Bacterial chromate reduction: A review of important genomic, proteomic, and bioinformatic analysis

References

• Ackerley, D. F., Gonzalez, C. F., Keyhan, M., Blake, R. II, and Matin, A. (2004b). Mechanism of chromate reduction by the E. coli protein, NfsA, and the role of different chromate reductases in minimizing oxidative stress during chromate reduction. Environ Microbiol, 6, 851–860.
   PubMed Web of Science ®Google Scholar
• Ackerley, D. F., Gonzalez, C. F., Park, C. H., Blake, R., Keyhan, M., and Matin, A. (2004a). Chromate reducing properties of soluble flavoproteins from Pseudomonas putida and E. coli. Appl Environ Microbiol, 70, 873–882.
   PubMed Web of Science ®Google Scholar
• Aguilar-Barajas, E., Paluscio, E., Cervantes, C., and Rensing, C. (2008). Expression of chromate resistance genes from Shewanella sp. strain ANA-3 in Escherichia coli. FEMS Microbiol Lett, 285, 97–100.
   PubMed Web of Science ®Google Scholar
• Alvarez, A. H., Moreno-Sanchez, R., and Cervantes, C. (1999). Chromate efflux by means of the ChrA chromate resistance protein from Pseudomonas aeruginosa. J Bacteriol, 18, 7398–7400.
   Google Scholar
• American Conference of Governmental Industrial Hygienists. (2004). Threshold limit values for chemical and physical agents and biological exposure indices. Cincinnati, OH: ACGIH.
   Google Scholar
• Assfalg, M., Bertini, I., Bruschi, M., Michel, C., and Turano, P. (2002). The metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c(7). Proc Natl Acad Sci USA, 99, 9750–9754.
   PubMed Web of Science ®Google Scholar
• Bae, W. C., Lee, H. K., Choe, Y. C., Jahng, D. J., Lee, S. H., Kim, S. J., Lee, J. H., and Jeong, B. C. (2005). Purification and characterization of NADPH-dependent Cr(VI) reductase from Escherichia coli ATCC 33456. J Microbiol, 43, 21–27.
   PubMed Web of Science ®Google Scholar
• Barak, Y., Ackerley, D. F., Dodge, C. J., Banwari, L., Alex, C., Francis, A. J., and Matin, A. (2006). Analysis of novel soluble chromate and uranyl reductases and generation of an improved enzyme by directed evolution. Appl Environ Microbiol, 72, 7074–7082.
   PubMed Web of Science ®Google Scholar
• Bartlett, R. J., and Kimble, J. M. (1976a). Behaviour of chromium in soils: I. Trivalent forms. J Environ Qual, 5, 379–383.
   Web of Science ®Google Scholar
• Bartlett, R. J., and Kimble, J. M. (1976b). Behaviour of chromium in soils: II. Hexavalent forms. J Environ Qual, 5, 383–386.
   Web of Science ®Google Scholar
• Belchik, S. M., Kennedy, D. W., Dohnalkova, A. C., Wang, Y., Sevinc, P. C., Wu, H., Lin, Y., Lu, P. H., Fredrickson, J. K., and Shi, L. (2011). Extracellular reduction of hexavalent chromium by cytochromes MtrC and OmcA of Shewanella oneidensis MR-1. Appl Environ Microbiol, 77, 4035–4041.
   PubMed Web of Science ®Google Scholar
• Bopp, L. H., and Ehrlich, H. L. (1988). Chromate resistance and reduction in Pseudomonas fluorescens strain LB300. Arch Microbiol, 150, 426–431.
   Web of Science ®Google Scholar
• Branco, R., Chung, A. P., Johnston, T., Gurel, V., Morais, P., and Zhitkovich, A. (2008). The chromate inducible chrBACF operon from the transposable element TnOtChr confers resistance to chromium(VI) and superoxide. J Bacteriol, 190, 6996–7003.
   PubMed Web of Science ®Google Scholar
• Brown, S. D., Martin, M., Deshpande, S., Seal, S., Huang, K., Alm, E., Yang, Y., Wu, L., Yan, T., Liu, X., Arkin, A., Chourey, K., Zhou, J., and Thompson, D. K. (2006). Cellular response of Shewanella oneidensis to strontium stress. Appl Environ Microbiol, 72, 890–900.
   PubMed Web of Science ®Google Scholar
• Calder, L. M. (1988). Chromium contamination of groundwater. In: J. O. Nriagu and E. Nieboer (Eds.), Chromium in the natural and human environments (pp. 215–231). New York: Wiley.
   Google Scholar
• Cervantes, C., Campos-Garcia, J., Devars, S., Gutierrez-Corona, F., Loza-Tavera, H., Torres-Guzman, J. C., and Moreno-Sanchez, R. (2001). Interactions of chromium with microorganisms and plants. FEMS Microbiol Rev, 25, 335–347.
   PubMed Web of Science ®Google Scholar
• Cervantes, C., Ohtake, H., Chu, L., Misra, T. K., and Silver, S. (1990). Cloning, nucleotide sequence and expression of the chromate resistance determinant of Pseudomonas aeruginosa plasmid pUM505. J Bacteriol, 172, 287–291.
   PubMed Web of Science ®Google Scholar
• Cervantes, C., and Silver, S. (1992). Plasmid chromate resistance and chromate reduction. Plasmid, 27, 65–71.
   PubMed Web of Science ®Google Scholar
• Chardin, B., Giudici-Orticoni, M. T., De Luca, G., Guigliarelli, B., and Bruschi, M. (2003). Hydrogenases in sulfate-reducing bacteria function as chromium reductase. Appl Microbiol Biotechnol, 63, 315–321.
   PubMed Web of Science ®Google Scholar
• Cheung, K. H., Lai, H. Y., and Gu, J. D. (2006). Membrane-associated hexavalent chromium reductase of Bacillus megaterium TKW3 with induced expression. J Microbiol Biotechnol, 16, 855–862.
   Web of Science ®Google Scholar
• Chourey, K., Thompson, M. R., Morrell-Falvey, J., VerBerkmoes, N. C., Brown, S. D., Shah, M., Zhou, J. Z., Doktycz, M., Hettich, R. L., and Thompson, D. K. (2006). Global molecular and morphological effects of 24-hour chromium(VI) exposure on Shewanella oneidensis MR-1. Appl Environ Microbiol, 72, 6331–6344.
   PubMed Web of Science ®Google Scholar
• Clark, D. P. (1994). Chromate reductase activity of Enterobacter aerogenus is induced by nitrite. FEMS Microbiol Lett, 122, 233–238.
   PubMed Web of Science ®Google Scholar
• Codd, R., Dillon, C. T., Levina, A., and Lay, P. A. (2001). Studies on the genotoxicity of chromium: from the test tube to the cell. Coord Chem Rev, 216, 537–82.
   Web of Science ®Google Scholar
• Coleman, R. N. (1988). Chromium toxicity: effects on microorganisms with special reference to the soil matrix. In J. O. Nriagu and E. Nieboer (Eds.), Chromium in the natural and human environments (pp. 335–368). New York: Wiley.
   Google Scholar
• Czakó-Vér, K., Batiè, M., Raspor, P., Sipiczki, M., and Pesti, M. (1999). Hexavalent chromium uptake by sensitive and tolerant mutants of Schizosaccharomyces pombe. FEMS Microbiol Lett, 178, 109–115.
   PubMed Web of Science ®Google Scholar
• Czjzek, M., Arnoux, P., Haser, R., and Shepard, W. (2001). Structure of cytochrome c7 from Desulfuromonas acetoxidans at 1.9° resolution. Acta Crystallogr Sect D: Biol Crystallogr, 57, 670–678.
   PubMedGoogle Scholar
• Das, S., Mishra, J., Das, S. K., Pandey, S., Rao, D. S., Chakraborty, A., Sudarshan, M., Das, N. N., and Thatoi, H. N. (2014). Investigation on mechanism of Cr(VI) reduction and removalby Bacillus amyloliquefaciens, a novel chromate tolerant bacterium isolated from chromite mine soil. Chemosphere, 96, 112–121.
   PubMed Web of Science ®Google Scholar
• Department for Environment, Food and Rural Affairs. (2002). Soil guideline values for chromium contamination. R&D Publication SGV 4. Bristol, UK: Environment Agency.
   Google Scholar
• Dhal, B., Thatoi, H. N., Das, N. N., and Pandey, B. D. (2010). Reduction of hexavalent chromium by Bacillus sp. isolated from chromite mine soils and characterization of reduced product. J Chem Technol Biotechnol, 85, 1471–1479.
   Web of Science ®Google Scholar
• Diaz-Perez, C., Cervantes, C., Campos-Garcia, J., Julian-Sanchez, A., and Riveros-Rosas, H. (2007). Phylogenetic analysis of the chromate ion transporter (CHR) superfamily. FEBS J., 274, 6215–6227.
   PubMed Web of Science ®Google Scholar
• Dillon, C. T., Lay, P. A., Cholewa, M., Legge, GJF, Bonin, A. M., Collins, T. J., Kostka, K. L., and SheaMcCarthy, G. (1997). Microprobe X-ray absorption spectroscopic determination of the oxidation state of intracellular chromium following exposure of V79 Chinese hamster lung cells to genotoxic chromium complexes. Chem Res Toxicol, 10, 533–535.
   PubMed Web of Science ®Google Scholar
• Efstathiou, J. D., and McKay, L. L. (1977). Inorganic salts resistance associated with a lactose fermenting plasmid in Streptococcus lactis. J Bacteriol, 130, 257–265.
   PubMed Web of Science ®Google Scholar
• Elangovan, R., Abhipsa, S., Rohit, B., Ligy, P., and Chandraraj, K. (2006). Reduction of Cr(VI) by a Bacillus sp. Biotechnol Lett, 28, 247–252.
   PubMed Web of Science ®Google Scholar
• Elangovan, R., Philip, L., and Chandraraj, K. (2010). Hexavalent chromium reduction by free and immobilized cell-free extract of Arthrobacter rhombi-RE. Appl Biochem Biotechnol, 160, 81–97.
   PubMed Web of Science ®Google Scholar
• Ellis, L. B., Hershberger, C. D., Bryan, E. M., and Wackett, L. P. (2001). The University of Minnesota Biocatalysis/Biodegradation Database: emphasizing enzymes. Nucleic Acids Res, 29, 340–343.
   PubMed Web of Science ®Google Scholar
• Emsley, J. (2001). “Chromium.” nature's building blocks: An A-Z guide to the elements. Oxford, UK: Oxford University Press.
   Google Scholar
• Eswaramoorthy, S., Poulain, S., Hienerwadel, R., Bremond, N., Sylvester, M. D., Zhang, Y. B., Berthomieu, C., Van Der Lelie, D., and Matin, A. (2012). Crystal structure of ChrR-a quinone reductase with the capacity to reduce chromate. PLoS One, 7, e36017.
   PubMed Web of Science ®Google Scholar
• Flores-Alvarez, L. J., Corrales-Escobosa, A. R., Cortes-Penagos, C., Martinez-Pacheco, M., Wrobel-Zasada, K., Wrobel-Kaczmarczyk, K., Cervantes, C., and Gutierrez-Corona, F. (2012). The Neurospora crass a chr-1 gene is up-regulated by chromate and its encoded CHR-1 protein causes chromate sensitivity and chromium accumulation. Curr Genet, 58, 281–290.
   PubMed Web of Science ®Google Scholar
• Francisco, R., Alpoim, M. C., and Morais, P. V. (2002). Diversity of chromium-resistant and -reducing bacteria in a chromium contaminated activated sludge. J Appl Microbiol, 92, 837–843.
   PubMed Web of Science ®Google Scholar
• Fredrickson, J. K., Kostandarithes, H. M., Li, S. W., Plymale, A. E., and Daly, M. J. (2000). Reduction of Fe(III), Cr(VI), U(VI), and TC (VII) by Deinococcus radiodurans R1. Appl Environ Microbiol, 66, 2006–2011.
   PubMed Web of Science ®Google Scholar
• Friello, D. A., and Chakrabarty, A. M. (1980). Transposable mercury resistance in Pseudomonas putida. In C. Stuttard and K. R. Rozee (Eds.), Plasmids and transposons: environmental effects and maintenance mechanisms (pp. 249–260). New York: Academic Press.
   Google Scholar
• Gadd, G. M. (1992). Metals and microorganisms: a problem of definition. FEMS Microbiol Lett, 100, 197–203.
   PubMed Web of Science ®Google Scholar
• Gadd, G. M. (2010). Metals, minerals and microbes: geomicrobiology and bioremediation. Microbiol, 156, 609–643.
   PubMed Web of Science ®Google Scholar
• Ganguli, A., and Tripathi, A. K. (1999). Survival and Chromate reducing ability of Pseudomonas aeruginosa in tannery effluent. Lett Appl Microbiol, 28, 76–80.
   PubMed Web of Science ®Google Scholar
• Garbisu, C., Alkorta, I., Llama, M. J., and Serra, J. L. (1998). Aerobic chromate reduction by Bacillus subtilis. Biodegr, 9, 133–141.
   PubMed Web of Science ®Google Scholar
• Gonzalez, C. F., Ackerley, D. F., Lynch, S. V., and Matin, A. (2005). ChrR a soluble quinone reductase of Pseudomonas putida that defends against H2O2. J Biol Chem, 280, 22590–22595.
   PubMed Web of Science ®Google Scholar
• Gutiérrez-Mañero, F. J., Ramos-Solano, B., Probanza, A., Mehouachi, J., Tadeo, F. R., and Talon, M. (2001). The plant growth-promoting rhizobacteria Bacillus pumilus and Bacillus licheniformis produce high amounts of physiologically active gibberellins. Physiol Plant, 111, 206–211.
   Web of Science ®Google Scholar
• Handa, B. K. (1988). Occurrence and distribution of chromium in natural waters of India. In J. O. Nriagu and E. Nieboer (Eds.), Chromium in the natural and human environments (pp. 189–215). New York: Wiley.
   Google Scholar
• Hauser, L. J., Miriam, L., Brown, S. D., Larimer, F., Keller, K. L., Rapp-Giles, B. J., et al. (2011). Complete genome sequence and updated annotation of Desulfovibrio alaskensis G20. J Bacteriol, 193, 4268–4269.
   PubMed Web of Science ®Google Scholar
• Higuchi, Y., Kusunoki, M., Matsuura, Y., Yasuoka, N., and Kakudo, M. (1984). Refined structure of cytochrome c3 at 1.8° resolution. J Mol Biol, 172, 109–139.
   PubMed Web of Science ®Google Scholar
• Hu, P., Brodie, E. L., Suzuki, Y., McAdams, H. H., and Andersen, G. L. (2005). Whole-Genome transcriptional analysis of heavy metal stresses in Caulobacter crescentus. J Bacteriol, 187, 8437–8449.
   PubMed Web of Science ®Google Scholar
• Ishibashi, Y., Cervantes, C., and Silver, S. (1990). Chromium reduction in Pseudomonas putida. Appl Environ Microbiol, 56, 2268–2270.
   PubMed Web of Science ®Google Scholar
• James, B. R. (1996). The challenge of remediation chromium-contaminated soil. Environ Sci Technol, 30, 248–251.
   PubMed Web of Science ®Google Scholar
• Jin, H., Zhang, Y., Buchko, G. W., Varnum, S. M., Robinson, H., Squier, T. C., and Long, P. E. (2012). Structure determination and functional analysis of a chromate reductase from Gluconacetobacter hansenii. PLoS One, 7, e42432.
   PubMed Web of Science ®Google Scholar
• Juhnke, S., Peitzsch, N., Hubener, N., Grobe, C., and Nies, D. H. (2002). New genes involved in chromate resistance in Ralstonia metallidurans strain CH34. Arch Microbiol, 179, 15–25.
   PubMed Web of Science ®Google Scholar
• Kanmani, P., Aravind, J., and Preston, D. (2012). Remediation of chromium contaminants using bacteria. Int J Environ Sci Technol, 9, 183–193.
   Web of Science ®Google Scholar
• Kanojia, R. K., Junaid, M., and Murthy, R. C. (1998). Embryo and fetotoxicity of hexavalent chromium: a long-term study. Toxicol Lett, 95, 165–172.
   PubMed Web of Science ®Google Scholar
• Kiilunen, M. (1994). Occupational exposure to chromium and nickel in Finland-analysis of registries of hygienic measurements and biological monitoring. Ann Occup Hyg, 38, 171–187.
   PubMed Web of Science ®Google Scholar
• Kobori, H., Harrison-Bernard, L. M., and Navar, L. G. (2001). Expression of angiotensinogen mRNA and protein in angiotensin II-dependent hypertension. J American Soc Nephrol, 12, 431–439.
   PubMed Web of Science ®Google Scholar
• Kwak, Y. H., Lee, D. S., and Kim, H. B. (2003). Vibrio harveyi nitroreductase is also a chromate reductase. Appl Environ Microbiol, 69, 4390–4395.
   PubMed Web of Science ®Google Scholar
• Li, X., and Krumholz, L. R. (2009). Thioredoxin is involved in U(VI) and Cr(VI) reduction in Desulfovibrio desulfuricans G20. J Bacteriol, 191, 4924–4933.
   PubMed Web of Science ®Google Scholar
• Liu, G., Zhou, J., Lv, H., Xiang, X., Wang, J., Zhou, M., and Qv, Y. (2007). Azoreductase from Rhodobacter sphaeroides AS1.1737 is a flavodoxin that also functions as nitroreductase and flavin mononucleotide reductase. Appl Microbiol Biotechnol, 76, 1271–1279.
   PubMed Web of Science ®Google Scholar
• Lloyd, J. R., Ridley, J., Khizniak, T., Lyalikova, N. N., and Macaskie, L. E. (1999). Reduction of technetium by Desulfovibrio desulfuricans: biocatalyst characterization and use in a flowthrough bioreactor. Appl Environ Microbiol, 65, 2691–2696.
   PubMed Web of Science ®Google Scholar
• Lovely, D. R. (1995). Bioremediation of organic and metal contaminates with dissimilatory metal reduction. J Indust Microbiol, 14, 85–93.
   PubMedGoogle Scholar
• Lovley, D. R., and Phillips, J. P. E. (1994). Reduction of chromate by Desulfovibrio vulgaris and its c3 cytochrome. Appl Environ Microbiol, 60, 726–728.
   PubMed Web of Science ®Google Scholar
• Lu, Y. L., and Yang, J. L. (1995). Long term exposure to chromium(VI) oxide leads to defects in sulfate transport system in Chinese hamster ovary cells. J Cell Biochem, 57, 655–665.
   PubMed Web of Science ®Google Scholar
• Magnuson, T. S., Swenson, M. W., Paszczynski, A. J., Deobald, L. A., Kerk, D., and Cummings, D. E. (2010). Proteogenomic and functional analysis of chromate reduction in Acidiphilium cryptum JF-5, an Fe(III)-respiring acidophile. Biometals, 23, 1129–1138.
   PubMed Web of Science ®Google Scholar
• Matin, A. C. (2006). Development of combinatorial bacteria for metal and radionuclide bioremediation. Grant No. ER63627-1021953-0009581, Final Technical Report, Reporting period: 09/15/2003-06/15/2006.
   Google Scholar
• Michel, C., Brugna, M., Aubert, C., Bernadac, A., and Bruschi, M. (2001). Enzymatic reduction of chromate: comparative studies using sulfate reducing bacteria. Appl Microbiol Biotechnol, 55, 95–100.
   PubMed Web of Science ®Google Scholar
• Miranda, A. T., González, M. V., González, G, Vargas, E., Campos-García, J., and Cervantes, C. (2005). Involvement of DNA helicases in chromate resistance by Pseudomonas aeruginosa PAO1. Mutat Res, 578, 202–209.
   PubMed Web of Science ®Google Scholar
• Mishra, R. R., Dhal, B., Dutta, S. K., Dangar, T. K., Das, N. N., and Thatoi, H. N. (2012). Optimization and characterization of chromium (VI) reduction in saline condition by moderately halophilic Vigribacillus sp. isolated from mangrove soil of Bhitarkanika, India. J Hazard Mater, 227, 219–226.
   PubMed Web of Science ®Google Scholar
• Morais, P. V., Branco, R., and Francisco, R. (2011). Chromium resistance strategies and toxicity: what makes Ochrobactrum tritici 5bvl1 a strain highly resistant. Biometals, 24, 401–410.
   PubMed Web of Science ®Google Scholar
• Morokutti, A., Lyskowski, A., Sollner, S., Pointner, E., Fitzpatrick, T. B., Kratky, C., Gruber, K., and Macheroux, P. (2005). Structure and function of YcnD from Bacillus subtilis, a flavin containing oxidoreductase. J Biochem, 44, 13724–13733.
   Web of Science ®Google Scholar
• Nepple, B. B., Kessi, J., and Bachofen, R. (2000). Chromate reduction by Rhodobacter sphaeroides. J Ind Microbiol Biotechnol, 25, 198–203.
   Web of Science ®Google Scholar
• Nies, A., Nies, D. H., and Silver, S. (1990). Nucleotide sequence and expression of a plasmid-encoded chromate resistance determinant from Alcaligenes eutrophus. J Biol Chem, 265, 5648–5653.
   PubMed Web of Science ®Google Scholar
• Nies, D. H., Koch, S., Wachi, S., Peitzsch, N., and Saier, M. H. (1998). CHR, a novel family of prokaryotic proton motive force-driven transporters probably containing chromate/ sulfate antiporters. J Bacteriol, 180, 5799–5802.
   PubMed Web of Science ®Google Scholar
• Opperman, D. J., Piater, L. A., and van Heerden, E. (2008). A novel chromate reductase from Thermus scotoductus SA-01 related to old yellow enzyme. J Bacteriol, 190, 3076–3082.
   PubMed Web of Science ®Google Scholar
• Opperman, D. J., Sewell, B. T., Litthauer, D., Isupov, M. N., Littlechild, J. A., and van Heerden, E. (2010). Crystal structure of a thermostable old yellow enzyme from Thermus scotoductus SA-01. Biochem Biophys Res Commun, 393, 426–431.
   PubMed Web of Science ®Google Scholar
• Ortega, R., Fayard, B., Salome, M., Deves, G., and Susini, J. (2005). Chromium oxidation state imaging in mammalian cells exposed in vitro to soluble or particulate chromate compounds. Chem Res Toxicol, 18, 1512–1519.
   PubMed Web of Science ®Google Scholar
• Park, C.-H, Gonzalez, D., Ackerley, D., Keyhan, M., and Matin, A. (2002). Molecular engineering of soluble bacterial proteins with chromate reductase activity. In M. Pellei, A. Porta, and R. E. Hinchee (Eds.), Remediation and beneficial reuse of contaminated sediments (pp.. Columbus, OH: Batelle Press.
   Google Scholar
• Park, C. H., Keyhan, M., Wielinga, B., Fendorf, S., and Matin, A. (2000). Purification to homogeneity and characterization of a novel Pseudomonas putida chromate reductase. Appl Environ Microbiol, 66, 1788–1795.
   PubMed Web of Science ®Google Scholar
• Pesti, M., Gazdag, Z., Emri, T., Farkas, N., Koosz, Z., Belagy, J., and Pocsi, I. (2002). Chromate sensitivity in fission yeast is caused by increased glutathione reductase activity and peroxide overproduction. J Basic Microbiol, 42, 408–419.
   PubMed Web of Science ®Google Scholar
• Philip, L., Iyengar, L., and Venkobacchar, C. (1998). Cr(VI) reduction by Bacillus coagulans isolated from contaminated soils. J Environ Eng, 124, 1165–1170.
   Web of Science ®Google Scholar
• Pimentel, B. E., Moreno-Sanchez, R., and Cervantes, C. (2002). Efflux of chromate by Pseudomonas aeruginosa cells expressing the ChrA protein. FEMS Microbiol Lett, 212, 249–254.
   PubMed Web of Science ®Google Scholar
• Plaper, A., Jenko-Brinovec, S., Premzl, A., Kos, J., and Raspor, P. (2002). Genotoxicity of trivalent chromium in bacterial cells. Possible effects on DNA topology. Chem Res Toxicol, 15, 943–949.
   PubMed Web of Science ®Google Scholar
• Poljsak, B., Pocsi, I., Raspor, P., and Pesti, M. (2010). Interference of chromium with biological systems in yeasts and fungi: a review. J Basic Microbiol, 50, 21–36.
   PubMed Web of Science ®Google Scholar
• Prosser, G. A., Copp, J. N., Syddall, S. P., Williams, E. M., Smaill, J. B., Wilson, W. R., and Patterson, A. V. (2010). Discovery and evaluation of Escherichia coli nitroreductases that activate the anti-cancer prodrug CB1954. Biochem Pharmacol, 79, 678–687.
   PubMed Web of Science ®Google Scholar
• Puzon, G. J., Petersen, J. N., Roberts, A. G., Kramer, D. B., and Xun, L. (2002). A bacterial flavin reductase system reduces chromate to a soluble chromium (III)–NAD(+) complex. J Biochem Biophys Res Commun, 294, 76–81.
   PubMed Web of Science ®Google Scholar
• Rajkumar, M., Nagendran, R., Lee, K. J., and Lee, W. H. (2005). Characterization of a novel Cr(VI) reducing Pseudomonas sp. with plant growth-promoting potential. Current Microbiol, 50, 266–271.
   PubMed Web of Science ®Google Scholar
• Ramirez-Diaz, M. I., Diaz-Perez, C., Vargas, E., Riveros-Rosas, H., Campos-Garcia, J., and Cervantes, C. (2008). Mechanisms of bacterial resistance to chromium compounds. Biometals, 21, 321–332.
   PubMed Web of Science ®Google Scholar
• Rath, B. P., Das, S., Mohapatra, P. K. D., and Thatoi, H. (2014). Optimization of extracellular chromate reductase production by Bacillus amyloliquefaciens (CSB 9) isolated from chromite mine environment. Biocatal Agri Biotechnol, 3, 35–41.
   Google Scholar
• Reardon, C. L., Dohnalkova, A. C., Nachimuthu, P., Kennedy, D. W., Saffarini, D. A., Arey, B. W., Shi, L., Wang, Z., Moore, D., McLean, L. S., Moyles, D., Marshall, M. J., Zachara, J. M., Fredrickson, J. K., Beliaev, A. S. (2010). Role of outer-membrane cytochromes MtrC and OmcA in the biomineralization of ferrihydrite by Shewanella oneidensis MR-1. Geobiol, 8, 56–68.
   PubMed Web of Science ®Google Scholar
• Reynolds, M. F., Peterson-Roth, E. C., Bespalov, I. A., Johnston, T., Gurel, V. M., Menard, H. L., and Zhitkovich, A. (2009). Rapid DNA double-strand breaks resulting from processing of Cr-DNA cross-links by both MutS dimers. Cancer Res, 69, 1071–1079.
   PubMed Web of Science ®Google Scholar
• Robins, K. J., Hooks, D. O., Rehm, B. H. A., and Ackerley, D. F. (2013). Escherichia coli NemA is an efficient chromate reductase that can be biologically immobilized toprovide a cell free system for remediation of hexavalent chromium. PLoS One, 8, e59200.
   PubMed Web of Science ®Google Scholar
• Romanenko, V. I., and Korenkov, V. N. (1975). Bacterial reduction of ions. Inform Byul In-ta Biol Vnutr Vod Akad Nauk SSR, 25, 8.
   Google Scholar
• Ross, D. S., Sjogren, R. E., and Bartlett, R. J. (1981). Behavior of chromium in soils: IV. Toxicity to microorganisms. J Environ Qual, 2, 145–168.
   Google Scholar
• Saito, K., Thiele, D. J., Davio, M., Lockridge, O., and Massey, V. (1991). The cloning and expression of a gene encoding old yellow enzyme from Saccharomyces carlsbergensis. J Biol Chem, 266, 20720–20724.
   PubMed Web of Science ®Google Scholar
• Salnikow, K., and Zhitkovich, A. (2008). Genetic and epigenetic mechanisms in metal carcinogenesis and cocarcinogenesis: nickel, arsenic and chromium. Chem Res Toxicol, 21, 28–44.
   PubMed Web of Science ®Google Scholar
• Sass, B. M., and Rai, D. (1987). Solubility of amorphous chromium(III)-iron(III) hydroxide solid solutions. Inorg Chem, 26, 2228–2232.
   Web of Science ®Google Scholar
• Sedláček, V., Klumpler, T., Marek, J., and Kučera, I. (2014). The structural and functional basis of catalysis mediated by NAD(P)H:acceptor oxidoreductase (FerB) of Paracoccus denitrificans. PLoS One, 9, e96262.
   PubMed Web of Science ®Google Scholar
• Shen, H., and Wang, Y. T. (1993). Characterization of enzymatic reduction of hexavalent chromium by Escherichia coli ATCC 33456. Appl Environ Microbiol, 59, 3771–3777.
   PubMed Web of Science ®Google Scholar
• Shi, L., Chen, B., Wang, Z., Elias, D. A., Mayer, M. U., and Gorby, Y. A. (2006). Isolation of a high-affinity functional protein complex between OmcA and MtrC: Two outer membrane decaheme c-type cytochromes of Shewanella oneidensis MR-1. J Bacteriol, 188, 4705–4714.
   PubMed Web of Science ®Google Scholar
• Shi, X. L., and Dalal, N. S. (1990). Evidence for a fenton-type mechanism for the generation of OH radicals in the reduction of Cr(VI) in cellular media. Arch Biochem Biophys, 281, 90–95.
   PubMed Web of Science ®Google Scholar
• Suzuki, T., Miyata, N., Horitsu, H., Kawai, K., Takamizawa, K., Tai, Y., and Okazaki, M. (1992). NAD(P)H-dependent chromium(VI) reductase of Pseudomonas ambigua G-1: a Cr(V) intermediate is formed during the reduction of Cr(VI) to Cr(III). J Bacteriol, 174, 5340–5345.
   PubMed Web of Science ®Google Scholar
• Tamura, K., Dudley, J., Nei, M., and Kumar, S. (2007). MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Molecular Biology and Evolution 24:1596–1599. (Publication PDF at http://www.kumarlab.net/publications).
   Google Scholar
• Thacker, N. (2007). Research in pediatric practice: an untapped arena. Indian Pediatr, 44, 811–812.
   PubMed Web of Science ®Google Scholar
• Thacker, U., and Madamwar, D. (2005). Reduction of toxic chromium and partial localization of chromium reductase activity in bacterial isolate DM1. World J Microbiol Biotechnol, 21, 891–899.
   Web of Science ®Google Scholar
• Thacker, U., Parikh, R., Shouche, Y., and Madamwar, D. (2006). Hexavalent chromium reduction by Providencia sp. Proc Biochem, 41, 1332–1337.
   Web of Science ®Google Scholar
• Thatoi, H., Das, S., Mishra, J., Rath, B. P., and Das, N. (2014). Bacterial chromate reductase, a potential enzyme for bioremediation of hexavalent chromium: a review. J Environ Manage, 146, 383–399.
   PubMed Web of Science ®Google Scholar
• Thompson, M. R., Verberkmoes, N. C., Chourey, K., Shah, M., Thompson, D. K., and Hettich, R. L. (2007). Dosage-dependent proteome response of Shewanella oneidensis MR-1 to acute chromate challenge. J Proteome Res, 6, 1745–1757.
   PubMed Web of Science ®Google Scholar
• Tucker, M. D., Barton, L. L., and Thomson, B. M. (1998). Reduction of Cr, Mo, Se and U by Desulfovibrio desulfuricans immobilized in polyacrylamide gels. J Ind Microbiol Biotechnol, 20, 13–19.
   PubMed Web of Science ®Google Scholar
• Viti, C., and Giovannetti, L. (2001). Characterization of cultivable heterotrophic bacterial communities in Cr-polluted and unpolluted soils using Biolog and ARDRA approaches. Appl Soil Ecol, 28, 101–112.
   Web of Science ®Google Scholar
• Viti, C., Pace, A., and Giovannetti, L. (2003). Characterization of Cr (VI)-resistant bacteria isolated from chromium-contaminated soil by tannery activity. Curr Microbiol, 46, 1–5.
   PubMed Web of Science ®Google Scholar
• Wang, P. C., Mori, T., Komori, K., Sasatsu, M., Toda, K., and Ohtake, H. (1989). Isolation and characterization of an Enterobacter cloacae strain that reduces hexavalent chromium under anaerobic conditions. Appl Environ Microbiol, 55, 1665–1669.
   PubMed Web of Science ®Google Scholar
• Wang, P. C., Toda, K., Ohtake, H., Kusaka, I., and Yabe, I. (1991). Membrane-bound respiratory system of Enterobacter cloacae strain HO1 grown anaerobically with chromate. FEMS Microbiol Lett, 78, 11–15.
   Web of Science ®Google Scholar
• Zahoor, A., and Rehman, A. (2009). Isolation of Cr(VI) reducing bacteria from industrial effluents and their potential use in bioremediation of chromium containing wastewater. J Environ Sci, 21, 814–820.
   Web of Science ®Google Scholar
• Zenno, S., Saigo, K., Kanoh, H., and Inouye, S. (1994). Identification of the gene encoding the major NAD(P)H-flavin oxidoreductase of the bioluminescent bacterium Vibrio fischeri ATCC 7744. J Bacteriol, 176, 3536–3543.
   PubMed Web of Science ®Google Scholar