| Year |
Citation |
Score |
| 2020 |
Lučić M, Chaplin AK, Moreno-Chicano T, Dworkowski FSN, Wilson MT, Svistunenko DA, Hough MA, Worrall JAR. A subtle structural change in the distal haem pocket has a remarkable effect on tuning hydrogen peroxide reactivity in dye decolourising peroxidases from Streptomyces lividans. Dalton Transactions (Cambridge, England : 2003). PMID 31942590 DOI: 10.1039/C9Dt04583J |
0.32 |
|
| 2019 |
Deacon OM, White RW, Moore GR, Wilson MT, Worrall JAR. Comparison of the structural dynamic and mitochondrial electron-transfer properties of the proapoptotic human cytochrome c variants, G41S, Y48H and A51V. Journal of Inorganic Biochemistry. 203: 110924. PMID 31760234 DOI: 10.1016/J.Jinorgbio.2019.110924 |
0.347 |
|
| 2019 |
Leiva Eriksson N, Reeder BJ, Wilson MT, Bülow L. Sugar beet hemoglobins: reactions with nitric oxide and nitrite reveal differential roles for nitrogen metabolism. The Biochemical Journal. PMID 31285352 DOI: 10.1042/Bcj20190154 |
0.308 |
|
| 2019 |
Chaplin AK, Chicano TM, Hampshire BV, Wilson MT, Hough MA, Svistunenko DA, Worrall JAR. An Aromatic Dyad Motif in Dye Decolourising Peroxidases Has Implications for Free Radical Formation and Catalysis. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 30945782 DOI: 10.1002/Chem.201806290 |
0.338 |
|
| 2018 |
Deacon OM, Svistunenko DA, Moore GR, Wilson MT, Worrall JAR. Naturally occurring disease-related mutations in the 40-57 Ω-loop of human cytochrome c control triggering of the alkaline isomerisation. Biochemistry. PMID 29949346 DOI: 10.1021/Acs.Biochem.8B00520 |
0.337 |
|
| 2017 |
Deacon OM, Karsisiotis AI, Moreno Chicano T, Hough MA, Macdonald CJ, Blumenschein T, Wilson MT, Moore GR, Worrall JAR. Heightened dynamics of the oxidized Y48H variant of human cytochrome c increases its peroxidatic activity. Biochemistry. PMID 29083920 DOI: 10.1021/Acs.Biochem.7B00890 |
0.352 |
|
| 2017 |
Chaplin AK, Wilson MT, Worrall JAR. Kinetic characterisation of a dye decolourising peroxidase from Streptomyces lividans: new insight into the mechanism of anthraquinone dye decolourisation. Dalton Transactions (Cambridge, England : 2003). PMID 28695933 DOI: 10.1039/C7Dt01144J |
0.321 |
|
| 2017 |
Kekilli D, Petersen CA, Pixton DA, Ghafoor DD, Abdullah GH, Dworkowski FSN, Wilson MT, Heyes DJ, Hardman SJO, Murphy LM, Strange RW, Scrutton NS, Andrew CR, Hough MA. Engineering proximal vs. distal heme-NO coordination via dinitrosyl dynamics: implications for NO sensor design. Chemical Science. 8: 1986-1994. PMID 28451315 DOI: 10.1039/C6Sc04190F |
0.302 |
|
| 2017 |
Chaplin AK, Svistunenko DA, Hough M, Wilson MT, Vijgenboom E, Worrall JA. Active site maturation and activity of the copper-radical oxidase GlxA is governed by a tryptophan residue. The Biochemical Journal. PMID 28093470 DOI: 10.1042/Bcj20160968 |
0.312 |
|
| 2017 |
Ioannis Karsisiotis A, Deacon OM, Wilson MT, Macdonald C, Blumenschein TM, Moore GR, Worrall JA. The G41S Variant of Human Cytochrome C Enhances Apoptosis via Increased Dynamics Biophysical Journal. 112: 32a-33a. DOI: 10.1016/J.Bpj.2016.11.210 |
0.343 |
|
| 2016 |
Welbourn EM, Wilson MT, Yusof A, Metodiev MV, Cooper CE. The mechanism of formation, structure and physiological relevance of covalent hemoglobin attachment to the erythrocyte membrane. Free Radical Biology & Medicine. PMID 28007575 DOI: 10.1016/J.Freeradbiomed.2016.12.024 |
0.331 |
|
| 2016 |
Alleyne T, Ignacio DN, Sampson VB, Ashe D, Wilson M. Simulating the slow to fast switch in cytochrome c oxidase catalysis by introducing a loop flip near to the enzyme's cytochrome c (substrate) binding site. Biotechnology and Applied Biochemistry. PMID 27489224 DOI: 10.1002/Bab.1526 |
0.377 |
|
| 2016 |
Silkstone GG, Silkstone RS, Simons M, Wilson MT, Bulow L, Kallberg K, Ratanasopa K, Ronda L, Mozzarelli A, Reeder BJ, Cooper CE. Engineering tyrosine electron transfer pathways decreases oxidative toxicity in hemoglobin: implications for blood substitute design. The Biochemical Journal. PMID 27470146 DOI: 10.1042/Bcj20160243 |
0.327 |
|
| 2016 |
Karsisiotis AI, Deacon OM, Wilson MT, Macdonald C, Blumenschein TM, Moore GR, Worrall JA. Increased dynamics in the 40-57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation. Scientific Reports. 6: 30447. PMID 27461282 DOI: 10.1038/Srep30447 |
0.329 |
|
| 2016 |
Chaplin AK, Wilson MT, Hough MA, Svistunenko DA, Hemsworth GR, Walton PH, Vijgenboom E, Worrall JA. Heterogeneity in the histidine-brace copper coordination sphere in AA10 lytic polysaccharide monooxygenases. The Journal of Biological Chemistry. PMID 27129229 DOI: 10.1074/Jbc.M116.722447 |
0.303 |
|
| 2015 |
van Wilderen LJ, Silkstone G, Mason M, van Thor JJ, Wilson MT. Kinetic studies on the oxidation of semiquinone and hydroquinone forms of Arabidopsis cryptochrome by molecular oxygen. Febs Open Bio. 5: 885-892. PMID 26649273 DOI: 10.1016/J.Fob.2015.10.007 |
0.357 |
|
| 2015 |
Kassa T, Jana S, Strader MB, Meng F, Jia Y, Wilson MT, Alayash AI. Sickle cell hemoglobin in the ferryl state promotes βCys93 oxidation and mitochondrial dysfunction in epithelial lung cells (E10). The Journal of Biological Chemistry. PMID 26396189 DOI: 10.1074/Jbc.M115.651257 |
0.325 |
|
| 2015 |
Ascenzi P, Coletta M, Wilson MT, Fiorucci L, Marino M, Polticelli F, Sinibaldi F, Santucci R. Cardiolipin-cytochrome c complex: Switching cytochrome c from an electron-transfer shuttle to a myoglobin- and a peroxidase-like heme-protein. Iubmb Life. 67: 98-109. PMID 25857294 DOI: 10.1002/Iub.1350 |
0.36 |
|
| 2015 |
Manole A, Kekilli D, Svistunenko DA, Wilson MT, Dobbin PS, Hough MA. Conformational control of the binding of diatomic gases to cytochrome c'. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 20: 675-86. PMID 25792378 DOI: 10.1007/S00775-015-1253-7 |
0.313 |
|
| 2015 |
Silaghi-Dumitrescu R, Scurtu F, Mason MG, Svistunenko DA, Wilson MT, Cooper CE. The reaction of oxyhemoglobin with nitric oxide: EPR evidence for an iron(III)-nitrate intermediate Inorganica Chimica Acta. 436: 179-183. DOI: 10.1016/J.Ica.2015.07.037 |
0.303 |
|
| 2014 |
Hough MA, Silkstone G, Worrall JA, Wilson MT. NO binding to the proapoptotic cytochrome c-cardiolipin complex. Vitamins and Hormones. 96: 193-209. PMID 25189388 DOI: 10.1016/B978-0-12-800254-4.00008-8 |
0.366 |
|
| 2014 |
Lobato L, Bouzhir-Sima L, Yamashita T, Wilson MT, Vos MH, Liebl U. Dynamics of the heme-binding bacterial gas-sensing dissimilative nitrate respiration regulator (DNR) and activation barriers for ligand binding and escape. The Journal of Biological Chemistry. 289: 26514-24. PMID 25037216 DOI: 10.1074/Jbc.M114.571398 |
0.302 |
|
| 2014 |
Ashe D, Alleyne T, Wilson M, Svistunenko D, Nicholls P. Redox equilibration after one-electron reduction of cytochrome c oxidase: radical formation and a possible hydrogen relay mechanism. Archives of Biochemistry and Biophysics. 554: 36-43. PMID 24811894 DOI: 10.1016/J.Abb.2014.04.015 |
0.359 |
|
| 2014 |
Soman J, Strader M, Hicks W, Kassa T, Singleton E, Olson J, Weiss M, Mollan T, Wilson M, Alayash A. Crystallographic evidence for oxidative Met→Asp conversion in human hemoglobin Acta Crystallographica Section a Foundations and Advances. 70: C310-C310. DOI: 10.1107/S2053273314096892 |
0.312 |
|
| 2013 |
Rong Z, Alayash AI, Wilson MT, Cooper CE. Modulating hemoglobin nitrite reductase activity through allostery: a mathematical model. Nitric Oxide : Biology and Chemistry / Official Journal of the Nitric Oxide Society. 35: 193-8. PMID 24177061 DOI: 10.1016/J.Niox.2013.10.007 |
0.321 |
|
| 2013 |
Rajagopal BS, Edzuma AN, Hough MA, Blundell KLIM, Kagan VE, Kapralov AA, Fraser LA, Butt JN, Silkstone GG, Wilson MT, Svistunenko DA, Worrall JAR. The hydrogen-peroxide-induced radical behaviour in human cytochrome c-phospholipid complexes: Implications for the enhanced pro-apoptotic activity of the G41S mutant Biochemical Journal. 456: 441-452. PMID 24099549 DOI: 10.1042/Bj20130758 |
0.364 |
|
| 2013 |
Nicholls P, Marshall DC, Cooper CE, Wilson MT. Sulfide inhibition of and metabolism by cytochrome c oxidase. Biochemical Society Transactions. 41: 1312-6. PMID 24059525 DOI: 10.1042/Bst20130070 |
0.378 |
|
| 2013 |
Rong Z, Wilson MT, Cooper CE. A model for the nitric oxide producing nitrite reductase activity of hemoglobin as a function of oxygen saturation. Nitric Oxide : Biology and Chemistry / Official Journal of the Nitric Oxide Society. 33: 74-80. PMID 23831540 DOI: 10.1016/J.Niox.2013.06.008 |
0.321 |
|
| 2013 |
Ascenzi P, Marino M, Polticelli F, Coletta M, Gioia M, Marini S, Pesce A, Nardini M, Bolognesi M, Reeder BJ, Wilson MT. Non-covalent and covalent modifications modulate the reactivity of monomeric mammalian globins. Biochimica Et Biophysica Acta. 1834: 1750-6. PMID 23416443 DOI: 10.1016/J.Bbapap.2013.02.012 |
0.33 |
|
| 2013 |
Blundell KL, Wilson MT, Svistunenko DA, Vijgenboom E, Worrall JA. Morphological development and cytochrome c oxidase activity in Streptomyces lividans are dependent on the action of a copper bound Sco protein. Open Biology. 3: 120163. PMID 23345541 DOI: 10.1098/Rsob.120163 |
0.307 |
|
| 2013 |
Cooper CE, Schaer DJ, Buehler PW, Wilson MT, Reeder BJ, Silkstone G, Svistunenko DA, Bulow L, Alayash AI. Haptoglobin binding stabilizes hemoglobin ferryl iron and the globin radical on tyrosine β145. Antioxidants & Redox Signaling. 18: 2264-73. PMID 22702311 DOI: 10.1089/Ars.2012.4547 |
0.353 |
|
| 2012 |
Silkstone G, Kapetanaki SM, Husu I, Vos MH, Wilson MT. Nitric oxide binding to the cardiolipin complex of ferric cytochrome C. Biochemistry. 51: 6760-6. PMID 22803508 DOI: 10.1021/Bi300582U |
0.383 |
|
| 2012 |
Reeder BJ, Svistunenko DA, Cooper CE, Wilson MT. Engineering tyrosine-based electron flow pathways in proteins: the case of aplysia myoglobin. Journal of the American Chemical Society. 134: 7741-9. PMID 22515641 DOI: 10.1021/Ja211745G |
0.332 |
|
| 2012 |
Rajagopal BS, Silkstone GG, Nicholls P, Wilson MT, Worrall JA. An investigation into a cardiolipin acyl chain insertion site in cytochrome c. Biochimica Et Biophysica Acta. 1817: 780-91. PMID 22365930 DOI: 10.1016/J.Bbabio.2012.02.010 |
0.363 |
|
| 2012 |
Rong Z, Wilson M, Cooper C. A model of the NO producing nitrite reductase activity of hemoglobin Nitric Oxide. 27. DOI: 10.1016/J.Niox.2012.04.087 |
0.309 |
|
| 2012 |
Marshall DCA, Nicholls P, Wilson MT, Cooper CE. A comparison of nitric oxide and hydrogen sulphide interactions with mitochondrial cytochrome c oxidase Nitric Oxide. 27. DOI: 10.1016/J.Niox.2012.04.043 |
0.329 |
|
| 2011 |
Bradley JM, Silkstone G, Wilson MT, Cheesman MR, Butt JN. Probing a complex of cytochrome c and cardiolipin by magnetic circular dichroism spectroscopy: implications for the initial events in apoptosis. Journal of the American Chemical Society. 133: 19676-9. PMID 22081937 DOI: 10.1021/Ja209144H |
0.368 |
|
| 2011 |
Rajagopal BS, Wilson MT, Bendall DS, Howe CJ, Worrall JA. 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. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 16: 577-88. PMID 21267610 DOI: 10.1007/S00775-011-0758-Y |
0.352 |
|
| 2011 |
Reeder BJ, Svistunenko DA, Wilson MT. Lipid binding to cytoglobin leads to a change in haem co-ordination: A role for cytoglobin in lipid signalling of oxidative stress Biochemical Journal. 434: 483-492. PMID 21171964 DOI: 10.1042/Bj20101136 |
0.302 |
|
| 2010 |
Silkstone G, Kapetanaki SM, Husu I, Vos MH, Wilson MT. Nitric oxide binds to the proximal heme coordination site of the ferrocytochrome c/cardiolipin complex: formation mechanism and dynamics. The Journal of Biological Chemistry. 285: 19785-92. PMID 20395293 DOI: 10.1074/Jbc.M109.067736 |
0.38 |
|
| 2010 |
Cooper CE, Holladay R, Nicholls P, Svistunenko DA, Mason MG, Silkstone G, Wilson MT. Nitric Oxide Interactions With Mitochondrial Cytochrome C And Cytochrome Oxidase Free Radical Biology and Medicine. 49. DOI: 10.1016/J.Freeradbiomed.2010.10.682 |
0.311 |
|
| 2010 |
Husu I, Kapetanaki S, Silkstone G, Liebl U, Wilson MT, Vos M. Interaction of CO/NO with the Apoptosis-Inducing Cytochrome C -Cardiolipin Complex Biophysical Journal. 98: 631a. DOI: 10.1016/J.Bpj.2009.12.3455 |
0.367 |
|
| 2009 |
Godoy LC, Muñoz-Pinedo C, Castro L, Cardaci S, Schonhoff CM, King M, Tórtora V, Marín M, Miao Q, Jiang JF, Kapralov A, Jemmerson R, Silkstone GG, Patel JN, Evans JE, ... Wilson MT, et al. Disruption of the M80-Fe ligation stimulates the translocation of cytochrome c to the cytoplasm and nucleus in nonapoptotic cells. Proceedings of the National Academy of Sciences of the United States of America. 106: 2653-8. PMID 19196960 DOI: 10.1073/Pnas.0809279106 |
0.332 |
|
| 2009 |
Kapetanaki SM, Silkstone G, Husu I, Liebl U, Wilson MT, Vos MH. Interaction of carbon monoxide with the apoptosis-inducing cytochrome c-cardiolipin complex. Biochemistry. 48: 1613-9. PMID 19183042 DOI: 10.1021/Bi801817V |
0.359 |
|
| 2008 |
Reeder BJ, Grey M, Silaghi-Dumitrescu RL, Svistunenko DA, Bülow L, Cooper CE, Wilson MT. Tyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes. The Journal of Biological Chemistry. 283: 30780-7. PMID 18728007 DOI: 10.1074/Jbc.M804709200 |
0.327 |
|
| 2008 |
Reeder BJ, Cutruzzola F, Bigotti MG, Hider RC, Wilson MT. Tyrosine as a redox-active center in electron transfer to ferryl heme in globins. Free Radical Biology & Medicine. 44: 274-83. PMID 18215736 DOI: 10.1016/J.Freeradbiomed.2007.06.030 |
0.323 |
|
| 2008 |
Wilson MT, Reeder BJ. Oxygen-binding haem proteins Experimental Physiology. 93: 128-132. PMID 17981931 DOI: 10.1113/Expphysiol.2007.039735 |
0.306 |
|
| 2008 |
Cooper C, Silkstone G, Mason M, Nicholls P, Wilson M. S10/1 Interactions of nitric oxide with cytochrome c and cytochrome c oxidase Biochimica Et Biophysica Acta. 1777. DOI: 10.1016/J.Bbabio.2008.05.227 |
0.336 |
|
| 2007 |
Svistunenko DA, Reeder BJ, Wankasi MM, Silaghi-Dumitrescu RL, Cooper CE, Rinaldo S, Cutruzzolà F, Wilson MT. Reaction of Aplysia limacina metmyoglobin with hydrogen peroxide. Dalton Transactions (Cambridge, England : 2003). 840-50. PMID 17297511 DOI: 10.1039/B615770J |
0.338 |
|
| 2007 |
Silaghi-Dumitrescu R, Reeder BJ, Nicholls P, Cooper CE, Wilson MT. Ferryl haem protonation gates peroxidatic reactivity in globins. The Biochemical Journal. 403: 391-5. PMID 17214588 DOI: 10.1042/Bj20061421 |
0.306 |
|
| 2007 |
Silkstone G, Jasaitis A, Wilson MT, Vos MH. Ligand dynamics in an electron transfer protein: Picosecond geminate recombination of carbon monoxide to heme in mutant forms of cytochrome C Journal of Biological Chemistry. 282: 1638-1649. PMID 17114183 DOI: 10.1074/Jbc.M605760200 |
0.351 |
|
| 2006 |
Dunne J, Caron A, Menu P, Alayash AI, Buehler PW, Wilson MT, Silaghi-Dumitrescu R, Faivre B, Cooper CE. Ascorbate removes key precursors to oxidative damage by cell-free haemoglobin in vitro and in vivo. The Biochemical Journal. 399: 513-24. PMID 16848758 DOI: 10.1042/Bj20060341 |
0.336 |
|
| 2006 |
Mason MG, Nicholls P, Wilson MT, Cooper CE. Nitric oxide inhibition of respiration involves both competitive (heme) and noncompetitive (copper) binding to cytochrome c oxidase. Proceedings of the National Academy of Sciences of the United States of America. 103: 708-13. PMID 16407136 DOI: 10.1073/Pnas.0506562103 |
0.356 |
|
| 2005 |
Reeder BJ, Wilson MT. Hemoglobin and myoglobin associated oxidative stress: From molecular mechanisms to disease states Current Medicinal Chemistry. 12: 2741-2751. PMID 16305469 DOI: 10.2174/092986705774463021 |
0.343 |
|
| 2005 |
Silkstone G, Jasaitis A, Vos MH, Wilson MT. Geminate carbon monoxide rebinding to a c-type haem Dalton Transactions. 3489-3494. PMID 16234930 DOI: 10.1039/B508183C |
0.349 |
|
| 2005 |
Cooper CE, Jurd M, Nicholls P, Wankasi MM, Svistunenko DA, Reeder BJ, Wilson MT. On the formation, nature, stability and biological relevance of the primary reaction intermediates of myoglobins with hydrogen peroxide. Dalton Transactions (Cambridge, England : 2003). 3483-8. PMID 16234929 DOI: 10.1039/B505786H |
0.35 |
|
| 2005 |
Vollaard NBJ, Reeder BJ, Shearman JP, Menu P, Wilson MT, Cooper CE. A new sensitive assay reveals that hemoglobin is oxidatively modified in vivo Free Radical Biology and Medicine. 39: 1216-1228. PMID 16214037 DOI: 10.1016/J.Freeradbiomed.2005.06.012 |
0.332 |
|
| 2005 |
Reeder BJ, Wilson MT. Desferrioxamine inhibits production of cytotoxic heme to protein cross-linked myoglobin: A mechanism to protect against oxidative stress without iron chelation Chemical Research in Toxicology. 18: 1004-1011. PMID 15962935 DOI: 10.1021/Tx049660Y |
0.318 |
|
| 2005 |
Silkstone GG, Cooper CE, Svistunenko D, Wilson MT. EPR and optical spectroscopic studies of Met80X mutants of yeast ferricytochrome c. models for intermediates in the alkaline transition Journal of the American Chemical Society. 127: 92-99. PMID 15631458 DOI: 10.1021/Ja045719B |
0.316 |
|
| 2005 |
Storr T, Cameron BR, Gossage RA, Yee H, Skerlj RT, Darkes MC, Fricker SP, Bridger GJ, Davies NA, Wilson MT, Maresca KP, Zubieta J. RuIII complexes of edta and dtpa polyaminocarboxylate analogues and their use as nitric oxide scavengers European Journal of Inorganic Chemistry. 2685-2697. DOI: 10.1002/Ejic.200500018 |
0.302 |
|
| 2004 |
Reeder BJ, Svistunenko DA, Cooper CE, Wilson MT. The radical and redox chemistry of myoglobin and hemoglobin: From in vitro studies to human pathology Antioxidants and Redox Signaling. 6: 954-966. PMID 15548893 DOI: 10.1089/Ars.2004.6.954 |
0.328 |
|
| 2004 |
Svistunenko DA, Wilson MT, Cooper CE. Tryptophan or tyrosine? On the nature of the amino acid radical formed following hydrogen peroxide treatment of cytochrome c oxidase Biochimica Et Biophysica Acta - Bioenergetics. 1655: 372-380. PMID 15100053 DOI: 10.1016/J.Bbabio.2003.06.006 |
0.32 |
|
| 2004 |
Wilson MT, Torres J. Reactions of Nitric Oxide with Copper Containing Oxidases; Cytochrome c Oxidase and Laccase Iubmb Life. 56: 7-11. PMID 14992374 DOI: 10.1080/152165430310001647293 |
0.349 |
|
| 2003 |
Mason MG, Nicholls P, Divne C, Hallberg BM, Henriksson G, Wilson MT. The heme domain of cellobiose oxidoreductase: a one-electron reducing system. Biochimica Et Biophysica Acta. 1604: 47-54. PMID 12686420 DOI: 10.1016/S0005-2728(03)00023-9 |
0.325 |
|
| 2002 |
Svistunenko DA, Dunne J, Fryer M, Nicholls P, Reeder BJ, Wilson MT, Bigotti MG, Cutruzzolà F, Cooper CE. Comparative study of tyrosine radicals in hemoglobin and myoglobins treated with hydrogen peroxide. Biophysical Journal. 83: 2845-55. PMID 12414716 DOI: 10.1016/S0006-3495(02)75293-4 |
0.301 |
|
| 2002 |
Silkstone G, Stanway G, Brzezinski P, Wilson MT. Production and characterisation of Met80X mutants of yeast iso-1-cytochrome c: spectral, photochemical and binding studies on the ferrous derivatives. Biophysical Chemistry. 98: 65-77. PMID 12128190 DOI: 10.1016/S0301-4622(02)00085-6 |
0.349 |
|
| 2002 |
Mason MG, Wilson MT, Ball A, Nicholls P. Oxygen reduction by cellobiose oxidoreductase: The role of the haem group Febs Letters. 518: 29-32. PMID 11997012 DOI: 10.1016/S0014-5793(02)02633-9 |
0.342 |
|
| 2002 |
Torres J, Svistunenko D, Karlsson B, Cooper CE, Wilson MT. Fast reduction of a copper center in laccase by nitric oxide and formation of a peroxide intermediate. Journal of the American Chemical Society. 124: 963-7. PMID 11829603 DOI: 10.1021/Ja016107J |
0.349 |
|
| 2002 |
Reeder BJ, Svistunenko DA, Sharpe MA, Wilson MT. Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin. Biochemistry. 41: 367-75. PMID 11772036 DOI: 10.1021/Bi011335B |
0.316 |
|
| 2001 |
Mason MG, Ball AS, Reeder BJ, Silkstone G, Nicholls P, Wilson MT. Extracellular Heme Peroxidases in Actinomycetes: a Case of Mistaken Identity Applied and Environmental Microbiology. 67: 4512-4519. PMID 11571150 DOI: 10.1128/Aem.67.10.4512-4519.2001 |
0.329 |
|
| 2001 |
Bellelli A, Brunori M, Brzezinski P, Wilson MT. Photochemically induced electron transfer. Methods (San Diego, Calif.). 24: 139-52. PMID 11384189 DOI: 10.1006/Meth.2001.1175 |
0.318 |
|
| 2001 |
Reeder BJ, Wilson MT. The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: A role for the protonated ferryl species Free Radical Biology and Medicine. 30: 1311-1318. PMID 11368929 DOI: 10.1016/S0891-5849(01)00534-2 |
0.313 |
|
| 2001 |
Pezeshk A, Torres J, Wilson MT, Symons MC. The EPR spectrum for CuB in cytochrome c oxidase. Journal of Inorganic Biochemistry. 83: 115-9. PMID 11237250 DOI: 10.1016/S0162-0134(00)00189-6 |
0.326 |
|
| 2000 |
Torres J, Sharpe MA, Rosquist A, Cooper CE, Wilson MT. Cytochrome c oxidase rapidly metabolises nitric oxide to nitrite. Febs Letters. 475: 263-6. PMID 10869568 DOI: 10.1016/S0014-5793(00)01682-3 |
0.333 |
|
| 1999 |
Torres J, Wilson MT. The reactions of copper proteins with nitric oxide Biochimica Et Biophysica Acta - Bioenergetics. 1411: 310-322. PMID 10320665 DOI: 10.1016/S0005-2728(99)00022-5 |
0.359 |
|
| 1999 |
Nicholls P, Pelekou P, Silkstone G, Wilson MT. Carboxymethyl cytochrome c as artificial heme enzyme Biochemical Society Transactions. 27. DOI: 10.1042/Bst027A127B |
0.336 |
|
| 1998 |
Nicholls P, Sharpe M, Torres J, Wilson MT, Cooper CE. Nitric oxide as an effector and a substrate for cytochrome c oxidase. Biochemical Society Transactions. 26. PMID 10047837 DOI: 10.1042/Bst026S323 |
0.342 |
|
| 1998 |
Karpefors M, Wilson MT, Brzezinski P. Photoinduced electron transfer from carboxymethylated cytochrome c to plastocyanin Biochimica Et Biophysica Acta - Bioenergetics. 1364: 385-389. PMID 9630728 DOI: 10.1016/S0005-2728(98)00063-2 |
0.353 |
|
| 1998 |
Torres J, Cooper CE, Sharpe M, Wilson MT. Reactivity of nitric oxide with cytochrome c oxidase: Interactions with the binuclear centre and mechanism of inhibition Journal of Bioenergetics and Biomembranes. 30: 63-69. PMID 9623807 DOI: 10.1023/A:1020559528124 |
0.366 |
|
| 1998 |
Torres J, Cooper CE, Wilson MT. A common mechanism for the interaction of nitric oxide with the oxidized binuclear centre and oxygen intermediates of cytochrome c oxidase Journal of Biological Chemistry. 273: 8756-8766. PMID 9535853 DOI: 10.1074/Jbc.273.15.8756 |
0.317 |
|
| 1997 |
Torres J, Wilson MT. Formation of the 'F' intermediate of cytochrome C oxidase using nitric oxide Biochemical Society Transactions. 25. PMID 9388632 DOI: 10.1042/Bst025402S |
0.308 |
|
| 1997 |
Cooper CE, Torres J, Sharpe MA, Wilson MT. Nitric oxide ejects electrons from the binuclear centre of cytochrome c oxidase by reacting with oxidised copper: a general mechanism for the interaction of copper proteins with nitric oxide? Febs Letters. 414: 281-4. PMID 9315702 DOI: 10.1016/S0014-5793(97)01009-0 |
0.326 |
|
| 1997 |
Brzezinski P, Wilson MT. Photochemical electron injection into redox-active proteins Proceedings of the National Academy of Sciences of the United States of America. 94: 6176-6179. PMID 9177190 DOI: 10.1073/Pnas.94.12.6176 |
0.358 |
|
| 1997 |
Torres J, Davies N, Darley-Usmar VM, Wilson MT. The inhibition of cytochrome c oxidase by nitric oxide using S-nitrosoglutathione Journal of Inorganic Biochemistry. 66: 207-212. PMID 9130394 DOI: 10.1016/S0162-0134(96)00206-1 |
0.545 |
|
| 1997 |
Patel RP, Svistunenko D, Wilson MT, Darley-Usmar VM. Reduction of Cu(II) by lipid hydroperoxides: Implications for the copper-dependent oxidation of low-density lipoprotein Biochemical Journal. 322: 425-433. PMID 9065759 DOI: 10.1042/Bj3220425 |
0.465 |
|
| 1996 |
Patel RP, Svistunenko DA, Darley-Usmar VM, Symons MCR, Wilson MT. Redox cycling of human methaemoglobin by H2O2 yields persistent ferryl iron and protein based radicals Free Radical Research. 25: 117-123. PMID 8885329 DOI: 10.3109/10715769609149916 |
0.503 |
|
| 1996 |
Torres J, Cooper CC, Wilson MT. Possible interaction of nitric oxide with the ferryl intermediate of cytochrome c oxidase Biochemical Society Transactions. 24. PMID 8878994 DOI: 10.1042/Bst024450S |
0.33 |
|
| 1996 |
Torres J, Wilson MT. Interaction of cytochrome-c oxidase with nitric oxide Methods in Enzymology. 269: 3-11. PMID 8791632 DOI: 10.1016/S0076-6879(96)69004-1 |
0.395 |
|
| 1996 |
Svistunenko DA, Patel RP, Wilson MT. An EPR investigation of human methaemoglobin oxidation by hydrogen peroxide: Methods to quantify all paramagnetic species observed in the reaction Free Radical Research. 24: 269-280. PMID 8731011 DOI: 10.3109/10715769609088024 |
0.314 |
|
| 1996 |
Jones GD, Russell L, Darley-Usmar VM, Stone D, Wilson MT. Role of lipid hydroperoxides in the activation of 15-lipoxygenase. Biochemistry. 35: 7197-203. PMID 8679548 DOI: 10.1021/Bi952425H |
0.5 |
|
| 1996 |
Blenkinsop C, Aitken AE, Wilson MT. Physical and functional characterisation of monomeric and dimeric eukaryotic cytochrome c oxidases Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology. 115: 421-428. DOI: 10.1016/S0305-0491(96)00160-5 |
0.358 |
|
| 1995 |
Brzezinski P, Sundahl M, Adelroth P, Wilson MT, el-Agez B, Wittung P, Malmström BG. Triplet-state quenching in complexes between Zn-cytochrome c and cytochrome oxidase or its CuA domain. Biophysical Chemistry. 54: 191-7. PMID 7756569 DOI: 10.1016/0301-4622(94)00128-7 |
0.347 |
|
| 1994 |
Sarti P, Hogg N, Darley-Usmar VM, Sanna MT, Wilson MT. The oxidation of cytochrome-c oxidase vesicles by hemoglobin Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1208: 38-44. PMID 8086437 DOI: 10.1016/0167-4838(94)90157-0 |
0.528 |
|
| 1993 |
Hogg N, Darley-Usmar VM, Wilson MT, Moncada S. The oxidation of α-tocopherol in human low-density lipoprotein by the simultaneous generation of superoxide and nitric oxide Febs Letters. 326: 199-203. PMID 8391994 DOI: 10.1016/0014-5793(93)81790-7 |
0.483 |
|
| 1991 |
Wilson MT, Bickar D. Cytochrome oxidase as a proton pump Journal of Bioenergetics and Biomembranes. 23: 755-771. PMID 1660873 DOI: 10.1007/Bf00786000 |
0.321 |
|
| 1990 |
Al-Jaff G, Silver J, Wilson MT. Studies on the binding of nitrogenous bases to protoporphyrin IX iron(II) in aqueous solution at high pH values. Part I. Pyridine and imidazole ligands Inorganica Chimica Acta. 176: 307-316. DOI: 10.1016/S0020-1693(00)84861-6 |
0.302 |
|
| 1990 |
Hogg N, Wilson M, Darley-Usmar V. Low levels of lipid peroxide increase the permeability of membranes to protons Free Radical Biology and Medicine. 9: 125. DOI: 10.1016/0891-5849(90)90623-Q |
0.361 |
|
| 1989 |
Wilson MT, Alleyne T, Clague M, Conroy K, El-Agez B. Electron transfer and conformation states in bovine cytochrome c oxidase Annals of the New York Academy of Sciences. 550: 167-176. PMID 2854389 DOI: 10.1111/J.1749-6632.1988.Tb35333.X |
0.347 |
|
| 1988 |
Saleem MMM, Wilson MT. Ligand binding to cytochrome c and other related haem proteins and peptides. Part III. Temperature dependence studies Inorganica Chimica Acta. 153: 105-113. DOI: 10.1016/S0020-1693(00)83867-0 |
0.311 |
|
| 1988 |
Saleem MMM, Wilson MT. Ligand binding to cytochrome c and other related haem proteins and peptides. Part I. Equilibrium studies Inorganica Chimica Acta. 153: 93-98. DOI: 10.1016/S0020-1693(00)83865-7 |
0.304 |
|
| 1987 |
Brunori M, Antonini G, Malatesta F, Sarti P, Wilson MT. Cytochrome-c oxidase. Subunit structure and proton pumping. Febs Journal. 169: 1-8. PMID 2445564 DOI: 10.1111/J.1432-1033.1987.Tb13572.X |
0.325 |
|
| 1987 |
Paddon ID, Wilson MT. Multiple electron-transfer sites in cytochrome c oxidase? Biochemical Society Transactions. 15: 526-527. DOI: 10.1042/Bst0150526 |
0.315 |
|
| 1987 |
Alleyne TA, Wilson MT. Conformational changes in cytochrome c oxidase Biochemical Society Transactions. 15: 524-525. DOI: 10.1042/Bst0150524 |
0.309 |
|
| 1987 |
Peterson J, Wilson MT. The reduction of haem peptides by dithionite. A kinetic investigation Inorganica Chimica Acta. 135: 101-107. DOI: 10.1016/S0020-1693(00)83271-5 |
0.35 |
|
| 1987 |
Saleem MMM, Wilson MT. Kinetic studies on the reduction of cytochrome c: reaction with organic oxy-compounds Inorganica Chimica Acta. 137: 139-143. DOI: 10.1016/S0020-1693(00)81156-1 |
0.335 |
|
| 1985 |
Sarti P, Jones MG, Antonini G, Malatesta F, Colosimo A, Wilson MT, Brunori M. Kinetics of redox-linked proton pumping activity of native and subunit III-depleted cytochrome c oxidase: a stopped-flow investigation. Proceedings of the National Academy of Sciences of the United States of America. 82: 4876-4880. PMID 2410909 DOI: 10.1073/Pnas.82.15.4876 |
0.382 |
|
| 1984 |
Jones GD, Wilson MT. Labeling of the Electron Entry Site of Cytochrome c Oxidase Using 51Cr2+ Journal of Inorganic Biochemistry. 21: 159-168. PMID 6330296 DOI: 10.1016/0162-0134(84)85048-5 |
0.332 |
|
| 1984 |
Jones GD, Wilson MT. A Comparison of the Reactions of Cytochrome c Oxidase, Cytochrome c and Azurin with Cr2+ Ions Journal of Inorganic Biochemistry. 21: 147-158. PMID 6330295 DOI: 10.1016/0162-0134(84)85047-3 |
0.354 |
|
| 1984 |
Bickar D, Bonaventura J, Bonaventura C, Auer H, Wilson M. Paradoxical effects of methylmercury on the kinetics of cytochrome c oxidase. Biochemistry. 23: 680-4. PMID 6324852 DOI: 10.1021/Bi00299A015 |
0.34 |
|
| 1984 |
Jensen P, Wilson MT, Aasa R, Malmström BG. Cyanide inhibition of cytochrome c oxidase. A rapid-freeze e.p.r. investigation. The Biochemical Journal. 224: 829-37. PMID 6098268 DOI: 10.1042/Bj2240829 |
0.318 |
|
| 1983 |
Brunori M, Silvestrini MC, Wilson MT, Weiss H. Transient kinetic studies of Neurospora crassa cytochrome c oxidase Biochemical Journal. 215: 425-427. PMID 6316928 DOI: 10.1042/Bj2150425 |
0.352 |
|
| 1983 |
Al-Tai WF, Jones MG, Rashid K, Wilson MT. An active cytochrome c oxidase that has no tightly bound cardiolipin Biochemical Journal. 209: 901-903. PMID 6307267 DOI: 10.1042/Bj2090901 |
0.328 |
|
| 1983 |
Brunori M, Colosimo A, Wilson MT, Sarti P, Antonini E. Interconversion between states in cytochrome oxidase: Interpretation of kinetic data on mixed-valence oxidase Febs Letters. 152: 75-78. PMID 6301877 DOI: 10.1016/0014-5793(83)80485-2 |
0.335 |
|
| 1983 |
Dahlin S, Reinhammar B, Wilson MT. The electron self-exchange rate constant for stellacyanin Inorganica Chimica Acta. 79: 126. DOI: 10.1016/S0020-1693(00)95158-2 |
0.309 |
|
| 1983 |
Wilson MT. Cytochrome c oxidase: A short review Inorganica Chimica Acta. 79: 71-72. DOI: 10.1016/S0020-1693(00)95100-4 |
0.373 |
|
| 1983 |
Hamed MY, Silver J, Wilson MT. Studies on the reactions of ferric iron with glutathione and some related thiols. Part III. A study of the iron catalyzed oxidation of glutathione by molecular oxygen Inorganica Chimica Acta. 80: 237-244. DOI: 10.1016/S0020-1693(00)91289-1 |
0.309 |
|
| 1982 |
Brunori M, Colosimo A, Wilson MT. Kinetic studies of cytochrome-c-oxidase: significance of different functional states of the enzyme Advances in Experimental Medicine and Biology. 148: 111-121. PMID 6289638 DOI: 10.1007/978-1-4615-9281-5_10 |
0.34 |
|
| 1982 |
Wilson MT, Jensen P, Aasa R, Malmström BG, Vänngård T. An investigation by e.p.r. and optical spectroscopy of cytochrome oxidase during turnover. The Biochemical Journal. 203: 483-92. PMID 6288002 DOI: 10.1042/Bj2030483 |
0.314 |
|
| 1982 |
Lukas B, Miller JR, Silver J, Wilson MT, Morrison IEG. Studies on copper–protoporphyrin–iron(III) complexes. A possible model for cytochrome c oxidase Journal of the Chemical Society-Dalton Transactions. 1035-1040. DOI: 10.1039/Dt9820001035 |
0.334 |
|
| 1982 |
Lukas B, Miller JR, Silver J, Wilson MT, Morrison IEG. Studies On Copper-Protoporphyrin-Iron(Iii) Complexes. A Possible Model For Cytochrome C Oxidase Cheminform. 13. DOI: 10.1002/Chin.198236264 |
0.318 |
|
| 1981 |
Darley-Usmar VM, Capaldi RA, Wilson MT. Identification of cysteines in subunit II as ligands to the redox centers of bovine cytochrome c oxidase Biochemical and Biophysical Research Communications. 103: 1223-1230. PMID 6277330 DOI: 10.1016/0006-291X(81)90253-9 |
0.64 |
|
| 1981 |
Wilson MT, Peterson J, Antonini E, Brunori M, Colosimo A, Wyman J. A plausible two-state model for cytochrome c oxidase. Proceedings of the National Academy of Sciences of the United States of America. 78: 7115-8. PMID 6273912 DOI: 10.1073/Pnas.78.11.7115 |
0.36 |
|
| 1981 |
Kimura K, Peterson J, Wilson M, Cookson DJ, Williams RJ. A study of the electron transfer properties of the heme undecapeptide from cytochrome c by 1H nmr spectroscopy. Journal of Inorganic Biochemistry. 15: 11-25. PMID 6268745 DOI: 10.1016/S0162-0134(00)80132-4 |
0.344 |
|
| 1981 |
Darley-Usmar VM, Wilson MT. On the identification and nomenclature of the polypeptide subunits of bovine cytochrome C oxidase Biochemical and Biophysical Research Communications. 99: 51-57. PMID 6263278 DOI: 10.1016/0006-291X(81)91711-3 |
0.506 |
|
| 1981 |
Silvestrini MC, Brunori M, Wilson MT, Darley-Usmar VM. The electron transfer system of Pseudomonas aeruginosa: a study of the pH-dependent transitions between redox forms of azurin and cytochrome c551 Journal of Inorganic Biochemistry. 14: 327-338. DOI: 10.1016/S0162-0134(00)80289-5 |
0.528 |
|
| 1981 |
Clore GM, Hollaway MR, Orengo C, Peterson J, Wilson MT. The Kinetics of the Reactions of Low Spin Ferric Haem Undecapeptide with Hydrogen Peroxide Inorganica Chimica Acta. 56: 143-148. DOI: 10.1016/S0020-1693(00)88559-X |
0.327 |
|
| 1981 |
Darley-Usmar VM, Alizai N, Al-Ayash AI, Jones GD, Sharpe A, Wilson MT. A comparison of the structural and functional properties of cytochrome c oxidase isolated from beef (Bos tauros), camel (Camelus dromedarius), chicken (Gallus domesticus) and rat (Rattus norvegicus) Comparative Biochemistry and Physiology -- Part B: Biochemistry And. 68: 445-456. DOI: 10.1016/0305-0491(81)90154-1 |
0.545 |
|
| 1981 |
Colosimo A, Brunori M, Sarti P, Antonini E, Wilson MT. “Pulsed” Cytochrome c Oxidase: A Critical Appraisal of Properties and Catalytic Relevance Israel Journal of Chemistry. 21: 30-33. DOI: 10.1002/Ijch.198100008 |
0.329 |
|
| 1979 |
Wilson MT, Silvestrini MC, Morpurgo L, Brunori M. Electron transfer kinetics between rhus vernicifera stellacyanin and cytochrome c (horse heart cytochrome c and pseudomonas cytochrome c551) Journal of Inorganic Biochemistry. 11: 95-100. PMID 228006 DOI: 10.1016/S0162-0134(00)80175-0 |
0.345 |
|
| 1979 |
Wilson MT, Bonaventura J, Brunori M. Mitochondrial cytochrome content and cytochrome oxidase activity of some Amazonian fish Comparative Biochemistry and Physiology -- Part a: Physiology. 62: 245-249. DOI: 10.1016/0300-9629(79)90763-1 |
0.32 |
|
| 1977 |
Antonini E, Brunori M, Colosimo A, Greenwood C, Wilson MT. Oxygen "pulsed" cytochrome c oxidase: functional properties and catalytic relevance Proceedings of the National Academy of Sciences of the United States of America. 74: 3128-3132. PMID 198771 DOI: 10.1073/Pnas.74.8.3128 |
0.614 |
|
| 1977 |
Stotter DA, Thomas RD, Wilson MT. Reductive dechlorination of DDT by haem proteins. Bioinorganic Chemistry. 7: 87-93. PMID 192320 DOI: 10.1016/S0006-3061(00)80130-1 |
0.357 |
|
| 1977 |
Al-Ayash AI, Wilson MT. Isolation and properties of cytochrome c from the slime mould, Dictyostelium discoideum Comparative Biochemistry and Physiology -- Part B: Biochemistry And. 56: 147-152. PMID 187374 DOI: 10.1016/0305-0491(77)90040-2 |
0.326 |
|
| 1977 |
Wilson MT, Ranson RJ, Masiakowski P, Czarnecka E, Brunori M. A kinetic study of the pH-dependent properties of the ferric undecapeptide of cytochrome c (microperoxidase). European Journal of Biochemistry / Febs. 77: 193-9. PMID 20304 DOI: 10.1111/J.1432-1033.1977.Tb11657.X |
0.338 |
|
| 1974 |
Parr SR, Wilson MT, Greenwood C. The reaction of Pseudomonas aeruginosa cytochrome c oxidase with sodium metabisulphite Biochemical Journal. 139: 273-276. PMID 4377097 DOI: 10.1042/Bj1390273 |
0.573 |
|
| 1974 |
Dupre S, Brunori M, Wilson MT, Greenwood C. Kinetics of carbon monoxide binding and electron transfer by cytochrome c polymers Biochemical Journal. 141: 299-304. PMID 4375972 DOI: 10.1042/Bj1410299 |
0.604 |
|
| 1973 |
Wilson MT, Brunori M, Bonaventura J, Bonaventura C. Effect of steady illumination on the binding of carbon monoxide by carboxymethylated cytochrome c Biochemical Journal. 131: 863-865. PMID 4352917 DOI: 10.1042/Bj1310863 |
0.305 |
|
| 1973 |
Antonini E, Brunori M, Greenwood C, Wilson MT. Kinetic Studies on Mammalian Cytochrome c Oxidase Biochemical Society Transactions. 1: 34-35. DOI: 10.1042/Bst0010034 |
0.56 |
|
| 1971 |
Greenwood C, Wilson MT. Studies on ferricytochrome c. I. Effect of pH, ionic strength and protein denaturants on the spectra of ferricytochrome c European Journal of Biochemistry. 22: 5-10. PMID 5099216 DOI: 10.1111/J.1432-1033.1971.Tb01507.X |
0.575 |
|
| 1971 |
Wilson MT, Greenwood C. Studies on ferricytochrome c. 2. A correlation between reducibility and the possession of the 695mm absorption band of ferricytochrome c European Journal of Biochemistry. 22: 11-18. PMID 5099209 DOI: 10.1111/J.1432-1033.1971.Tb01508.X |
0.534 |
|
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