s) Cr 5+ and/or Cr 4+ before further reduction to Cr 3+. YieF displays a four-electron transfer that reduces Cr 6+ directly to Cr 3+. The membrane-associated Cr 6+ reductase of B. megaterium TKW3 was isolated, but its reduction kinetics is as yet uncharacterized. Under anaerobic conditions, both soluble and membrane-associated enzymes of the electron transfer system were reported to mediate Cr 6+ reduction as a fortuitous process coupled to the oxidation of an electron donor substrate. In this process, Cr 6+ serves as the terminal electron acceptor of an electron transfer chain that frequently involves cytochromes (e.g., b and c). An expanding array of Cr 6+ reductases allows the selection of enzymes with higher reductive activity, which genetic and/or protein engineering may further enhance their efficiencies. With the advancement in technology for enzyme immobilization, it is speculated that the direct application of Cr 6+ reductases may be a promising approach for bioremediation of Cr 6+ in a wide range of environments.