Michael T Wilson

Summary

Affiliation: University of Essex
Country: UK

Publications

  1. doi request reprint Introduction: Andrew Thomson and the Centre for Metalloprotein Spectroscopy and Biology at the University of East Anglia
    Michael T Wilson
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, UK
    Biochem Soc Trans 36:1103-5. 2008
  2. ncbi request reprint Oxygen-binding haem proteins
    Michael T Wilson
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, UK
    Exp Physiol 93:128-32. 2008
  3. ncbi request reprint Reactions of nitric oxide with copper containing oxidases; cytochrome c oxidase and laccase
    Michael T Wilson
    Department of Biological Sciences, University of Essex, Colchester CO4 3SQ, UK
    IUBMB Life 56:7-11. 2004
  4. pmc Haptoglobin binding stabilizes hemoglobin ferryl iron and the globin radical on tyrosine β145
    Chris E Cooper
    School of Biological Sciences, University of Essex, Essex, United Kingdom
    Antioxid Redox Signal 18:2264-73. 2013
  5. doi request reprint An investigation into a cardiolipin acyl chain insertion site in cytochrome c
    Badri S Rajagopal
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, UK
    Biochim Biophys Acta 1817:780-91. 2012
  6. ncbi request reprint Ligand dynamics in an electron transfer protein. Picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome c
    Gary Silkstone
    Department of Biological Sciences, Wivenhoe Park, University of Essex, Colchester CO4 3SQ, United Kingdom
    J Biol Chem 282:1638-49. 2007
  7. pmc Ascorbate removes key precursors to oxidative damage by cell-free haemoglobin in vitro and in vivo
    Jacqueline Dunne
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK
    Biochem J 399:513-24. 2006
  8. pmc Tyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes
    Brandon J Reeder
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, UK
    J Biol Chem 283:30780-7. 2008
  9. ncbi request reprint The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology
    Brandon J Reeder
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, UK
    Antioxid Redox Signal 6:954-66. 2004
  10. doi request reprint Tyrosine as a redox-active center in electron transfer to ferryl heme in globins
    Brandon J Reeder
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, UK
    Free Radic Biol Med 44:274-83. 2008

Collaborators

Detail Information

Publications47

  1. doi request reprint Introduction: Andrew Thomson and the Centre for Metalloprotein Spectroscopy and Biology at the University of East Anglia
    Michael T Wilson
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, UK
    Biochem Soc Trans 36:1103-5. 2008
    ..J. Thomson and C. Greenwood, and charts the exceptional success that this centre has had in fostering bioinorganic chemistry in the U.K. and the impact that it has had internationally...
  2. ncbi request reprint Oxygen-binding haem proteins
    Michael T Wilson
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, UK
    Exp Physiol 93:128-32. 2008
    ..g. protection from reactive oxygen and nitrogen species. Haemoglobins are also widespread in plants and bacteria and may serve similar protective functions...
  3. ncbi request reprint Reactions of nitric oxide with copper containing oxidases; cytochrome c oxidase and laccase
    Michael T Wilson
    Department of Biological Sciences, University of Essex, Colchester CO4 3SQ, UK
    IUBMB Life 56:7-11. 2004
    ..The reactions of nitric oxide with copper containing oxidases such as cytochrome c oxidase and laccase are described and discussed in the present review...
  4. pmc Haptoglobin binding stabilizes hemoglobin ferryl iron and the globin radical on tyrosine β145
    Chris E Cooper
    School of Biological Sciences, University of Essex, Essex, United Kingdom
    Antioxid Redox Signal 18:2264-73. 2013
    ....
  5. doi request reprint An investigation into a cardiolipin acyl chain insertion site in cytochrome c
    Badri S Rajagopal
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, UK
    Biochim Biophys Acta 1817:780-91. 2012
    ....
  6. ncbi request reprint Ligand dynamics in an electron transfer protein. Picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome c
    Gary Silkstone
    Department of Biological Sciences, Wivenhoe Park, University of Essex, Colchester CO4 3SQ, United Kingdom
    J Biol Chem 282:1638-49. 2007
    ..Experiments on double mutants in which Phe-82 is replaced by Asp or Gly as well as the M80D substitution indicate that such steric changes substantially increase the motional freedom-dissociated CO...
  7. pmc Ascorbate removes key precursors to oxidative damage by cell-free haemoglobin in vitro and in vivo
    Jacqueline Dunne
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK
    Biochem J 399:513-24. 2006
    ..g. haemolytic anaemias, subarachnoid haemorrhage, rhabdomyolysis...
  8. pmc Tyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes
    Brandon J Reeder
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, UK
    J Biol Chem 283:30780-7. 2008
    ..Engineering hemoglobin with enhanced rates of ferryl removal, as we show here, is therefore likely to result in molecules better suited for in vivo oxygen delivery...
  9. ncbi request reprint The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology
    Brandon J Reeder
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, UK
    Antioxid Redox Signal 6:954-66. 2004
    ....
  10. doi request reprint Tyrosine as a redox-active center in electron transfer to ferryl heme in globins
    Brandon J Reeder
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, UK
    Free Radic Biol Med 44:274-83. 2008
    ..The consequence of a high-affinity through-protein electron transfer pathway to the cytotoxicity of ferryl heme is discussed...
  11. ncbi request reprint A new sensitive assay reveals that hemoglobin is oxidatively modified in vivo
    Niels B J Vollaard
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, UK
    Free Radic Biol Med 39:1216-28. 2005
    ..The exercise-induced increase is short-lived, suggesting the existence of an active mechanism for repairing or removing the damaged heme proteins...
  12. doi request reprint The role of the Cys-X-X-X-Cys motif on the kinetics of cupric ion loading to the Streptomyces lividans Sco protein
    Katie L I M Blundell
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, UK
    Dalton Trans 42:10608-16. 2013
    ..We put forward an explanation for this behaviour whereby we propose that the cupric ion is moving to a second site with no thiolate coordination. ..
  13. doi request reprint Lipid binding to cytoglobin leads to a change in haem co-ordination: a role for cytoglobin in lipid signalling of oxidative stress
    Brandon J Reeder
    Department of Biological Sciences, University of Essex, Colchester, Essex, UK
    Biochem J 434:483-92. 2011
    ..We propose that the binding of ferric cytoglobin to lipids and their subsequent transformation may be integral to the physiological function of cytoglobin, generating cell signalling lipid molecules under an oxidative environment...
  14. doi request reprint Modulating hemoglobin nitrite reductase activity through allostery: a mathematical model
    Zimei Rong
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK Centre for English Language Education, The University of Nottingham Ningbo China, 199 Taikang East Road, University Park, Ningbo, Zhejiang 315100, China Electronic address
    Nitric Oxide 35:193-8. 2013
    ..0087m(-1)s(-1) to 0.083m(-1)s(-1). ..
  15. pmc Ferryl haem protonation gates peroxidatic reactivity in globins
    Radu Silaghi-Dumitrescu
    Department of Biological Sciences, University of Essex, Colchester CO4 3SQ, UK
    Biochem J 403:391-5. 2007
    ..We also demonstrate for the first time a direct correlation between Hb/Mb ferryl reactivity and ferryl protonation status, simultaneously informing on chemical mechanism and toxicity and with broader biochemical implications...
  16. pmc Comparative study of tyrosine radicals in hemoglobin and myoglobins treated with hydrogen peroxide
    Dimitri A Svistunenko
    Department of Biological Sciences, Central Campus, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK
    Biophys J 83:2845-55. 2002
    ..Tyr103 is the closest to the heme. We suggest that Tyr103 is the initial site of the radical, which then rapidly migrates to Tyr151...
  17. pmc Nitric oxide inhibition of respiration involves both competitive (heme) and noncompetitive (copper) binding to cytochrome c oxidase
    Maria G Mason
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom
    Proc Natl Acad Sci U S A 103:708-13. 2006
    ..The combination of competitive (heme) and noncompetitive (copper) modes of binding enables NO to interact with mitochondria across the full in vivo dynamic range of oxygen tension and consumption rates...
  18. ncbi request reprint Hemoglobin and myoglobin associated oxidative stress: from molecular mechanisms to disease States
    Brandon J Reeder
    Department of Biological Sciences, University of Essex, Colchester, Essex CO4 3SQ UK
    Curr Med Chem 12:2741-51. 2005
    ..Suppression of the peroxidatic activity of hemoglobin is discussed in the context of the development of blood substitutes...
  19. pmc Nitric oxide binds to the proximal heme coordination site of the ferrocytochrome c/cardiolipin complex: formation mechanism and dynamics
    Gary Silkstone
    Department of Biological Sciences, Wivenhoe Park, University of Essex, Colchester CO4 3SQ, United Kingdom
    J Biol Chem 285:19785-92. 2010
    ..These features all point at a remarkable mobility of the proximal heme environment induced by cardiolipin...
  20. ncbi request reprint Histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin
    Brandon J Reeder
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, UK
    IUBMB Life 59:477-89. 2007
    ..The distal histidine is, therefore, vital for the formation of haem to protein cross-link and we explore this outcome...
  21. ncbi request reprint The heme domain of cellobiose oxidoreductase: a one-electron reducing system
    Maria G Mason
    Department of Biological Sciences, University of Essex, Colchester, UK
    Biochim Biophys Acta 1604:47-54. 2003
    ..Analogous reactions with natural one-electron acceptors can promote Fenton chemistry, which may explain evolutionary retention of the heme domain and the enzyme's unique character among secreted sugar dehydrogenases...
  22. ncbi request reprint Fast reduction of a copper center in laccase by nitric oxide and formation of a peroxide intermediate
    Jaume Torres
    Department of Biological Sciences, University of Essex, Wivenhoe Park CO4 3SQ, Colchester, Essex, UK
    J Am Chem Soc 124:963-7. 2002
    ..This enables the O-O scission step in the catalytic cycle to be studied by electron addition to the peroxide derivative through the native electron entry site, type 1 copper...
  23. ncbi request reprint EPR and optical spectroscopic studies of Met80X mutants of yeast ferricytochrome c. Models for intermediates in the alkaline transition
    Gary G Silkstone
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, Essex, UK
    J Am Chem Soc 127:92-9. 2005
    ..The ligand sets and the pK values of the transitions are rationalized in terms of the structure of the heme pocket, and a possible mechanism of the "trigger" in the alkaline transition of the native protein is suggested...
  24. ncbi request reprint Desferrioxamine inhibits production of cytotoxic heme to protein cross-linked myoglobin: a mechanism to protect against oxidative stress without iron chelation
    Brandon J Reeder
    Department of Biological Sciences, Central Campus, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, United Kingdom
    Chem Res Toxicol 18:1004-11. 2005
    ..Thus, the ameliorative effects of treatment of posthemolytic events by desferrioxamine cannot be exclusively assigned to its ability to chelate free iron...
  25. doi request reprint Iron chelators can protect against oxidative stress through ferryl heme reduction
    Brandon J Reeder
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, UK
    Free Radic Biol Med 44:264-73. 2008
    ..The antioxidant effects of chelators in vivo cannot, therefore, be attributed solely to iron chelation...
  26. doi request reprint A model for the nitric oxide producing nitrite reductase activity of hemoglobin as a function of oxygen saturation
    Zimei Rong
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK
    Nitric Oxide 33:74-80. 2013
    ..This has allowed the calculation of the hemoglobin nitrite reductase activity rate profiles for the human hemoglobin and for bovine hemoglobin. The properties of these rate profiles are discussed. ..
  27. doi request reprint Engineering tyrosine-based electron flow pathways in proteins: the case of aplysia myoglobin
    Brandon J Reeder
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, United Kingdom
    J Am Chem Soc 134:7741-9. 2012
    ....
  28. ncbi request reprint Oxygen reduction by cellobiose oxidoreductase: the role of the haem group
    Maria G Mason
    Department of Biological Sciences, University of Essex, Wivenhoe Park, CO4 3SQ, Colchester, UK
    FEBS Lett 518:29-32. 2002
    ..We discuss this mechanism in relationship to the biological function of this enzyme, namely lignocellulose degradation...
  29. ncbi request reprint On the formation, nature, stability and biological relevance of the primary reaction intermediates of myoglobins with hydrogen peroxide
    Chris E Cooper
    Department of Biological Sciences, University of Essex, Colchester, UK CO4 3SQ
    Dalton Trans . 2005
    ..Myoglobin can therefore act as a true ascorbate peroxidase. Ascorbate in vivo may be critical in controlling and preventing toxic side reactions of this and related haem proteins...
  30. pmc Heterogeneity in the Histidine-brace Copper Coordination Sphere in Auxiliary Activity Family 10 (AA10) Lytic Polysaccharide Monooxygenases
    Amanda K Chaplin
    From the School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom
    J Biol Chem 291:12838-50. 2016
    ..Our findings highlight that heterogeneity exists in the active site copper coordination sphere of LPMOs that may have implications for the mechanism of loading copper in the cell...
  31. ncbi request reprint Reaction of Aplysia limacina metmyoglobin with hydrogen peroxide
    Dimitri A Svistunenko
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, United Kingdom
    Dalton Trans . 2007
    ..All intermediates of the reaction are kinetically characterised...
  32. pmc Morphological development and cytochrome c oxidase activity in Streptomyces lividans are dependent on the action of a copper bound Sco protein
    Katie L I M Blundell
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK
    Open Biol 3:120163. 2013
    ..The mechanism of cupric ion capture by Sco(Sl) has been investigated, and an important role for a conserved His residue is identified...
  33. doi request reprint Structural and kinetic studies of imidazole binding to two members of the cytochrome c (6) family reveal an important role for a conserved heme pocket residue
    Badri S Rajagopal
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, UK
    J Biol Inorg Chem 16:577-88. 2011
    ....
  34. ncbi request reprint Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin
    Brandon J Reeder
    Department of Biological Sciences, Central Campus, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, United Kingdom
    Biochemistry 41:367-75. 2002
    ..g., therapy for rhabdomyolysis-associated renal dysfunction...
  35. doi request reprint Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding
    Penny Beckerson
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, United Kingdom
    FEBS Lett 589:507-12. 2015
    ..We present a model that describes how the cysteine redox state of the monomer controls histidine dissociation rate constants and hence extrinsic ligand binding...
  36. doi request reprint Cytoglobin ligand binding regulated by changing haem-co-ordination in response to intramolecular disulfide bond formation and lipid interaction
    Penny Beckerson
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, U K
    Biochem J 465:127-37. 2015
    ..The redox state of these cysteine residues in vivo is therefore highly significant and may be a mechanism to modulate the biochemical properties of the haem under conditions of stress...
  37. doi request reprint The hydrogen-peroxide-induced radical behaviour in human cytochrome c-phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant
    Badri S Rajagopal
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, U K
    Biochem J 456:441-52. 2013
    ....
  38. ncbi request reprint Production and characterisation of Met80X mutants of yeast iso-1-cytochrome c: spectral, photochemical and binding studies on the ferrous derivatives
    Gary Silkstone
    Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, UK
    Biophys Chem 98:65-77. 2002
    ..The potential of these proteins to act as light activated electron donors for the study of electron transfer is discussed...
  39. doi request reprint Active site maturation and activity of the copper-radical oxidase GlxA is governed by a tryptophan residue
    Amanda K Chaplin
    School of Biolgical Sciences, University of Essex, Wivenhoe Park, Colchester, N A, CO4 3SQ, United Kingdom
    Biochem J . 2017
    ....
  40. pmc Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute design
    Gary G A Silkstone
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, U K
    Biochem J 473:3371-83. 2016
    ..This class of mutations has the potential to decrease adverse side effects as one component of a HBOC product. ..
  41. doi request reprint Conformational control of the binding of diatomic gases to cytochrome c'
    Andreea Manole
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, UK
    J Biol Inorg Chem 20:675-86. 2015
    ..The binding of distal ligands is thus controlled by the conformation of the phenylalanine ring. Only a proximal 5-coordinate NO adduct, confirmed by structural data, is observed with no detectable hexacoordinate distal NO adduct. ..
  42. doi request reprint NO binding to the proapoptotic cytochrome c-cardiolipin complex
    Michael A Hough
    School of Biological Sciences, University of Essex, Colchester, United Kingdom
    Vitam Horm 96:193-209. 2014
    ..Insights into the structure of the complex are provided by comparison with cytochrome c' for which X-ray structures are available. ..
  43. ncbi request reprint Exercise-induced hemolysis is caused by protein modification and most evident during the early phase of an ultraendurance race
    Ashril Yusof
    Centre for Sports and Exercise Science, Dept of Biological Sciences, Univ of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom
    J Appl Physiol (1985) 102:582-6. 2007
    ..Exercise-induced hemolysis reflects alterations in erythrocyte membrane spectrins and occurs particularly in the early phase of an ultraendurance race because of a relative older cell population...
  44. ncbi request reprint Imaging the production of singlet oxygen in vivo using a new fluorescent sensor, Singlet Oxygen Sensor Green
    Cristina Flors
    Department of Biological Sciences, University of Essex, Colchester, Essex CO4 3SQ, UK
    J Exp Bot 57:1725-34. 2006
    ..Wounding of leaves was followed by an increase in SOSG fluorescence, even in the dark. It is concluded that SOSG is a useful in vivo probe for the detection of singlet oxygen...
  45. pmc Increased dynamics in the 40-57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation
    Andreas Ioannis Karsisiotis
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, UK
    Sci Rep 6:30447. 2016
    ....
  46. pmc A Further Investigation of the Effects of Extremely Low Frequency Magnetic Fields on Alkaline Phosphatase and Acetylcholinesterase
    Gary Silkstone
    School of Biology, University of Essex, Wivenhoe Park, Colchester, Essex, CO4 3SQ, United Kingdom
    PLoS ONE 11:e0148369. 2016
    ..We discuss possible reasons for the discrepancy between this and earlier work and note the particularly complex influence of small temperature changes that may confound analysis. ..
  47. doi request reprint Copper and nickel bind via two distinct kinetic mechanisms to a CsoR metalloregulator
    Tatiana V Porto
    School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, UK
    Dalton Trans 44:20176-85. 2015
    ..In particular Ni(II) has two binding sites; one that has identical amino acid coordination as the Cu(I) binding site and the second involving His103, a residue determined here not to be involved in the mechanism of Cu(I) binding...