Dr David Pattison

Senior Research Fellow
Medicine, Central Clinical School
Heart Research Institute

Telephone +61 2 8208 8900
Fax 9565 5584

Map

Research interests

I use a thorough kinetic and product characterisation approach to gain chemical mechanistic insight into processes that are implicated in the development and progression of inflammatory diseases such as atherosclerosis.

My research currently focuses on: (a) the peroxidase enzymes, myeloperoxidase and eosinophil peroxidase, and the potent oxidants that they produce (HOCl, HOBr and HOSCN). Myeloperoxidase is implicated in the progression of atherosclerosis and other inflammatory diseases. (b) identifying potential antioxidants against protein oxidation, particularly that mediated by free radicals. Radical-mediated protein damage occurs in numerous diseases and natural aging, thus development of new compounds with therapeutic potential is desirable.

Selected grants

2014

  • Protein oxidation induced by singlet oxygen and peroxyl radicals and its consequences; Davies M, Pattison D; Australian Research Council (ARC)/Discovery Projects (DP).
  • Assessing the fate of tryptophan radicals in peptides and proteins: the balance between crosslinks and peroxides; Pattison D; Australian Institute of Nuclear Science and Engineering (AINSE)/Awards.

2013

  • Does the chemical structure of selenol antioxidants affect their ability to scavenge protein radicals?; Pattison D; Australian Institute of Nuclear Science and Engineering (AINSE)/Awards.
  • SF-61SX2/s stopped-flow fluorimeter and Service and upgrade of SX-17MV stopped-flow spectrometer; Clarke R, Davies M, Lay P, Witting P, Rasmussen H, Matthews J, Pattison D, Vandenberg J; National Health and Medical Research Council (NHMRC)/Equipment Grants.

2012

  • Are selenium based antioxidants effective in the repair of protein radicals?; Pattison D, Davies M, Anderson R; Australian Institute of Nuclear Science and Engineering (AINSE)/Awards.

2011

  • Intercepting Trp- and Tyr-derived protein radicals with nitroxide antioxidants: Unravelling structural influences; Pattison D; Australian Institute of Nuclear Science and Engineering (AINSE)/Awards.

Selected publications

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Book Chapters

  • Hawkins, C., Pattison, D., Whiteman, M., Davies, M. (2007). Chlorination and nitration of DNA and nucleic acid components. In Evans M; Cooke M (Eds.), Oxidative Damage to Nucleic Acids, (pp. 14-39). United States: Springer.

Journals

  • Gad, N., Mizdrak, J., Pattison, D., Davies, M., Truscott, R., Jamie, J. (2014). Detection, quantification, and total synthesis of novel 3-hydroxykynurenine glucoside-derived metabolites present in human lenses. Investigative Ophthalmology & Visual Science, 55(2), 849-855. [More Information]
  • Morgan, P., Sheahan, P., Pattison, D., Davies, M. (2013). Methylglyoxal-induced modification of arginine residues decreases the activity of NADPH-generating enzymes. Free Radical Biology and Medicine, 61, 229-242. [More Information]
  • Hadfield, K., Pattison, D., Brown, B., Hou, L., Rye, K., Davies, M., Hawkins, C. (2013). Myeloperoxidase-derived oxidants modify apolipoprotein A-I and generate dysfunctional high-density lipoproteins: comparison of hypothiocyanous acid (HOSCN) with hypochlorous acid (HOCI). The Biochemical Journal, 449(2), 531-542. [More Information]
  • Karton, A., O'Reilly, R., Pattison, D., Davies, M., Radom, L. (2012). Computational design of effective, bioinspired HOCI antioxidants: The role of intramolecular C1(+) and H(+) shifts. Journal of the American Chemical Society, 134(46), 19240-19245. [More Information]
  • Talib, J., Pattison, D., Harmer, J., Celermajer, D., Davies, M. (2012). High plasma thiocyanate levels modulate protein damage induced by myeloperoxidase and perturb measurement of 3-chlorotyrosine. Free Radical Biology and Medicine, 53(1), 20-29. [More Information]
  • Barrett, T., Pattison, D., Leonard, S., Carroll, K., Davies, M., Hawkins, C. (2012). Inactivation of thiol-dependent enzymes by hypothiocyanous acid: role of sulfenyl thiocyanate and sulfenic acid intermediates. Free Radical Biology and Medicine, 52(6), 1075-1085. [More Information]
  • Cook, N., Pattison, D., Davies, M. (2012). Myeloperoxidase-derived oxidants rapidly oxidize and disrupt zinc-cysteine/histidine clusters in proteins. Free Radical Biology and Medicine, 53(11), 2072-2080. [More Information]
  • Pattison, D., Rahmanto, A., Davies, M. (2012). Photo-oxidation of proteins. Photochemical and Photobiological Sciences, 11(1), 38-53. [More Information]
  • Rahmanto, A., Pattison, D., Davies, M. (2012). Photo-oxidation-induced inactivation of the selenium-containing protective enzymes thioredoxin reductase and glutathione peroxidase. Free Radical Biology and Medicine, 53(6), 1308-1316. [More Information]
  • Storkey, C., Pattison, D., White, J., Schiesser, C., Davies, M. (2012). Preventing Protein Oxidation with Sugars: Scavenging of Hypohalous Acids by 5-Selenopyranose and 4-Selenofuranose Derivatives. Chemical Research in Toxicology, 25(11), 2589-2599. [More Information]
  • Morgan, P., Pattison, D., Davies, M. (2012). Quantification of hydroxyl radical-derived oxidation products in peptides containing glycine, alanine, valine, and proline. Free Radical Biology and Medicine, 52(2), 328-339. [More Information]
  • Pattison, D., Davies, M., Hawkins, C. (2012). Reactions and reactivity of myeloperoxidase-derived oxidants: Differential biological effects of hypochlorous and hypothiocyanous acids. Free Radical Research, 46(8), 975-995. [More Information]
  • Skaff, O., Pattison, D., Morgan, P., Bachana, R., Jain, V., Priyadarsini, I., Davies, M. (2012). Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: determination of absolute rate constants and implications for biological damage. The Biochemical Journal, 441(1), 305-316. [More Information]
  • Pattison, D., Lam, M., Shinde, S., Anderson, R., Davies, M. (2012). The nitroxide TEMPO is an efficient scavenger of protein radicals: Cellular and kinetic studies. Free Radical Biology and Medicine, 53, 1664-1674. [More Information]
  • Morgan, P., Pattison, D., Talib, J., Summers, F., Harmer, J., Celermajer, D., Hawkins, C., Davies, M. (2011). High plasma thiocyanate levels in smokers are a key determinant of thiol oxidation induced by myeloperoxidase. Free Radical Biology and Medicine, 51(9), 1815-1822. [More Information]
  • Pattison, D., O'Reilly, R., Skaff, O., Radom, L., Anderson, R., Davies, M. (2011). One-electron Reduction of N-chlorinated and N-Brominated Species Is a Source of Radicals and Bromine Atom Formation. Chemical Research in Toxicology, 24(3), 371-382. [More Information]
  • Stanley, N., Pattison, D., Hawkins, C. (2010). Ability of Hypochlorous Acid and N-Chloramines to Chlorinate DNA and Its Constituents. Chemical Research in Toxicology, 23(7), 1293-1302. [More Information]
  • Koelsch, M., Mallak, R., Graham, G., Kajer, T., Milligan, M., Nguyen, L., Newsham, D., Keh, J., Kettle, A., Scott, K., Pattison, D., Hawkins, C., Davies, M., et al (2010). Acetaminophen (paracetamol) inhibits myeloperoxidase-catalyzed oxidant production and biological damage at therapeutically achievable concentrations. Biochemical Pharmacology, 79(8), 1156-1164. [More Information]
  • Szuchman-Sapir, A., Pattison, D., Davies, M., Witting, P. (2010). Site-specific hypochlorous acid-induced oxidation of recombinant human myoglobin affects specific amino acid residues and the rate of cytochrome b(5)-mediated heme reduction. Free Radical Biology and Medicine, 48(1), 35-46. [More Information]
  • Skaff, O., Pattison, D., Davies, M. (2009). Hypothiocyanous acid reactivity with low-molecular-mass and protein thiols: absolute rate constants and assessment of biological relevance. Biochemical Journal, 422(1), 111-117. [More Information]
  • Gracanin, M., Hawkins, C., Pattison, D., Davies, M. (2009). Singlet-oxygen-mediated amino acid and protein oxidation: formation of tryptophan peroxides and decomposition products. Free Radical Biology and Medicine, 47(1), 92-102. [More Information]
  • Pattison, D., Hawkins, C., Davies, M. (2009). What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach. Chemical Research in Toxicology, 22(5), 807-817. [More Information]
  • Szuchman-Sapir, A., Pattison, D., Ellis, N., Hawkins, C., Davies, M., Witting, P. (2008). Hypochlorous acid oxidizes methionine and tryptophan residues in myoglobin. Free Radical Biology and Medicine, 45(6), 789-798. [More Information]
  • Szuchman-Sapir, A., Pattison, D., Hamilton (Ellis), N., Hawkins, C., Davies, M., Witting, P. (2008). Hypochlorous acid oxidizes methionine and tryptophan residues in myoglobin. Free Radical Biology and Medicine, 45(6), 789-798.
  • Davies, M., Hawkins, C., Pattison, D., Rees, M. (2008). Mammalian heme peroxidases: from molecular mechanisms to health implications. Antioxidants & Redox Signaling, 10(7), 1199-1234. [More Information]
  • Lam, M., Pattison, D., Bottle, S., Keddie, D., Davies, M. (2008). Nitric Oxide and Nitroxides Can Act as Efficient Scavengers of Protein-Derived Free Radicals. Chemical Research in Toxicology, 21(11), 2111-2119. [More Information]
  • Morgan, P., Pattison, D., Hawkins, C., Davies, M. (2008). Separation, detection, and quantification of hydroperoxides formed at side-chain and backbone sites on amino acids, peptides, and proteins. Free Radical Biology and Medicine, 45(9), 1279-1289. [More Information]
  • Skaff, O., Pattison, D., Davies, M. (2008). The vinyl ether linkages of plasmalogens are favored targets for myeloperoxidase-derived oxidants: a kinetic study. Biochemistry, 47(31), 8237-8245. [More Information]
  • Hawkins, C., Pattison, D., Stanley, N., Davies, M. (2008). Tryptophan residues are targets in hypothiocyanous acid-mediated protein oxidation. Biochemical Journal, 416(3), 441-452. [More Information]
  • Pattison, D., Hawkins, C., Davies, M. (2007). Hypochlorous Acid-Mediated Protein Oxidation: How Important Are Chloramine Transfer Reactions and Protein Tertiary Structure? Biochemistry, 46(34), 9853-9864. [More Information]
  • Skaff, O., Pattison, D., Davies, M. (2007). Kinetics of hypobromous acid-mediated oxidation of lipid components and antioxidants. Chemical Research in Toxicology, 20(12), 1980-1988. [More Information]
  • Pattison, D., Davies, M. (2006). Actions of ultraviolet light on cellular structures. EXS, 96, 131-157. [More Information]
  • Pattison, D., Davies, M. (2006). Evidence for rapid inter- and intramolecular chlorine transfer reactions of histamine and carnosine chloramines: implications for the prevention of hypochlorous-Acid-mediated damage. Biochemistry, 45(26), 8152-8162. [More Information]
  • Pattison, D., Davies, M. (2006). Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases. Current Medicinal Chemistry, 13(27), 3271-3290. [More Information]
  • Pattison, D., Davies, M. (2005). Kinetic analysis of the role of histidine chloramines in hypochlorous acid mediated protein oxidation. Biochemistry, 44(19), 7378-7387. [More Information]
  • Rees, M., Pattison, D., Davies, M. (2005). Oxidation of heparan sulphate by hypochlorite: role of N-chloro derivatives and dichloramine-dependent fragmentation. Biochemical Journal, 391(Pt 1), 125-134. [More Information]
  • Pattison, D., Davies, M. (2004). Kinetic Analysis Of The Reactions Of Hypobromous Acid With Protein Components: Implications For Cellular Damage And Use Of 3-Bromotyrosine As A Marker Of Oxidative Stress. Biochemistry, 43(16), 4799-4809.
  • Levina, A., Foran, G., Pattison, D., Lay, P. (2004). X-Ray Absorption Spectroscopic And Electrochemical Studies Of Tris(Catecholato (2-))Chromate (V/I V/Iii) Complexes. Angewandte Chemie (International Edition), 43(4), 462-465. [More Information]
  • Hawkins, C., Pattison, D., Davies, M. (2003). Hypochlorite-induced oxidation of amino acids, peptides and proteins. Amino Acids, 25(3-4), 259-274. [More Information]
  • Pattison, D., Hawkins, C., Davies, M. (2003). Hypochlorous Acid-Mediated Oxidation of Lipid Components and Antioxidants Present in Low- Density Lipoproteins: Absolute Rate Constants, Product Analysis, and Computational Modeling. Chemical Research in Toxicology, 16(4), 439-449.
  • Hawkins, C., Pattison, D., Davies, M. (2002). Reaction of protein chloramines with DNA and nucleosides: evidence for the formation of radicals, protein-DNA cross-links and DNA fragmentation. Biochemical Journal, 365(3), 605-615.
  • Pattison, D., Levina, A., Lay, P., Davies, M. (2001). An investigation of the chromium oxidation state of a monoanionic chromium tris(catecholate) complex by X-ray absorption and EPR spectroscopies. Inorganic Chemistry, 40, 214-217.
  • Pattison, D., Levina, A., Lay, P., Davies, M., Dixon, N. (2001). Chromium(VI) reduction by catechol(amine)s results in DNA cleavage in vitro: Relevance to chromium genotoxicity. Chemical Research in Toxicology, 14, 500-510.

Conferences

  • Pattison, D., Davies, M. (2005). Histidine side-chain chloramines are important intermediates in HOCL-mediated protein oxidation. 13th Biennial Meeting of the Society for Free Radical Research, United Kingdom: Taylor and Francis.

2014

  • Gad, N., Mizdrak, J., Pattison, D., Davies, M., Truscott, R., Jamie, J. (2014). Detection, quantification, and total synthesis of novel 3-hydroxykynurenine glucoside-derived metabolites present in human lenses. Investigative Ophthalmology & Visual Science, 55(2), 849-855. [More Information]

2013

  • Morgan, P., Sheahan, P., Pattison, D., Davies, M. (2013). Methylglyoxal-induced modification of arginine residues decreases the activity of NADPH-generating enzymes. Free Radical Biology and Medicine, 61, 229-242. [More Information]
  • Hadfield, K., Pattison, D., Brown, B., Hou, L., Rye, K., Davies, M., Hawkins, C. (2013). Myeloperoxidase-derived oxidants modify apolipoprotein A-I and generate dysfunctional high-density lipoproteins: comparison of hypothiocyanous acid (HOSCN) with hypochlorous acid (HOCI). The Biochemical Journal, 449(2), 531-542. [More Information]

2012

  • Karton, A., O'Reilly, R., Pattison, D., Davies, M., Radom, L. (2012). Computational design of effective, bioinspired HOCI antioxidants: The role of intramolecular C1(+) and H(+) shifts. Journal of the American Chemical Society, 134(46), 19240-19245. [More Information]
  • Talib, J., Pattison, D., Harmer, J., Celermajer, D., Davies, M. (2012). High plasma thiocyanate levels modulate protein damage induced by myeloperoxidase and perturb measurement of 3-chlorotyrosine. Free Radical Biology and Medicine, 53(1), 20-29. [More Information]
  • Barrett, T., Pattison, D., Leonard, S., Carroll, K., Davies, M., Hawkins, C. (2012). Inactivation of thiol-dependent enzymes by hypothiocyanous acid: role of sulfenyl thiocyanate and sulfenic acid intermediates. Free Radical Biology and Medicine, 52(6), 1075-1085. [More Information]
  • Cook, N., Pattison, D., Davies, M. (2012). Myeloperoxidase-derived oxidants rapidly oxidize and disrupt zinc-cysteine/histidine clusters in proteins. Free Radical Biology and Medicine, 53(11), 2072-2080. [More Information]
  • Pattison, D., Rahmanto, A., Davies, M. (2012). Photo-oxidation of proteins. Photochemical and Photobiological Sciences, 11(1), 38-53. [More Information]
  • Rahmanto, A., Pattison, D., Davies, M. (2012). Photo-oxidation-induced inactivation of the selenium-containing protective enzymes thioredoxin reductase and glutathione peroxidase. Free Radical Biology and Medicine, 53(6), 1308-1316. [More Information]
  • Storkey, C., Pattison, D., White, J., Schiesser, C., Davies, M. (2012). Preventing Protein Oxidation with Sugars: Scavenging of Hypohalous Acids by 5-Selenopyranose and 4-Selenofuranose Derivatives. Chemical Research in Toxicology, 25(11), 2589-2599. [More Information]
  • Morgan, P., Pattison, D., Davies, M. (2012). Quantification of hydroxyl radical-derived oxidation products in peptides containing glycine, alanine, valine, and proline. Free Radical Biology and Medicine, 52(2), 328-339. [More Information]
  • Pattison, D., Davies, M., Hawkins, C. (2012). Reactions and reactivity of myeloperoxidase-derived oxidants: Differential biological effects of hypochlorous and hypothiocyanous acids. Free Radical Research, 46(8), 975-995. [More Information]
  • Skaff, O., Pattison, D., Morgan, P., Bachana, R., Jain, V., Priyadarsini, I., Davies, M. (2012). Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: determination of absolute rate constants and implications for biological damage. The Biochemical Journal, 441(1), 305-316. [More Information]
  • Pattison, D., Lam, M., Shinde, S., Anderson, R., Davies, M. (2012). The nitroxide TEMPO is an efficient scavenger of protein radicals: Cellular and kinetic studies. Free Radical Biology and Medicine, 53, 1664-1674. [More Information]

2011

  • Morgan, P., Pattison, D., Talib, J., Summers, F., Harmer, J., Celermajer, D., Hawkins, C., Davies, M. (2011). High plasma thiocyanate levels in smokers are a key determinant of thiol oxidation induced by myeloperoxidase. Free Radical Biology and Medicine, 51(9), 1815-1822. [More Information]
  • Pattison, D., O'Reilly, R., Skaff, O., Radom, L., Anderson, R., Davies, M. (2011). One-electron Reduction of N-chlorinated and N-Brominated Species Is a Source of Radicals and Bromine Atom Formation. Chemical Research in Toxicology, 24(3), 371-382. [More Information]

2010

  • Stanley, N., Pattison, D., Hawkins, C. (2010). Ability of Hypochlorous Acid and N-Chloramines to Chlorinate DNA and Its Constituents. Chemical Research in Toxicology, 23(7), 1293-1302. [More Information]
  • Koelsch, M., Mallak, R., Graham, G., Kajer, T., Milligan, M., Nguyen, L., Newsham, D., Keh, J., Kettle, A., Scott, K., Pattison, D., Hawkins, C., Davies, M., et al (2010). Acetaminophen (paracetamol) inhibits myeloperoxidase-catalyzed oxidant production and biological damage at therapeutically achievable concentrations. Biochemical Pharmacology, 79(8), 1156-1164. [More Information]
  • Szuchman-Sapir, A., Pattison, D., Davies, M., Witting, P. (2010). Site-specific hypochlorous acid-induced oxidation of recombinant human myoglobin affects specific amino acid residues and the rate of cytochrome b(5)-mediated heme reduction. Free Radical Biology and Medicine, 48(1), 35-46. [More Information]

2009

  • Skaff, O., Pattison, D., Davies, M. (2009). Hypothiocyanous acid reactivity with low-molecular-mass and protein thiols: absolute rate constants and assessment of biological relevance. Biochemical Journal, 422(1), 111-117. [More Information]
  • Gracanin, M., Hawkins, C., Pattison, D., Davies, M. (2009). Singlet-oxygen-mediated amino acid and protein oxidation: formation of tryptophan peroxides and decomposition products. Free Radical Biology and Medicine, 47(1), 92-102. [More Information]
  • Pattison, D., Hawkins, C., Davies, M. (2009). What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach. Chemical Research in Toxicology, 22(5), 807-817. [More Information]

2008

  • Szuchman-Sapir, A., Pattison, D., Ellis, N., Hawkins, C., Davies, M., Witting, P. (2008). Hypochlorous acid oxidizes methionine and tryptophan residues in myoglobin. Free Radical Biology and Medicine, 45(6), 789-798. [More Information]
  • Szuchman-Sapir, A., Pattison, D., Hamilton (Ellis), N., Hawkins, C., Davies, M., Witting, P. (2008). Hypochlorous acid oxidizes methionine and tryptophan residues in myoglobin. Free Radical Biology and Medicine, 45(6), 789-798.
  • Davies, M., Hawkins, C., Pattison, D., Rees, M. (2008). Mammalian heme peroxidases: from molecular mechanisms to health implications. Antioxidants & Redox Signaling, 10(7), 1199-1234. [More Information]
  • Lam, M., Pattison, D., Bottle, S., Keddie, D., Davies, M. (2008). Nitric Oxide and Nitroxides Can Act as Efficient Scavengers of Protein-Derived Free Radicals. Chemical Research in Toxicology, 21(11), 2111-2119. [More Information]
  • Morgan, P., Pattison, D., Hawkins, C., Davies, M. (2008). Separation, detection, and quantification of hydroperoxides formed at side-chain and backbone sites on amino acids, peptides, and proteins. Free Radical Biology and Medicine, 45(9), 1279-1289. [More Information]
  • Skaff, O., Pattison, D., Davies, M. (2008). The vinyl ether linkages of plasmalogens are favored targets for myeloperoxidase-derived oxidants: a kinetic study. Biochemistry, 47(31), 8237-8245. [More Information]
  • Hawkins, C., Pattison, D., Stanley, N., Davies, M. (2008). Tryptophan residues are targets in hypothiocyanous acid-mediated protein oxidation. Biochemical Journal, 416(3), 441-452. [More Information]

2007

  • Hawkins, C., Pattison, D., Whiteman, M., Davies, M. (2007). Chlorination and nitration of DNA and nucleic acid components. In Evans M; Cooke M (Eds.), Oxidative Damage to Nucleic Acids, (pp. 14-39). United States: Springer.
  • Pattison, D., Hawkins, C., Davies, M. (2007). Hypochlorous Acid-Mediated Protein Oxidation: How Important Are Chloramine Transfer Reactions and Protein Tertiary Structure? Biochemistry, 46(34), 9853-9864. [More Information]
  • Skaff, O., Pattison, D., Davies, M. (2007). Kinetics of hypobromous acid-mediated oxidation of lipid components and antioxidants. Chemical Research in Toxicology, 20(12), 1980-1988. [More Information]

2006

  • Pattison, D., Davies, M. (2006). Actions of ultraviolet light on cellular structures. EXS, 96, 131-157. [More Information]
  • Pattison, D., Davies, M. (2006). Evidence for rapid inter- and intramolecular chlorine transfer reactions of histamine and carnosine chloramines: implications for the prevention of hypochlorous-Acid-mediated damage. Biochemistry, 45(26), 8152-8162. [More Information]
  • Pattison, D., Davies, M. (2006). Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases. Current Medicinal Chemistry, 13(27), 3271-3290. [More Information]

2005

  • Pattison, D., Davies, M. (2005). Histidine side-chain chloramines are important intermediates in HOCL-mediated protein oxidation. 13th Biennial Meeting of the Society for Free Radical Research, United Kingdom: Taylor and Francis.
  • Pattison, D., Davies, M. (2005). Kinetic analysis of the role of histidine chloramines in hypochlorous acid mediated protein oxidation. Biochemistry, 44(19), 7378-7387. [More Information]
  • Rees, M., Pattison, D., Davies, M. (2005). Oxidation of heparan sulphate by hypochlorite: role of N-chloro derivatives and dichloramine-dependent fragmentation. Biochemical Journal, 391(Pt 1), 125-134. [More Information]

2004

  • Pattison, D., Davies, M. (2004). Kinetic Analysis Of The Reactions Of Hypobromous Acid With Protein Components: Implications For Cellular Damage And Use Of 3-Bromotyrosine As A Marker Of Oxidative Stress. Biochemistry, 43(16), 4799-4809.
  • Levina, A., Foran, G., Pattison, D., Lay, P. (2004). X-Ray Absorption Spectroscopic And Electrochemical Studies Of Tris(Catecholato (2-))Chromate (V/I V/Iii) Complexes. Angewandte Chemie (International Edition), 43(4), 462-465. [More Information]

2003

  • Hawkins, C., Pattison, D., Davies, M. (2003). Hypochlorite-induced oxidation of amino acids, peptides and proteins. Amino Acids, 25(3-4), 259-274. [More Information]
  • Pattison, D., Hawkins, C., Davies, M. (2003). Hypochlorous Acid-Mediated Oxidation of Lipid Components and Antioxidants Present in Low- Density Lipoproteins: Absolute Rate Constants, Product Analysis, and Computational Modeling. Chemical Research in Toxicology, 16(4), 439-449.

2002

  • Hawkins, C., Pattison, D., Davies, M. (2002). Reaction of protein chloramines with DNA and nucleosides: evidence for the formation of radicals, protein-DNA cross-links and DNA fragmentation. Biochemical Journal, 365(3), 605-615.

2001

  • Pattison, D., Levina, A., Lay, P., Davies, M. (2001). An investigation of the chromium oxidation state of a monoanionic chromium tris(catecholate) complex by X-ray absorption and EPR spectroscopies. Inorganic Chemistry, 40, 214-217.
  • Pattison, D., Levina, A., Lay, P., Davies, M., Dixon, N. (2001). Chromium(VI) reduction by catechol(amine)s results in DNA cleavage in vitro: Relevance to chromium genotoxicity. Chemical Research in Toxicology, 14, 500-510.

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