| Year |
Citation |
Score |
| 2020 |
Lim H, Baker ML, Cowley RE, Kim S, Bhadra M, Siegler MA, Kroll T, Sokaras D, Weng TC, Biswas DR, Dooley DM, Karlin KD, Hedman B, Hodgson KO, Solomon EI. Kβ X-ray Emission Spectroscopy as a Probe of Cu(I) Sites: Application to the Cu(I) Site in Preprocessed Galactose Oxidase. Inorganic Chemistry. PMID 33136386 DOI: 10.1021/acs.inorgchem.0c02495 |
0.306 |
|
| 2019 |
Adelson CN, Johnston EM, Hilmer KM, Watts H, Dey SG, Brown DE, Broderick JB, Shepard EM, Dooley DM, Solomon EI. Characterization of the preprocessed copper site equilibrium in amine oxidase and assignment of the reactive copper site in topaquinone biogenesis. Journal of the American Chemical Society. PMID 31060358 DOI: 10.1021/Jacs.9B01922 |
0.676 |
|
| 2016 |
Cowley RE, Cirera J, Qayyum MF, Rokhsana D, Hedman B, Hodgson KO, Dooley DM, Solomon EI. Structure of the Reduced Copper Active Site in Pre-Processed Galactose Oxidase: Ligand Tuning for One-Electron O2 Activation in Cofactor Biogenesis. Journal of the American Chemical Society. PMID 27626829 DOI: 10.1021/Jacs.6B05792 |
0.518 |
|
| 2015 |
Shepard EM, Dooley DM. Inhibition and oxygen activation in copper amine oxidases. Accounts of Chemical Research. 48: 1218-26. PMID 25897668 DOI: 10.1021/Ar500460Z |
0.735 |
|
| 2013 |
Liu Y, Mukherjee A, Nahumi N, Ozbil M, Brown D, Angeles-Boza AM, Dooley DM, Prabhakar R, Roth JP. Experimental and computational evidence of metal-O2 activation and rate-limiting proton-coupled electron transfer in a copper amine oxidase. The Journal of Physical Chemistry. B. 117: 218-29. PMID 23240607 DOI: 10.1021/Jp3121484 |
0.35 |
|
| 2012 |
Fujita K, Hirasawa-Fujita M, Brown DE, Obara Y, Ijima F, Kohzuma T, Dooley DM. Direct electron transfer from pseudoazurin to nitrous oxide reductase in catalytic N2O reduction. Journal of Inorganic Biochemistry. 115: 163-73. PMID 22910335 DOI: 10.1016/J.Jinorgbio.2012.07.013 |
0.765 |
|
| 2012 |
Rokhsana D, Howells AE, Dooley DM, Szilagyi RK. Role of the Tyr-Cys cross-link to the active site properties of galactose oxidase. Inorganic Chemistry. 51: 3513-24. PMID 22372371 DOI: 10.1021/Ic2022769 |
0.459 |
|
| 2012 |
Mills SA, Brown DE, Dang K, Sommer D, Bitsimis A, Nguyen J, Dooley DM. Cobalt substitution supports an inner-sphere electron transfer mechanism for oxygen reduction in pea seedling amine oxidase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 17: 507-15. PMID 22258083 DOI: 10.1007/S00775-011-0872-X |
0.367 |
|
| 2011 |
Rokhsana D, Shepard EM, Brown DE, Dooley DM. Amine Oxidase and Galactose Oxidase Copper-Oxygen Chemistry. 53-106. DOI: 10.1002/9781118094365.ch3 |
0.654 |
|
| 2010 |
Ran Y, Liu M, Zhu H, Nygaard TK, Brown DE, Fabian M, Dooley DM, Lei B. Spectroscopic identification of heme axial ligands in HtsA that are involved in heme acquisition by Streptococcus pyogenes. Biochemistry. 49: 2834-42. PMID 20180543 DOI: 10.1021/Bi901987H |
0.322 |
|
| 2010 |
Fitzpatrick MB, Obara Y, Fujita K, Brown DE, Dooley DM, Kohzuma T, Czernuszewicz RS. Non-covalent interactions in blue copper protein probed by Met16 mutation and electronic and resonance Raman spectroscopy of Achromobacter cycloclastes pseudoazurin. Journal of Inorganic Biochemistry. 104: 250-60. PMID 20007000 DOI: 10.1016/J.Jinorgbio.2009.11.004 |
0.417 |
|
| 2010 |
Hirasawa M, Fujita K, Dooley DM, Kohzuma T. 3P086 Electron-transfer reaction and related enzymatic studies of nitrous oxide reductase from Achromobacter cycloclastes IAM 1013.(Protein: Function,The 48th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 50: S159-S160. DOI: 10.2142/Biophys.50.S159_6 |
0.328 |
|
| 2009 |
McGrath AP, Hilmer KM, Collyer CA, Shepard EM, Elmore BO, Brown DE, Dooley DM, Guss JM. Structure and inhibition of human diamine oxidase. Biochemistry. 48: 9810-22. PMID 19764817 DOI: 10.1021/Bi9014192 |
0.817 |
|
| 2008 |
Shepard EM, Okonski KM, Dooley DM. Kinetics and spectroscopic evidence that the Cu(I)-semiquinone intermediate reduces molecular oxygen in the oxidative half-reaction of Arthrobacter globiformis amine oxidase. Biochemistry. 47: 13907-20. PMID 19053231 DOI: 10.1021/Bi8011516 |
0.701 |
|
| 2008 |
Rogers MS, Hurtado-Guerrero R, Firbank SJ, Halcrow MA, Dooley DM, Phillips SE, Knowles PF, McPherson MJ. Cross-link formation of the cysteine 228-tyrosine 272 catalytic cofactor of galactose oxidase does not require dioxygen. Biochemistry. 47: 10428-39. PMID 18771294 DOI: 10.1021/Bi8010835 |
0.467 |
|
| 2008 |
Langley DB, Trambaiolo DM, Duff AP, Dooley DM, Freeman HC, Guss JM. Complexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromine. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 64: 577-83. PMID 18607080 DOI: 10.1107/S174430910801556X |
0.429 |
|
| 2008 |
Mukherjee A, Smirnov VV, Lanci MP, Brown DE, Shepard EM, Dooley DM, Roth JP. Inner-sphere mechanism for molecular oxygen reduction catalyzed by copper amine oxidases. Journal of the American Chemical Society. 130: 9459-73. PMID 18582059 DOI: 10.1021/Ja801378F |
0.697 |
|
| 2008 |
Langley DB, Brown DE, Cheruzel LE, Contakes SM, Duff AP, Hilmer KM, Dooley DM, Gray HB, Guss JM, Freeman HC. Enantiomer-specific binding of ruthenium(II) molecular wires by the amine oxidase of Arthrobacter globiformis. Journal of the American Chemical Society. 130: 8069-78. PMID 18507382 DOI: 10.1021/Ja801289F |
0.469 |
|
| 2008 |
Rokhsana D, Dooley DM, Szilagyi RK. Systematic development of computational models for the catalytic site in galactose oxidase: impact of outer-sphere residues on the geometric and electronic structures. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 13: 371-83. PMID 18057969 DOI: 10.1007/S00775-007-0325-8 |
0.457 |
|
| 2007 |
Fujita K, Chan JM, Bollinger JA, Alvarez ML, Dooley DM. Anaerobic purification, characterization and preliminary mechanistic study of recombinant nitrous oxide reductase from Achromobacter cycloclastes. Journal of Inorganic Biochemistry. 101: 1836-44. PMID 17681606 DOI: 10.1016/J.Jinorgbio.2007.06.029 |
0.478 |
|
| 2007 |
Rogers MS, Tyler EM, Akyumani N, Kurtis CR, Spooner RK, Deacon SE, Tamber S, Firbank SJ, Mahmoud K, Knowles PF, Phillips SE, McPherson MJ, Dooley DM. The stacking tryptophan of galactose oxidase: a second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis. Biochemistry. 46: 4606-18. PMID 17385891 DOI: 10.1021/Bi062139D |
0.455 |
|
| 2007 |
Ghosh S, Gorelsky SI, George SD, Chan JM, Cabrito I, Dooley DM, Moura JJ, Moura I, Solomon EI. Spectroscopic, computational, and kinetic studies of the mu4-sulfide-bridged tetranuclear CuZ cluster in N2O reductase: pH effect on the edge ligand and its contribution to reactivity. Journal of the American Chemical Society. 129: 3955-65. PMID 17352474 DOI: 10.1021/Ja068059E |
0.423 |
|
| 2007 |
Fujita K, Dooley DM. Insights into the mechanism of N2O reduction by reductively activated N2O reductase from kinetics and spectroscopic studies of pH effects. Inorganic Chemistry. 46: 613-5. PMID 17257001 DOI: 10.1021/Ic061843F |
0.375 |
|
| 2007 |
Abdelhamid RF, Obara Y, Uchida Y, Kohzuma T, Dooley DM, Brown DE, Hori H. Pi-pi interaction between aromatic ring and copper-coordinated His81 imidazole regulates the blue copper active-site structure. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 12: 165-73. PMID 17031705 DOI: 10.1007/S00775-006-0176-8 |
0.37 |
|
| 2006 |
Rokhsana D, Dooley DM, Szilagyi RK. Structure of the oxidized active site of galactose oxidase from realistic in silico models. Journal of the American Chemical Society. 128: 15550-1. PMID 17147339 DOI: 10.1021/Ja062702F |
0.333 |
|
| 2006 |
Duff AP, Shepard EM, Langley DB, Dooley DM, Freeman HC, Guss JM. A C-terminal disulfide bond in the copper-containing amine oxidase from pea seedlings violates the twofold symmetry of the molecular dimer. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62: 1168-73. PMID 17142890 DOI: 10.1107/S1744309106043685 |
0.647 |
|
| 2006 |
Taubner LM, McGuirl MA, Dooley DM, Copié V. Structural studies of Apo NosL, an accessory protein of the nitrous oxide reductase system: insights from structural homology with MerB, a mercury resistance protein. Biochemistry. 45: 12240-52. PMID 17014077 DOI: 10.1021/bi061089+ |
0.314 |
|
| 2006 |
Duff AP, Cohen AE, Ellis PJ, Hilmer K, Langley DB, Dooley DM, Freeman HC, Guss JM. The 1.23 Angstrom structure of Pichia pastoris lysyl oxidase reveals a lysine-lysine cross-link. Acta Crystallographica. Section D, Biological Crystallography. 62: 1073-84. PMID 16929109 DOI: 10.1107/S0907444906026333 |
0.435 |
|
| 2006 |
Shepard EM, Dooley DM. Intramolecular electron transfer rate between active-site copper and TPQ in Arthrobacter globiformis amine oxidase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 1039-48. PMID 16924556 DOI: 10.1007/S00775-006-0153-2 |
0.721 |
|
| 2006 |
Juda GA, Shepard EM, Elmore BO, Dooley DM. A comparative study of the binding and inhibition of four copper-containing amine oxidases by azide: implications for the role of copper during the oxidative half-reaction. Biochemistry. 45: 8788-800. PMID 16846222 DOI: 10.1021/Bi060481K |
0.791 |
|
| 2006 |
Qiao C, Ling KQ, Shepard EM, Dooley DM, Sayre LM. Mechanism-based cofactor derivatization of a copper amine oxidase by a branched primary amine recruits the oxidase activity of the enzyme to turn inactivator into substrate. Journal of the American Chemical Society. 128: 6206-19. PMID 16669691 DOI: 10.1021/Ja058838F |
0.748 |
|
| 2005 |
Contakes SM, Juda GA, Langley DB, Halpern-Manners NW, Duff AP, Dunn AR, Gray HB, Dooley DM, Guss JM, Freeman HC. Reversible inhibition of copper amine oxidase activity by channel-blocking ruthenium(II) and rhenium(I) molecular wires. Proceedings of the National Academy of Sciences of the United States of America. 102: 13451-6. PMID 16157884 DOI: 10.1073/Pnas.0506336102 |
0.812 |
|
| 2005 |
Bollinger JA, Brown DE, Dooley DM. The Formation of lysine tyrosylquinone (LTQ) is a self-processing reaction. Expression and characterization of a Drosophila lysyl oxidase. Biochemistry. 44: 11708-14. PMID 16128571 DOI: 10.1021/Bi0504310 |
0.431 |
|
| 2005 |
Mure M, Kurtis CR, Brown DE, Rogers MS, Tambyrajah WS, Saysell C, Wilmot CM, Phillips SE, Knowles PF, Dooley DM, McPherson MJ. Active site rearrangement of the 2-hydrazinopyridine adduct in Escherichia coli amine oxidase to an azo copper(II) chelate form: a key role for tyrosine 369 in controlling the mobility of the TPQ-2HP adduct. Biochemistry. 44: 1583-94. PMID 15683242 DOI: 10.1021/Bi0479860 |
0.458 |
|
| 2005 |
Mure M, Brown DE, Saysell C, Rogers MS, Wilmot CM, Kurtis CR, McPherson MJ, Phillips SE, Knowles PF, Dooley DM. Role of the interactions between the active site base and the substrate Schiff base in amine oxidase catalysis. Evidence from structural and spectroscopic studies of the 2-hydrazinopyridine adduct of Escherichia coli amine oxidase. Biochemistry. 44: 1568-82. PMID 15683241 DOI: 10.1021/Bi047988K |
0.43 |
|
| 2005 |
Obara Y, Abdelhamid RF, Brown DE, Juda GA, Shepard EM, Dooley DM, Hori H, Kohzuma T. 1P034 Spectroscopic and Electrochemical Studies of Pseudoazurin M16X Variants Seibutsu Butsuri. 45: S40. DOI: 10.2142/Biophys.45.S40_2 |
0.739 |
|
| 2004 |
Firbank S, Rogers M, Guerrero RH, Dooley DM, Halcrow MA, Phillips SE, Knowles PF, McPherson MJ. Cofactor processing in galactose oxidase. Biochemical Society Symposium. 15-25. PMID 15777009 |
0.424 |
|
| 2004 |
Duff AP, Trambaiolo DM, Cohen AE, Ellis PJ, Juda GA, Shepard EM, Langley DB, Dooley DM, Freeman HC, Guss JM. Using xenon as a probe for dioxygen-binding sites in copper amine oxidases. Journal of Molecular Biology. 344: 599-607. PMID 15533431 DOI: 10.1016/J.Jmb.2004.09.075 |
0.797 |
|
| 2004 |
O'Connell KM, Langley DB, Shepard EM, Duff AP, Jeon HB, Sun G, Freeman HC, Guss JM, Sayre LM, Dooley DM. Differential inhibition of six copper amine oxidases by a family of 4-(aryloxy)-2-butynamines: evidence for a new mode of inactivation. Biochemistry. 43: 10965-78. PMID 15323556 DOI: 10.1021/Bi0492004 |
0.702 |
|
| 2004 |
Taubner LM, McGuirl MA, Dooley DM, Copié V. 1H, 13C, 15N backbone and sidechain resonance assignments of apo-NosL, a novel copper(I) binding protein from the nitrous oxide reductase gene cluster of Achromobacter cycloclastes. Journal of Biomolecular Nmr. 29: 211-2. PMID 15014237 DOI: 10.1023/B:Jnmr.0000019240.29152.Ac |
0.35 |
|
| 2004 |
Chan JM, Bollinger JA, Grewell CL, Dooley DM. Reductively activated nitrous oxide reductase reacts directly with substrate. Journal of the American Chemical Society. 126: 3030-1. PMID 15012115 DOI: 10.1021/ja0398868 |
0.36 |
|
| 2004 |
Shepard EM, Juda GA, Ling KQ, Sayre LM, Dooley DM. Cyanide as a copper and quinone-directed inhibitor of amine oxidases from pea seedlings ( Pisum sativum) and Arthrobacter globiformis: evidence for both copper coordination and cyanohydrin derivatization of the quinone cofactor. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 256-68. PMID 14986071 DOI: 10.1007/S00775-004-0522-7 |
0.807 |
|
| 2003 |
Duff AP, Cohen AE, Ellis PJ, Kuchar JA, Langley DB, Shepard EM, Dooley DM, Freeman HC, Guss JM. The crystal structure of Pichia pastoris lysyl oxidase. Biochemistry. 42: 15148-57. PMID 14690425 DOI: 10.1021/Bi035338V |
0.815 |
|
| 2003 |
Hess CR, Juda GA, Dooley DM, Amii RN, Hill MG, Winkler JR, Gray HB. Gold electrodes wired for coupling with the deeply buried active site of Arthrobacter globiformis amine oxidase. Journal of the American Chemical Society. 125: 7156-7. PMID 12797771 DOI: 10.1021/Ja029538Q |
0.766 |
|
| 2003 |
Firbank SJ, Rogers M, Hurtado-Guerrero R, Dooley DM, Halcrow MA, Phillips SE, Knowles PF, McPherson MJ. Cofactor processing in galactose oxidase. Biochemical Society Transactions. 31: 506-9. PMID 12773145 DOI: 10.1042/ |
0.403 |
|
| 2003 |
Rogers MS, Dooley DM. Copper-tyrosyl radical enzymes. Current Opinion in Chemical Biology. 7: 189-96. PMID 12714051 DOI: 10.1016/S1367-5931(03)00024-3 |
0.323 |
|
| 2003 |
Shepard EM, Heggem H, Juda GA, Dooley DM. Inhibition of six copper-containing amine oxidases by the antidepressant drug tranylcypromine. Biochimica Et Biophysica Acta. 1647: 252-9. PMID 12686142 DOI: 10.1016/S1570-9639(03)00062-1 |
0.807 |
|
| 2003 |
Freeman HC, Cohen A, Dooley DM, Duff AP, Ellis PJ, Guss J, Langley DB, Trambaiolo DM. New crystallographic studies of copper amine oxidases Journal of Inorganic Biochemistry. 96: 132. DOI: 10.1016/S0162-0134(03)80615-3 |
0.413 |
|
| 2002 |
Lee M, Willingham K, Langley D, Maher MJ, Cohen AE, Ellis PJ, Kuchar JA, Dooley DM, Freeman HC, Guss JM. Crystallization of Pichia pastoris lysyl oxidase. Acta Crystallographica. Section D, Biological Crystallography. 58: 2177-9. PMID 12454493 DOI: 10.1107/S0907444902016827 |
0.752 |
|
| 2002 |
Lee Y, Ling KQ, Lu X, Silverman RB, Shepard EM, Dooley DM, Sayre LM. 3-pyrrolines are mechanism-based inactivators of the quinone-dependent amine oxidases but only substrates of the flavin-dependent amine oxidases. Journal of the American Chemical Society. 124: 12135-43. PMID 12371853 DOI: 10.1021/Ja0205434 |
0.695 |
|
| 2002 |
Shepard EM, Smith J, Elmore BO, Kuchar JA, Sayre LM, Dooley DM. Towards the development of selective amine oxidase inhibitors. Mechanism-based inhibition of six copper containing amine oxidases. European Journal of Biochemistry / Febs. 269: 3645-58. PMID 12153561 DOI: 10.1046/J.1432-1033.2002.03035.X |
0.79 |
|
| 2002 |
Elmore BO, Bollinger JA, Dooley DM. Human kidney diamine oxidase: heterologous expression, purification, and characterization. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 7: 565-79. PMID 12072962 DOI: 10.1007/S00775-001-0331-1 |
0.769 |
|
| 2002 |
Green EL, Nakamura N, Dooley DM, Klinman JP, Sanders-Loehr J. Rates of oxygen and hydrogen exchange as indicators of TPQ cofactor orientation in amine oxidases. Biochemistry. 41: 687-96. PMID 11781110 DOI: 10.1021/Bi011685Y |
0.335 |
|
| 2001 |
Firbank SJ, Rogers MS, Wilmot CM, Dooley DM, Halcrow MA, Knowles PF, McPherson MJ, Phillips SE. Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme. Proceedings of the National Academy of Sciences of the United States of America. 98: 12932-7. PMID 11698678 DOI: 10.1073/Pnas.231463798 |
0.371 |
|
| 2001 |
Rogers MS, Dooley DM. Posttranslationally modified tyrosines from galactose oxidase and cytochrome C oxidase Advances in Protein Chemistry. 58: 387-436. PMID 11665492 DOI: 10.1016/S0065-3233(01)58009-2 |
0.397 |
|
| 2001 |
Juda GA, Bollinger JA, Dooley DM. Construction, overexpression, and purification of Arthrobacter globiformis amine oxidase-Strep-tag II fusion protein. Protein Expression and Purification. 22: 455-61. PMID 11483008 DOI: 10.1006/Prep.2001.1468 |
0.79 |
|
| 2001 |
Alvarez ML, Ai J, Zumft W, Sanders-Loehr J, Dooley DM. Characterization of the copper-sulfur chromophores in nitrous oxide reductase by resonance raman spectroscopy: evidence for sulfur coordination in the catalytic cluster. Journal of the American Chemical Society. 123: 576-87. PMID 11456570 DOI: 10.1021/Ja994322I |
0.443 |
|
| 2001 |
McGuirl MA, Bollinger JA, Cosper N, Scott RA, Dooley DM. Expression, purification, and characterization of NosL, a novel Cu(I) protein of the nitrous oxide reductase (nos) gene cluster. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 6: 189-95. PMID 11293413 DOI: 10.1007/S007750000190 |
0.451 |
|
| 2001 |
Kuchar JA, Dooley DM. Cloning, sequence analysis, and characterization of the 'Lysyl Oxidase' from Pichia Pastoris Journal of Inorganic Biochemistry. 83: 193-204. PMID 11237259 DOI: 10.1016/S0162-0134(00)00202-6 |
0.81 |
|
| 2001 |
Lee Y, Shepard E, Smith J, Dooley DM, Sayre LM. Catalytic turnover of substrate benzylamines by the quinone-dependent plasma amine oxidase leads to H2O2-dependent inactivation: evidence for generation of a cofactor-derived benzoxazole. Biochemistry. 40: 822-9. PMID 11170400 DOI: 10.1021/Bi002118Y |
0.703 |
|
| 2001 |
Elmore BO, Dooley DM. Visualization of dioxygen bound to copper during enzyme catalysis Chemtracts. 14: 243-251. |
0.733 |
|
| 2000 |
Rasmussen T, Berks BC, Sanders-Loehr J, Dooley DM, Zumft WG, Thomson AJ. The catalytic center in nitrous oxide reductase, CuZ, is a copper-sulfide cluster. Biochemistry. 39: 12753-6. PMID 11041839 DOI: 10.1021/Bi001811I |
0.487 |
|
| 2000 |
Allardyce C, Spooner R, Rogers M, Dooley D, Knowles P, McPherson M. Investigation of substrate binding to galactose oxidase Biochemical Society Transactions. 28: A71-A71. DOI: 10.1042/Bst028A071C |
0.356 |
|
| 2000 |
Saysell CG, Murray JM, Wilmot CM, Brown DE, Dooley DM, Phillips SEV, McPherson MJ, Knowles PF. Investigation into the mechanism of λ(max) shifts and their dependence on pH for the 2-hydrazinopyridine derivatives of two copper amine oxidases Journal of Molecular Catalysis - B Enzymatic. 8: 17-25. DOI: 10.1016/S1381-1177(99)00068-5 |
0.374 |
|
| 1999 |
Dooley DM. Structure and biogenesis of topaquinone and related cofactors Journal of Biological Inorganic Chemistry. 4: 1-11. PMID 10499097 DOI: 10.1007/s007750050283 |
0.323 |
|
| 1999 |
Edens WA, Goins TQ, Dooley D, Henson JM. Purification and characterization of a secreted laccase of Gaeumannomyces graminis var. tritici. Applied and Environmental Microbiology. 65: 3071-4. PMID 10388705 DOI: 10.1128/Aem.65.7.3071-3074.1999 |
0.351 |
|
| 1999 |
McGuirl MA, Dooley DM. Copper-containing oxidases Current Opinion in Chemical Biology. 3: 138-144. PMID 10226045 DOI: 10.1016/S1367-5931(99)80025-8 |
0.357 |
|
| 1998 |
McGuirl MA, Nelson LK, Bollinger JA, Chan YK, Dooley DM. The nos (nitrous oxide reductase) gene cluster from the soil bacterium Achromobacter cycloclastes: cloning, sequence analysis, and expression. Journal of Inorganic Biochemistry. 70: 155-69. PMID 9720302 DOI: 10.1016/S0162-0134(98)10001-6 |
0.344 |
|
| 1998 |
Dooley DM, Scott RA, Knowles PF, Colangelo CM, McGuirl MA, Brown DE. Structures of the Cu(I) and Cu(II) forms of amine oxidases from X-ray absorption spectroscopy Journal of the American Chemical Society. 120: 2599-2605. DOI: 10.1021/Ja970312A |
0.506 |
|
| 1998 |
Rogers MS, Knowles PF, Baron AJ, McPherson MJ, Dooley DM. Characterization of the active site of galactose oxidase and its active site mutational variants Y495F/H/K and W290H by circular dichroism spectroscopy Inorganica Chimica Acta. 275: 175-181. DOI: 10.1016/S0020-1693(97)06142-2 |
0.406 |
|
| 1997 |
Wilce MC, Dooley DM, Freeman HC, Guss JM, Matsunami H, McIntire WS, Ruggiero CE, Tanizawa K, Yamaguchi H. Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone. Biochemistry. 36: 16116-33. PMID 9405045 DOI: 10.1021/Bi971797I |
0.482 |
|
| 1997 |
Ruggiero CE, Smith JA, Tanizawa K, Dooley DM. Mechanistic studies of topa quinone biogenesis in phenylethylamine oxidase Biochemistry. 36: 1953-1959. PMID 9047291 DOI: 10.1021/bi9628836 |
0.42 |
|
| 1997 |
McGuirl MA, Brown DE, Dooley DM. Cyanide as a copper-directed inhibitor of amine oxidases: Implications for the mechanism of amine oxidation Journal of Biological Inorganic Chemistry. 2: 336-342. DOI: 10.1007/S007750050140 |
0.526 |
|
| 1996 |
Dove JE, Smith AJ, Kuchar J, Brown DE, Dooley DM, Klinman JP. Identification of the quinone cofactor in a lysyl oxidase from Pichia pastoris. Febs Letters. 398: 231-4. PMID 8977113 DOI: 10.1016/S0014-5793(96)01245-8 |
0.788 |
|
| 1996 |
Kumar V, Dooley DM, Freeman HC, Guss JM, Harvey I, McGuirl MA, Wilce MC, Zubak VM. Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 A resolution. Structure (London, England : 1993). 4: 943-55. PMID 8805580 DOI: 10.1016/S0969-2126(96)00101-3 |
0.512 |
|
| 1996 |
Dooley DM, Alvarez ML, Rosenzweig AC, Hollis RS, Zumft WG. Exogenous ligand binding to Pseudomonas stutzeri nitrous oxide reductase Inorganica Chimica Acta. 242: 239-244. DOI: 10.1016/0020-1693(95)04873-1 |
0.416 |
|
| 1996 |
Dooley DM, Brown DE. Intramolecular electron transfer in the oxidation of amines by methylamine oxidase from Arthrobacter P1 Journal of Biological Inorganic Chemistry. 1: 205-209. DOI: 10.1007/S007750050044 |
0.37 |
|
| 1994 |
Baron AJ, Stevens C, Wilmot C, Seneviratne KD, Blakeley V, Dooley DM, Phillips SEV, Knowles PF, McPherson MJ. Structure and mechanism of galactose oxidase: The free radical site Journal of Biological Chemistry. 269: 25095-25105. PMID 7929198 |
0.317 |
|
| 1994 |
Carter SR, McGuirl MA, Brown DE, Dooley DM. Purification and active-site characterization of equine plasma amine oxidase Journal of Inorganic Biochemistry. 56: 127-141. PMID 7798894 DOI: 10.1016/0162-0134(94)85043-7 |
0.408 |
|
| 1993 |
Turowski PN, McGuirl MA, Dooley DM. Intramolecular electron transfer rate between active-site copper and topa quinone in pea seedling amine oxidase Journal of Biological Chemistry. 268: 17680-17682. PMID 8349651 |
0.369 |
|
| 1992 |
Cooper RA, Knowles PF, Brown DE, McGuirl MA, Dooley DM. Evidence for copper and 3,4,6-trihydroxyphenylalanine quinone cofactors in an amine oxidase from the Gram-negative bacterium Escherichia coli K-12 Biochemical Journal. 288: 337-340. PMID 1334402 DOI: 10.1042/Bj2880337 |
0.342 |
|
| 1992 |
Janes SM, Palcic MM, Scaman CH, Smith AJ, Brown DE, Dooley DM, Mure M, Klinman JP. Identification of topaquinone and its consensus sequence in copper amine oxidases Biochemistry. 31: 12147-12154. DOI: 10.1021/Bi00163A025 |
0.303 |
|
| 1992 |
Dooley DM. Copper-site structure and reactivity in copper-containing amine oxidases and nitrous oxide reductases Journal of Inorganic Biochemistry. 47: 11. DOI: 10.1016/0162-0134(92)84082-X |
0.479 |
|
| 1991 |
Klinman JP, Dooley DM, Duine JA, Knowles PF, Mondovi B, Villafranca JJ. Status of the cofactor identity in copper oxidative enzymes. Febs Letters. 282: 1-4. PMID 1851106 DOI: 10.1016/0014-5793(91)80431-2 |
0.379 |
|
| 1991 |
Dooley DM, McGuirl MA, Brown DE, Turowski PN, Mclntire WS, Knowles PF. A Cu(I)-semiquinone state in substrate-reduced amine oxidases Nature. 349: 262-264. PMID 1846226 DOI: 10.1038/349262A0 |
0.4 |
|
| 1991 |
Farrar JA, Thomson AJ, Cheesman MR, Dooley DM, Zumft WG. A model of the copper centres of nitrous oxide reductase (Pseudomonas stutzeri). Evidence from optical, EPR and MCD spectroscopy Febs Letters. 294: 11-15. PMID 1660405 DOI: 10.1016/0014-5793(91)81331-2 |
0.433 |
|
| 1991 |
Dooley DM, McGuirl MA, Cote CE, Knowles PF, Singh I, Spiller M, Brown RD, Koenig SH. Coordination chemistry of copper-containing amine oxidases: Nuclear magnetic relaxation dispersion studies of copper binding, solvent-water exchange, substrate and inhibitor binding, and protein aggregation Journal of the American Chemical Society. 113: 754-761. DOI: 10.1021/Ja00003A004 |
0.407 |
|
| 1991 |
Turowski PN, Dooley DM, McGuirl MA. Variable temperature magnetic circular dichroism spectroscopy of copper-containing amine oxidases. Journal of Inorganic Biochemistry. 43: 187. DOI: 10.1016/0162-0134(91)84179-D |
0.316 |
|
| 1991 |
McGuirl M, Brown D, McCahon C, Turowski P, Dooley D. Copper-quinone interactions in amine oxidases Journal of Inorganic Biochemistry. 43: 186. DOI: 10.1016/0162-0134(91)84178-C |
0.4 |
|
| 1991 |
Farrar JA, Thomson AJ, Cheesman MR, Dooley DM, Zumft WG. The nature of the copper centres in nitrous oxide reductase (Pseudomonas stutzeri) Journal of Inorganic Biochemistry. 43: 181. DOI: 10.1016/0162-0134(91)84173-7 |
0.399 |
|
| 1990 |
McIntire WS, Dooley DM, McGuirl MA, Cote CE, Bates JL. Methylamine oxidase from Arthrobacter P1 as a prototype of eukaryotic plasma amine oxidase and diamine oxidase Journal of Neural Transmission, Supplement. 32: 315-318. PMID 1965196 DOI: 10.1007/978-3-7091-9113-2_40 |
0.416 |
|
| 1990 |
Dooley DM, McIntire WS, McGuirl MA, Cote CE, Bates JL. Characterization of the active site of Arthrobacter P1 methylamine oxidase: Evidence for copper-quinone interactions Journal of the American Chemical Society. 112: 2782-2789. DOI: 10.1021/Ja00163A047 |
0.583 |
|
| 1989 |
Collison D, Knowles PF, Mabbs FE, Rius FX, Singh I, Dooley DM, Cote CE, McGuirl M. Studies on the active site of pig plasma amine oxidase Biochemical Journal. 264: 663-669. PMID 2559715 DOI: 10.1042/Bj2640663 |
0.336 |
|
| 1989 |
Scott RA, Zumft WG, Coyle CL, Dooley DM. Pseudomonas stutzeri N2O reductase contains Cu(A)-type sites Proceedings of the National Academy of Sciences of the United States of America. 86: 4082-4086. PMID 2542963 DOI: 10.1073/Pnas.86.11.4082 |
0.495 |
|
| 1989 |
Dooley D. Characterization of the copper sites in nitrite reductase and nitrous oxide reductase Journal of Inorganic Biochemistry. 36: 170. DOI: 10.1016/0162-0134(89)84076-0 |
0.33 |
|
| 1988 |
Dooley DM, Moog RS, Liu MY, Payne WJ, LeGall J. Resonance Raman spectra of the copper-sulfur chromophores in Achromobacter cycloclastes nitrite reductase Journal of Biological Chemistry. 263: 14625-14628. PMID 3170560 |
0.301 |
|
| 1988 |
Scott RA, Cote CE, Dooley DM. Copper x-ray absorption spectroscopic studies of the bovine plasma amine oxidase-sulfide complex [Erratum to document cited in CA109(21):186258n] Inorganic Chemistry. 27: 4774-4774. DOI: 10.1021/Ic00299A020 |
0.321 |
|
| 1988 |
Scott RA, Coté CE, Dooley DM. Copper X-ray absorption spectroscopic studies of the bovine plasma amine oxidase-sulfide complex Inorganic Chemistry. 27: 3859-3861. DOI: 10.1021/Ic00294A035 |
0.429 |
|
| 1988 |
Dooley DM. Spectroscopic studies of the active sites in copper-containing amine oxidases Pharmacological Research Communications. 20: 151-152. DOI: 10.1016/S0031-6989(88)80584-8 |
0.355 |
|
| 1987 |
Dooley DM, McGuirl MA, Peisach J, McCracken J. The generation of an organic free radical in substrate-reduced pig kidney diamine oxidase-cyanide. Febs Letters. 214: 274-8. PMID 3106087 DOI: 10.1016/0014-5793(87)80069-8 |
0.338 |
|
| 1987 |
Dooley DM, Moog RS, Zumft WG. Characterization of the copper sites in Pseudomonas perfectomarina nitrous oxide reductase by resonance Raman spectroscopy Journal of the American Chemical Society. 109: 6730-6735. |
0.367 |
|
| 1986 |
Moog RS, McGuirl MA, Cote CE, Dooley DM. Evidence for methoxatin (pyrroloquinolinequinone) as the cofactor in bovine plasma amine oxidase from resonance Raman spectroscopy Proceedings of the National Academy of Sciences of the United States of America. 83: 8435-8439. PMID 3464962 DOI: 10.1073/Pnas.83.22.8435 |
0.392 |
|
| 1986 |
Dooley DM, McGuirl MA. Thermodynamics of azide and thiocyanate binding to bovine copper-zinc superoxide dismutase Inorganic Chemistry. 25: 1261-1264. DOI: 10.1002/Chin.198633079 |
0.486 |
|
| 1985 |
Dooley DM, Coté CE. Copper(II) coordination chemistry in bovine plasma amine oxidase: Azide and thiocyanate binding Inorganic Chemistry. 24: 3996-4000. DOI: 10.1021/Ic00218A007 |
0.511 |
|
| 1984 |
Dooley DM, Cote CE. Inactivation of beef plasma amine oxidase by sulfide Journal of Biological Chemistry. 259: 2923-2926. PMID 6321486 |
0.418 |
|
| 1984 |
Dooley DM, Coté CE, Golink KC. Inhibition of copper-containing amine oxidases by Cu(II) complexes and anions Journal of Molecular Catalysis. 23: 243-253. DOI: 10.1016/0304-5102(84)80012-7 |
0.413 |
|
| 1983 |
Dooley DM, Golnik KC. Spectroscopic and kinetics studies of the inhibition of pig kidney diamine oxidase by anions Journal of Biological Chemistry. 258: 4245-4248. PMID 6403525 |
0.362 |
|
| 1983 |
Dooley DM, Cote C, Golnik K. Inhibition of amine oxidases by Cu(II) complexes and anions: Mechanistic implications Inorganica Chimica Acta. 79: 52-53. DOI: 10.1016/S0020-1693(00)95078-3 |
0.314 |
|
| 1981 |
Dooley DM, Dawson JH, Stephens PJ, Gray HB. Spectroscopic studies of ascorbate oxidase. Electronic structure of the blue copper sites. Biochemistry. 20: 2024-8. PMID 7225370 DOI: 10.1021/Bi00510A044 |
0.369 |
|
| 1980 |
Dawson JH, Dooley DM, Gray HB. Coordination environment and fluoride binding of type 2 copper in the blue copper protein ascorbate oxidase. Proceedings of the National Academy of Sciences of the United States of America. 77: 5028-31. PMID 16592868 DOI: 10.1073/Pnas.77.9.5028 |
0.47 |
|
| 1980 |
Dooley DM, Coolbaugh TS. Inhibition of bovine plasma amine oxidase by superoxide dismutase active CU(II) complexes Biochemical and Biophysical Research Communications. 96: 823-830. PMID 6775631 |
0.33 |
|
| 1980 |
Solomon EI, Hare JW, Dooley DM, Dawson JH, Stephens PJ, Gray HB. Spectroscopic studies of stellacyanin, plastocyanin, and azurin. Electronic structure of the blue copper sites Journal of the American Chemical Society. 102: 168-178. DOI: 10.1021/Ja00521A029 |
0.398 |
|
| 1979 |
Dooley DM, Rawlings J, Dawson JH, Stephens PJ, Andreasson L, Malmstrom BG, Gray HB. Spectroscopic studies of Rhus vernicifera and Polyporus versicolor laccase. Electronic structures of the copper sites Journal of the American Chemical Society. 101: 5038-5046. DOI: 10.1021/Ja00511A039 |
0.399 |
|
| 1979 |
Roundhill SGN, Roundhill DM, Bloomquist DR, Landee C, Willett RD, Dooley DM, Gray HB. Molecular structure and magnetic properties of the chloro-bridged dimer chloro[hydrotris(1-pyrazolyl)borato]copper(II). Observation of a ferromagnetic ground state Inorganic Chemistry. 18: 831-835. DOI: 10.1021/Ic50193A059 |
0.333 |
|
| 1979 |
Dawson JH, Dooley DM, Clark R, Stephens PJ, Gray HB. Spectroscopic studies of ceruloplasmin. Electronic structures of the copper sites Journal of the American Chemical Society. 101: 5046-5053. |
0.302 |
|
| 1978 |
Dawson JH, Dooley DM, Gray HB. Coordination environment and fluoride binding of type 2 copper in the blue copper oxidase ceruloplasmin. Proceedings of the National Academy of Sciences of the United States of America. 75: 4078-81. PMID 212731 DOI: 10.1073/Pnas.75.9.4078 |
0.427 |
|
| Show low-probability matches. |