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

TitleMechanism of hexavalent chromium detoxification by microorganisms and bioremediation application potential: A review
Authors
KeywordsBioremediation
Chromium
Detoxification
Metal Reduction
Proteomics
Issue Date2007
PublisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/ibiod
Citation
International Biodeterioration And Biodegradation, 2007, v. 59 n. 1, p. 8-15 How to Cite?
AbstractChromium 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. © 2006.
Persistent Identifierhttp://hdl.handle.net/10722/178975
ISSN
2015 Impact Factor: 2.429
2015 SCImago Journal Rankings: 0.919
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorCheung, KHen_US
dc.contributor.authorGu, JDen_US
dc.date.accessioned2012-12-19T09:51:11Z-
dc.date.available2012-12-19T09:51:11Z-
dc.date.issued2007en_US
dc.identifier.citationInternational Biodeterioration And Biodegradation, 2007, v. 59 n. 1, p. 8-15en_US
dc.identifier.issn0964-8305en_US
dc.identifier.urihttp://hdl.handle.net/10722/178975-
dc.description.abstractChromium 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. © 2006.en_US
dc.languageengen_US
dc.publisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/ibioden_US
dc.relation.ispartofInternational Biodeterioration and Biodegradationen_US
dc.subjectBioremediationen_US
dc.subjectChromiumen_US
dc.subjectDetoxificationen_US
dc.subjectMetal Reductionen_US
dc.subjectProteomicsen_US
dc.titleMechanism of hexavalent chromium detoxification by microorganisms and bioremediation application potential: A reviewen_US
dc.typeArticleen_US
dc.identifier.emailGu, JD: jdgu@hkucc.hku.hken_US
dc.identifier.authorityGu, JD=rp00701en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.ibiod.2006.05.002en_US
dc.identifier.scopuseid_2-s2.0-33845972300en_US
dc.identifier.hkuros134268-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33845972300&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume59en_US
dc.identifier.issue1en_US
dc.identifier.spage8en_US
dc.identifier.epage15en_US
dc.identifier.isiWOS:000244017700002-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridCheung, KH=7402406659en_US
dc.identifier.scopusauthoridGu, JD=7403129601en_US

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