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Heme-iron in lipid oxidation
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LXXIII.—Oxidation of tartaric acid in presence of iron
Fenton, H. J. H. (1894) · J. Chem. Soc., Trans. · doi:10.1039/ct8946500899 · Cited by 3,179
The Pecking Order of Free Radicals and Antioxidants: Lipid Peroxidation, α-Tocopherol, and Ascorbate
Buettner, G. R. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1074 · Cited by 2,417
Reactivity of HO2/O− 2 radicals in aqueous solution
Bielski, B. H. J., Cabelli, D. E., Arudi, R. L., & Ross, A. B. (1985) · Journal of Physical and Chemical Reference Data · doi:10.1063/1.555739 · Cited by 2,169
Hydrogen peroxide in the human body
Halliwell, B., Clement, M. V., & Long, L. H. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02197-9 · Cited by 1,075
Transition metals as catalysts of “autoxidation” reactions
Miller, D. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90148-c · Cited by 739
Oxidation of nitrogen-oxides by bound dioxygen in hemoproteins
Doyle, M. P., & Hoekstra, J. W. (1981) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)80291-3 · Cited by 643
Mechanism of NO-induced oxidation of myoglobin and hemoglobin
Eich, R. F., Li, T., Lemon, D. D., Doherty, D. H., Curry, S. R., Aitken, J. F., Mathews, A. J., Johnson, K. A., Smith, R. D., Phillips, et al. (1996) · Biochemistry · doi:10.1021/bi960442g · Cited by 613
The Toxicities of Native and Modified Hemoglobins
Everse, J., & Hsia, N. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00499-6 · Cited by 346
Kinetic and Mechanistic Studies of the NO•-Mediated Oxidation of Oxymyoglobin and Oxyhemoglobin
Herold, S., Exner, M., & Nauser, T. (2001) · Biochemistry · doi:10.1021/bi002407m · Cited by 324
Sources and role of iron in lipid peroxidation
Minotti, G. (1993) · Chemical Research in Toxicology · doi:10.1021/tx00032a001 · Cited by 154
Research works printed but not linked: 105
- D. Kristensen, M.V. Kröger-Ohlsen, L.H. Skibsted, in: M.J. Morello, F. Shahidi, C.-T. Ho (Eds.), ACS Symposium Series 807, Free Radicals in Food, American Chemical Society, Washington, DC, 2002, pp. 114–125. · doi:10.1021/bk-2002-0807.ch008
- Brash, 1999, J. Biol. Chem., 274, 23679, 10.1074/jbc.274.34.23679 · DOI · Paper page
- Skibsted, 2000, Bull. IDF, 346, 4
- Carlsen, 2004, J. Agric. Food Chem., 52, 1675, 10.1021/jf030494u · DOI
- Garry, 1998, Nature, 395, 905, 10.1038/27681 · DOI · Paper page
- Frauenfelder, 2001, Proc. Natl. Acad. Sci. U.S.A., 98, 2370, 10.1073/pnas.041614298 · DOI · Paper page
- Sulc, 2004, J. Am. Chem. Soc., 162, 1096, 10.1021/ja0376184 · DOI
- Cho, 2003, J. Food Sci., 68
- Jacobsen, 2001, J. Agric. Food Chem., 49, 1009, 10.1021/jf000729r · DOI
- Taube, 1952, Chem. Rev., 50, 69, 10.1021/cr60155a003 · doi:10.1021/cr60155a003
- Hedström, 1953, Arkiv för Kemi., 6, 1
- Sylva, 1972, Rev. Pure Appl. Chem., 22, 115
- Welch, 2002, Arch. Biochem. Biophys., 397, 360, 10.1006/abbi.2001.2694 · DOI · Paper page
- Comporti, 2002, Free Radical Biol. Med., 32, 565, 10.1016/S0891-5849(02)00758-X · DOI
- Welch, 2002, Free Radical Biol. Med., 32, 577, 10.1016/S0891-5849(02)00760-8 · DOI · Paper page
- Kremer, 1999, Phys. Chem. Phys., 1, 3595, 10.1039/a903915e · DOI · Paper page
- Dunford, 2002, Coord. Chem. Rev., 233–234, 311, 10.1016/S0010-8545(02)00024-3 · DOI
- Koppenol, 1990, FEBS Lett., 264, 165, 10.1016/0014-5793(90)80239-F · DOI · Paper page
- Saran, 2000, Free Radical Res., 33, 567, 10.1080/10715760000301101 · DOI
- Buettner, 1997, Radiat. Res., 145, 532, 10.2307/3579271 · DOI · Paper page
- Brantley, 1993, J. Biol. Chem., 268, 6995, 10.1016/S0021-9258(18)53138-0 · DOI · Paper page
- McCord, 1969, J. Biol. Chem., 244, 6049, 10.1016/S0021-9258(18)63504-5 · DOI · Paper page
- De Grey, 2002, DNA Cell Biol., 21, 251, 10.1089/104454902753759672 · DOI · Paper page
- Gutteridge, 1990, Trends Biochem. Sci., 15, 129, 10.1016/0968-0004(90)90206-Q · DOI · Paper page
- Andersen, 2000, J. Agric. Food Chem., 48, 3106, 10.1021/jf000354+ · doi:10.1021/jf000354+
- Schaich, 1992, Lipids, 27, 209, 10.1007/BF02536181 · DOI · Paper page
- Puppo, 1988, Biochem. J., 249, 185, 10.1042/bj2490185 · DOI · Paper page
- Kanner, 2001, Free Radical Biol. Med., 31, 1388, 10.1016/S0891-5849(01)00718-3 · DOI · Paper page
- E. Antonini, M. Brunori, in: Hemoglobin and Myoglobin in their Reactions with Ligands, North-Holland Publishing Company, Amsterdam, Holland, 1971, pp. 327–347.
- Tsukahara, 1983, J. Biochem., 93, 15, 10.1093/oxfordjournals.jbchem.a134149 · doi:10.1093/oxfordjournals.jbchem.a134149
- E. Antonini, M. Brunori, in: Hemoglobin and Myoglobin in their Reactions with Ligands, North-Holland Publishing Company, Amsterdam, Holland, 1971, pp. 13–39.
- King, 1963, J. Biol. Chem., 238, 1520, 10.1016/S0021-9258(18)81216-9 · DOI · Paper page
- Patel, 1996, Free Radical Res., 25, 117, 10.3109/10715769609149916 · DOI
- Akkara, 2000, Macromolecules, 33, 2377, 10.1021/ma9906534 · DOI
- Everse, 1998, Free Radical Biol. Med., 24, 1338, 10.1016/S0891-5849(97)00451-6 · DOI
- George, 1955, Biochem. J., 60, 596, 10.1042/bj0600596 · DOI
- Kanner, 1985, Arch. Biochem. Biophys., 237, 314, 10.1016/0003-9861(85)90282-6 · DOI · Paper page
- Baron, 1997, J. Agric. Food Chem., 45, 1704, 10.1021/jf960639f · DOI
- Kröger-Ohlsen, 2000, Food Chem., 70, 209, 10.1016/S0308-8146(00)00082-0 · doi:10.1016/s0308-8146(00)00082-0
- Carlsen, 2000, J. Agric. Food Chem., 48, 204, 10.1021/jf9908906 · doi:10.1021/jf9908906
- Jørgensen, 1998, Free Radical Res., 28, 335, 10.3109/10715769809069285 · doi:10.3109/10715769809069285
- Mikkelsen, 1992, Z. Lebensm. Untersuch. Forsch., 194, 9, 10.1007/BF01191032 · doi:10.1007/bf01191032
- Reeder, 1998, Biochem. J., 330, 1317, 10.1042/bj3301317 · DOI
- Reeder, 2001, Free Radical Biol. Med., 30, 1311, 10.1016/S0891-5849(01)00534-2 · DOI
- Walter, 1983, FEBS Lett., 163, 292, 10.1016/0014-5793(83)80838-2 · DOI
- Egawa, 2000, J. Biol. Chem., 275, 34858, 10.1074/jbc.M004026200 · DOI
- Chance, 1986, Biochemistry, 25, 1259, 10.1021/bi00354a010 · DOI
- Yonetani, 1967, J. Biol. Chem., 242, 1974, 10.1016/S0021-9258(18)96096-5 · DOI
- Modi, 1991, J. Chem. Soc., Chem. Comm., 12, 830, 10.1039/c39910000830 · doi:10.1039/c39910000830
- Yusa, 1987, Biochemistry, 26, 6684, 10.1021/bi00395a018 · DOI
- Matsui, 1999, J. Am. Chem. Soc., 121, 9952, 10.1021/ja9914846 · doi:10.1021/ja9914846
- Redaelli, 2002, ChemBioChem., 3, 226, 10.1002/1439-7633(20020301)3:2/3<226::AID-CBIC226>3.0.CO;2-7 · doi:10.1002/1439-7633(20020301)3:2/3<226::aid-cbic226>3.0.co;2-7
- Allentoff, 1992, J. Am. Chem. Soc., 114, 9744, 10.1021/ja00051a003 · DOI
- Matsui, 1999, J. Biol. Chem., 274, 2838, 10.1074/jbc.274.5.2838 · DOI · Paper page
- Svistunenko, 2001, Biochim. Biophys. Acta, 1546, 365, 10.1016/S0167-4838(01)00157-1 · DOI
- Davies, 1988, Biochim. Biophys. Acta, 964, 28, 10.1016/0304-4165(88)90063-3 · doi:10.1016/0304-4165(88)90063-3
- Barr, 1995, J. Biol. Chem., 270, 12709, 10.1074/jbc.270.21.12709 · DOI
- Van der Zee, 1996, Free Radical Biol. Med., 20, 199, 10.1016/0891-5849(95)02031-4 · doi:10.1016/0891-5849(95)02031-4
- Dikalov, 1999, Free Radical Biol. Med., 27, 864, 10.1016/S0891-5849(99)00134-3 · DOI
- Jones, 2002, J. Chem. Soc., Perkin Trans., 2, 2044, 10.1039/b207709b · doi:10.1039/b207709b
- Adachi, 1993, Biochemistry, 32, 241, 10.1021/bi00052a031 · DOI · Paper page
- Mehan, 1961, J. Am. Chem. Soc., 83, 2232, 10.1021/ja01471a004 · doi:10.1021/ja01471a004
- Withburn, 1987, Arch. Biochem. Biophys., 253, 419, 10.1016/0003-9861(87)90195-0 · DOI
- Giulivi, 1990, J. Biol. Chem., 265, 19453, 10.1016/S0021-9258(17)45394-4 · DOI · Paper page
- Withburn, 1985, J. Inorg. Biochem., 24, 35, 10.1016/0162-0134(85)85012-1 · DOI
- Kröger-Ohlsen, 1997, J. Agric. Food Chem., 45, 668, 10.1021/jf9604798 · doi:10.1021/jf9604798
- Reeder, 2002, Biochemistry, 41, 367, 10.1021/bi011335b · DOI
- Beckman, 1994, Methods Enzymol., 233, 229, 10.1016/S0076-6879(94)33026-3 · DOI · Paper page
- Schmidt, 1994, Biochem. J., 301, 645, 10.1042/bj3010645 · DOI
- Conolly, 2002, J. Agric. Food Chem., 50, 5220, 10.1021/jf020289z · DOI
- Exner, 2000, Chem. Res. Toxicol., 13, 287, 10.1021/tx990201k · DOI
- Herold, 2003, Chem. Res. Toxicol., 16, 390, 10.1021/tx025595l · DOI
- Carlsen, 2003, J. Agric. Food Chem., 51, 5815, 10.1021/jf030067g · doi:10.1021/jf030067g
- Andersen, 1988, Acta Chem. Scand. A, 42, 226, 10.3891/acta.chem.scand.42a-0226 · doi:10.3891/acta.chem.scand.42a-0226
- Herold, 1998, FEBS Lett., 439, 85, 10.1016/S0014-5793(98)01345-3 · DOI
- Murphy, 1994, Methods Enzymol., 233, 240, 10.1016/S0076-6879(94)33027-1 · DOI · Paper page
- Gow, 1999, Proc. Natl. Acad. Sci. U.S.A., 96, 9027, 10.1073/pnas.96.16.9027 · DOI · Paper page
- Patel, 1996, J. Lipid Res., 37, 2361, 10.1016/S0022-2275(20)37485-X · DOI
- Ischiropoulos, 1995, FEBS Lett., 364, 279, 10.1016/0014-5793(95)00307-U · DOI · Paper page
- Cunin, 1986, Microbiol. Rev., 50, 314, 10.1128/MMBR.50.3.314-352.1986 · doi:10.1128/mmbr.50.3.314-352.1986 · Paper page
- Radi, 1998, Chem. Res. Toxicol., 11, 720, 10.1021/tx980096z · DOI · Paper page
- Khairutdinov, 2000, Biochemistry, 39, 14238, 10.1021/bi001270x · DOI
- Hensley, 2000, Free Radical Biol. Med., 28, 520, 10.1016/S0891-5849(00)00155-6 · DOI
- Witting, 2001, Biochem. Biophys. Res. Commun., 286, 352, 10.1006/bbrc.2001.5397 · DOI
- Bourassa, 2001, J. Am. Chem. Soc., 123, 5142, 10.1021/ja015621m · DOI
- Grzelak, 2001, Biochim. Biophys. Acta, 1528, 97, 10.1016/S0304-4165(01)00176-3 · DOI
- Lymar, 1996, Chem. Res. Toxicol., 9, 845, 10.1021/tx960046z · DOI · Paper page
- Squadrito, 1998, Free Radical Biol. Med., 25, 392, 10.1016/S0891-5849(98)00095-1 · DOI · Paper page
- Pryor, 1998, Free Radical Biol. Med., 23, 331, 10.1016/S0891-5849(97)00121-4 · DOI
- Goldstein, 1998, J. Am. Chem. Soc., 120, 3458, 10.1021/ja9733043 · DOI
- Wink, 1996, Methods Enzymol., 268, 12, 10.1016/S0076-6879(96)68006-9 · DOI
- Brannan, 2001, Trends Food Sci. Technol., 12, 164, 10.1016/S0924-2244(01)00073-5 · DOI
- Brannan, 2001, J. Agric. Food Chem., 49, 3074, 10.1021/jf001407q · DOI
- Romero, 2003, J. Biol. Chem., 278, 44049, 10.1074/jbc.M305895200 · DOI
- Hogg, 1999, Biochim. Biophys. Acta, 1411, 378, 10.1016/S0005-2728(99)00027-4 · DOI · Paper page
- Jourd’heuil, 1998, Nitric Oxide Biol. Chem., 2, 37, 10.1006/niox.1998.0167 · DOI
- Kelley, 1999, Arch. Biochem. Biophys., 370, 97, 10.1006/abbi.1999.1386 · DOI
- Gorbunov, 1998, Biochem. Biophys. Res. Commun., 244, 647, 10.1006/bbrc.1997.7951 · DOI
- Kanner, 1984, J. Agric. Food Chem., 32, 512, 10.1021/jf00123a023 · DOI
- Morrissey, 1985, Meat Sci., 14, 175, 10.1016/0309-1740(85)90063-4 · doi:10.1016/0309-1740(85)90063-4
- Kanner, 1996, Methods Enzymol., 269, 218, 10.1016/S0076-6879(96)69024-7 · DOI
- Møller, 2002, Biochim. Biophys. Acta, 1570, 129, 10.1016/S0304-4165(02)00186-1 · doi:10.1016/s0304-4165(02)00186-1
- Herold, 2001, J. Biol. Ing. Chem., 6, 543, 10.1007/s007750100231 · DOI
- Kanner, 1994, Meat Sci., 36, 169, 10.1016/0309-1740(94)90040-X · DOI · Paper page
- Møller, 2002, Chem. Rev., 102, 1167, 10.1021/cr000078y · DOI · Paper page
Cited by
What Is Responsible for the Initiating Chemistry of Iron-Mediated Lipid Peroxidation: An Update
Cheng, Z., & Li, Y. (2007) · Chemical Reviews · doi:10.1021/cr040077w · Cited by 211
Metadata
- Authors
- Carlsen, C. U., Møller, J. K. S., & Skibsted, L. H.
- Venue
- Coordination Chemistry Reviews
- Publisher
- Elsevier BV
- Published
- 2005-02
- Volume
- 249
- Issue
- 3-4
- Pages
- 485-498
- ISSN
- 0010-8545 (ISSN-L)
- OpenAlex
- W2088334726
- Cited by
- 240
- References
- 10
- FWCI
- 1.31
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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