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Biomolecule−Mercury Interactions: Modalities of DNA Base−Mercury Binding Mechanisms. Remediation Strategies
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ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTBiomolecule−Mercury Interactions: Modalities of DNA Base−Mercury Binding Mechanisms. Remediation StrategiesIkenna Onyido, Albert R. Norris, and Erwin BuncelView Author Information Department of Chemistry and Center for Agrochemical Technology, University of Agriculture, Makurdi, Nigeria, and Department of Chemistry, Queen's University, Kingston, Canada K7L 3N6 Cite this: Chem. Rev. 2004, 104, 12, 5911–5930Publication Date (Web):October 6, 2004Publication History Received15 September 2003Published online6 October 2004Published inissue 1 December 2004https://pubs.acs.org/doi/10.1021/cr030443whttps://doi.org/10.1021/cr030443wresearch-articleACS PublicationsCopyright © 2004 American Chemical SocietyRequest reuse permissionsArticle Views2564Altmetric-Citations397LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Genetics,Ions,Mercury,Metals,Monomers Get e-Alerts
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Citations
Cites
Environmental Chemistry of Soils
McBride, M. B. (1994) · Medical Entomology and Zoology · Cited by 5,997
Principles of bioinorganic chemistry
(1995) · Choice Reviews Online · doi:10.5860/choice.32-4515 · Cited by 1,534
Bacterial mercury resistance from atoms to ecosystems
Barkay, T., Miller, S. M., & Summers, A. O. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00046-9 · Cited by 1,054
Biological Methylation of Mercury in Aquatic Organisms
JENSEN, S., & JERNELÖV, A. (1969) · Nature · doi:10.1038/223753a0 · Cited by 936
The relative affinities of ligand atoms for acceptor molecules and ions
Ahrland, S., Chatt, J., & Davies, N. R. (1958) · Quarterly Reviews, Chemical Society · doi:10.1039/qr9581200265 · Cited by 912
The biological chemistry of the elements
Exley, C. (1992) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(92)90327-6 · Cited by 717
The Biogeochemistry of mercury in the environment
Förstner, U. (1980) · Geochimica et Cosmochimica Acta · doi:10.1016/0016-7037(80)90239-2 · Cited by 645
Bioremedial potential of microbial mechanisms of metal mobilization and immobilization
Gadd, G. M. (2000) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(00)00095-1 · Cited by 567
Removal of Contaminants from Soils by Electric Fields
Probstein, R. F., & Hicks, R. E. (1993) · Science · doi:10.1126/science.260.5107.498 · Cited by 522
Microbial Transformations of Metals
Summers, A. O., & Silver, S. (1978) · Annual Review of Microbiology · doi:10.1146/annurev.mi.32.100178.003225 · Cited by 418
Photodegradation of methylmercury in lakes
Seller, P., Kelly, C. A., Rudd, J. W. M., & MacHutchon, A. R. (1996) · Nature · doi:10.1038/380694a0 · Cited by 396
Phytodetoxification of hazardous organomercurials by genetically engineered plants
Bizily, S. P., Rugh, C. L., & Meagher, R. B. (2000) · Nature Biotechnology · doi:10.1038/72678 · Cited by 380
Platinum and Other Metal Coordination Compounds in Cancer Chemotherapy
(1991) · Springer eBooks · doi:10.1007/978-1-4899-0738-7 · Cited by 374
The Crystal Structures of Purines, Pyrimidines and Their Intermolecular Complexes
Voet, D., & Rich, A. (1970) · Progress in Nucleic Acid Research and Molecular Biology · doi:10.1016/s0079-6603(08)60565-6 · Cited by 340
A PHYSICOCHEMICAL RATIONALE FOR THE BIOLOGICAL ACTIVITY OF MERCURY AND ITS COMPOUNDS
Hughes, W. L. (1957) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1956.tb36650.x · Cited by 326
Bizily, S. P., Rugh, C. L., Summers, A. O., & Meagher, R. B. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6808 · Cited by 272
Nucleic Acid–Metal Ion Interactions
(2008) · Royal Society of Chemistry eBooks · doi:10.1039/9781847558763 · Cited by 265
Nascimento, A. M. A., & Chartone‐Souza, E. (2003) · PubMed · Cited by 226
Brown, N. L., Ford, S. J., Pridmore, R. D., & Fritzinger, D. C. (1983) · Biochemistry · doi:10.1021/bi00286a015 · Cited by 225
DNA-bend modulation in a repressor-to-activator switching mechanism
Ansari, A. Z., Bradner, J. E., & O'Halloran, T. V. (1995) · Nature · doi:10.1038/374370a0 · Cited by 215
Glutathione depletion sensitizes tumor cells to oxidative cytolysis.
Arrick, B. A., Nathan, C. F., Griffith, O. W., & Cohn, Z. A. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68180-9 · Cited by 211
The aqueous solution chemistry of methylmercury and its complexes
Rabenstein, D. L. (1978) · Accounts of Chemical Research · doi:10.1021/ar50123a004 · Cited by 194
Steele, R. A., & Opella, S. J. (1997) · Biochemistry · doi:10.1021/bi9631632 · Cited by 192
Schottel, J. L. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34725-7 · Cited by 185
Mercury-199 NMR of the Metal Receptor Site in MerR and Its Protein-DNA Complex
Utschig, L. M., Bryson, J. W., & O'Halloran, T. V. (1995) · Science · doi:10.1126/science.7716541 · Cited by 183
Biliary secretion of glutathione and of glutathione-metal complexes*1
BALLATORI, N. (1985) · Fundamental and Applied Toxicology · doi:10.1016/0272-0590(85)90165-4 · Cited by 166
Pilot plant for bioremediation of mercury-containing industrial wastewater
Wagner‐Döbler, I. (2003) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-003-1322-7 · Cited by 157
Šponer, J., Sabat, M., Gorb, L., Leszczyński, J., Lippert, B., & Hobza, P. (2000) · The Journal of Physical Chemistry B · doi:10.1021/jp001711m · Cited by 151
Misra, T. K., Brown, N., Fritzinger, D. C., et al. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.19.5975 · Cited by 150
Ralston, D. M., & O’Halloran, T. V. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.10.3846 · Cited by 150
Cheesman, B. V., Arnold, A. P., & Rabenstein, D. L. (1988) · Journal of the American Chemical Society · doi:10.1021/ja00227a014 · Cited by 149
Wang, Y., Moore, M. W., Levinson, H. S., et al. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.1.83-92.1989 · Cited by 144
Christensen, J. J., Rytting, J. H., & Izatt, R. M. (1970) · Biochemistry · doi:10.1021/bi00827a012 · Cited by 142
Laddaga, R. A., Chu, L., Misra, T. K., & Silver, S. D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5106 · Cited by 137
Griffin, H. G., Foster, T. J., Silver, S. D., & Misra, T. K. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.10.3112 · Cited by 135
Mechanistic steps in the photoreduction of mercury in natural waters
Nriagu, J. O. (1994) · The Science of The Total Environment · doi:10.1016/0048-9697(94)90608-4 · Cited by 129
Increased free intrasynaptosomal Ca2+ by neurotoxic organometals: Distinctive mechanisms
Komulainen, H., & Bondy, S. C. (1987) · Toxicology and Applied Pharmacology · doi:10.1016/0041-008x(87)90271-7 · Cited by 126
Rabenstein, D. L., & Fairhurst, M. T. (1975) · Journal of the American Chemical Society · doi:10.1021/ja00841a015 · Cited by 125
Zamora, F., Kunsman, M., Sabat, M., et al. (1997) · Inorganic Chemistry · doi:10.1021/ic961167p · Cited by 119
Mercury and Organomercurial Resistances Determined by Plasmids in Pseudomonas
Clark, D., Weiss, A. A., & Silver, S. D. (1977) · Journal of Bacteriology · doi:10.1128/jb.132.1.186-196.1977 · Cited by 116
Genetic engineering of bacteria and their potential for Hg2+ bioremediation
Chen, S., & Wilson, D. B. (1997) · Biodegradation · doi:10.1023/a:1008233704719 · Cited by 112
Transposon A-generated mutations in the mercuric resistance genes of plasmid R100-1
Foster, T. J., Nakahara, H., Weiss, A. A., et al. (1979) · Journal of Bacteriology · doi:10.1128/jb.140.1.167-181.1979 · Cited by 112
Electrodialytic remediation of soils polluted with Cu, Cr, Hg, Pb and Zn
Hansen, H. K., Ottosen, L. M., Kliem, B. K., & Villumsen, A. (1997) · Journal of Chemical Technology & Biotechnology · Cited by 109
Arnold, A. P., Tan, K. S., & Rabenstein, D. L. (1986) · Inorganic Chemistry · doi:10.1021/ic00234a030 · Cited by 105
Electrokinetic Remediation of Mercury-Contaminated Soils Using Iodine/Iodide Lixiviant
Cox, C. D., Shoesmith, M. A., & Ghosh, M. M. (1996) · Environmental Science & Technology · doi:10.1021/es950633r · Cited by 104
Misra, T. K., Brown, N. L., Haberstroh, L., Schmidt, A., Goddette, D. W., & Silver, S. D. (1985) · Gene · doi:10.1016/0378-1119(85)90134-9 · Cited by 101
The Formation Constants of Mercury(II)−Glutathione Complexes
Oram, P. D., Fang, X., Fernaǹdo, Q., Letkeman, P., & Letkeman, D. (1996) · Chemical Research in Toxicology · doi:10.1021/tx9501896 · Cited by 98
Nakahara, H., Silver, S. D., Miki, T., et al. (1979) · Journal of Bacteriology · doi:10.1128/jb.140.1.161-166.1979 · Cited by 96
Morby, A. P., Hobman, J. L., & Brown, N. L. (1995) · Molecular Microbiology · doi:10.1111/j.1365-2958.1995.mmi_17010025.x · Cited by 84
Cloning and DNA sequence analysis of the mercury resistance genes of Streptomyces lividans
Sedlmeier, R., & Altenbuchner, J. (1992) · Molecular and General Genetics MGG · doi:10.1007/bf00279645 · Cited by 80
Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase
Miller, S. M., Moore, M. J., Massey, V., Williams, C. H., Distefano, M. D., Ballou, D. P., & Walsh, C. T. (1989) · Biochemistry · doi:10.1021/bi00429a037 · Cited by 79
Mechanisms of mercury bioremediation
Essa, A. M. M., Macaskie, L. E., & Brown, N. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300672 · Cited by 78
Bacterial resistance to mercury — reductio ad absurdum?
Brown, N. L. (1985) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(85)90069-6 · Cited by 77
Kusano, T., Ji, G. Y., Inoue, C., et al. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.5.2688-2692.1990 · Cited by 73
Rabenstein, D. L., & Isab, A. A. (1982) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(82)90092-1 · Cited by 70
Arrick, B. A., Nathan, C. F., & Cohn, Z. A. (1983) · Journal of Clinical Investigation · doi:10.1172/jci110766 · Cited by 66
Mercury transport and resistance
Brown, N., Shih, Y. C., Leang, C., et al. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300715 · Cited by 58
Distefano, M. D., Moore, M. J., & Walsh, C. T. (1990) · Biochemistry · doi:10.1021/bi00463a013 · Cited by 53
Engst, S., & Miller, S. M. (1999) · Biochemistry · doi:10.1021/bi982680c · Cited by 50
Immunomodulating effects after perinatal exposure to methylmercury in mice
Thuvander, A., Sundberg, J., & Oskarsson, A. (1996) · Toxicology · doi:10.1016/s0300-483x(96)03486-5 · Cited by 48
Distefano, M. D., Au, K. G., & Walsh, C. T. (1989) · Biochemistry · doi:10.1021/bi00429a035 · Cited by 45
Mercuric Ion Binding Abilities of MerP Variants Containing Only One Cysteine
Sahlman, L., & Skärfstad, E. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2289 · Cited by 44
Reniero, D., Galli, E., & Barbieri, P. (1995) · Gene · doi:10.1016/0378-1119(95)00546-4 · Cited by 44
The reaction between NADPH and mercuric reductase from Pseudomonas aeruginosa.
Sahlman, L., Lambeir, A., Lindskog, S., et al. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90760-x · Cited by 38
Ogawa, H. L., Tolle, C. L., & Summers, A. O. (1984) · Gene · doi:10.1016/0378-1119(84)90006-4 · Cited by 37
Baldwin, G. S., Waley, S. G., & Abraham, E. P. (1979) · Biochemical Journal · doi:10.1042/bj1790459 · Cited by 36
Miller, S. M., Massey, V., Williams, C. H., Ballou, D. P., & Walsh, C. T. (1991) · Biochemistry · doi:10.1021/bi00224a006 · Cited by 34
Biomethylation of mercury(II) adsorbed on mineral colloids common in freshwater sediments
Farrell, R. E., Huang, P., & Germida, J. J. (1998) · Applied Organometallic Chemistry · Cited by 33
C-Terminal cysteines of Tn501 mercuric ion reductase
Moore, M. J., Miller, S. M., & Walsh, C. T. (1992) · Biochemistry · doi:10.1021/bi00121a015 · Cited by 31
Eriksson, P., & Sahlman, L. (1993) · Journal of Biomolecular NMR · doi:10.1007/bf00198367 · Cited by 30
Isotopic hydrogen exchange in purines—mechanisms and applications
Jones, J. R. M., & Taylor, S. E. (1981) · Chemical Society Reviews · doi:10.1039/cs9811000329 · Cited by 29
Norris, A. R., Buncel, E., & Taylor, S. E. (1982) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)80265-2 · Cited by 26
Self-citationLiu, Y., Cotgreave, I. A., Atzori, L., et al. (1992) · Chemico-Biological Interactions · doi:10.1016/0009-2797(92)90053-n · Cited by 24
Engst, S., & Miller, S. M. (1998) · Biochemistry · doi:10.1021/bi9808161 · Cited by 21
Synthesis and applications of isotopically labelled compounds 1988
Basketter, N. S. (1990) · International Journal of Radiation Applications and Instrumentation Part A Applied Radiation and Isotopes · doi:10.1016/0883-2889(90)90094-w · Cited by 13
Bacterial Heavy Metal Detoxification and Resistance Systems
Silver, S. D. (1992) · Springer eBooks · doi:10.1007/978-0-585-32386-2_14 · Cited by 12
Prevention of organomercurial intoxication by thyroid deficiency in the rat
Szabó, S., Kourounakis, P., Kovács, K., Tuchweber, B., & Garg, B. D. (1974) · Toxicology and Applied Pharmacology · doi:10.1016/0041-008x(74)90089-1 · Cited by 9
Structure of a methylmercury complex with 4-nitroimidazole
Norris, A. R., Kumar, R., & Beauchamp, A. L. (1989) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(00)83132-1 · Cited by 6
Self-citationEngst, S., & Miller, S. M. (1999) · Biochemistry · doi:10.1021/bi9850571 · Cited by 3
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Metadata
- Authors
- Onyido, I., Norris, A. R., & Buncel, E.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2004-10-06
- Volume
- 104
- Issue
- 12
- Pages
- 5911-5930
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2041500335
- Cited by
- 440
- References
- 79
- FWCI
- 0.22
- Type
- journal article
- Language
- en
- Open access
- closed
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