Amine Oxidase Publications

Amine Oxidase and Galactose Oxidase in Copper Oxygen Chemistry, Wiley Series on Reactive Intermediates in Chemistry and Biochemistry: Rokhsana D, Shepard EM, Brown DE, and Dooley DM. (K. Karlin and Itoh, S., Eds.) Wiley Press (2010 in press).
A New Crystal Form of Human Diamine Oxidase, McGrath AP, Hilmer KM, Collyer CA, Dooley DM, Guss JM. Acta Crystallogr, Sect. F Struct Biol Cryst Comm. Feb 1;66(Pt 2):137-42 (2010).
Structure and Inhibition of Human Diamine Oxidase, McGrath AP, Hilmer KM, Collyer CA, Shepard EM, Elmore BO, Dooley DM, Guss JM. Biochemistry :48:9810-22 (2009).
Concluding Remarks (Chapter 18) in Copper Amine Oxidases: Structures, Catalytic Mechanisms and Role in Pathophysiology. Dooley D.M., (Floris, G and Mondovi, B; Eds). CRC Press (2009).
Kinetics and Spectroscopic Evidence that the Cu(I) – Semiquinone Intermediate Reduces Molecular Oxygen in the Oxidative Half-Reaction of Arthrobacter globiformis Amine Oxidase. Shepard EM, Okonski KM, Dooley DM. Biochemistry.47(52):13907-20 (2008).
Inner-sphere Mechanism for Molecular Oxygen Reduction Catalyzed by Copper Amine Oxidases. Mukherjee A, Smirnov VV, Lanci MP, Brown DE, Shepard EM, Dooley DM, Roth JP. J. Am. Chem. Soc. 130(29):9459-73 (2008).

Complexes of the Copper-Containing Amine Oxidase from Arthrobacter globiformis with the Inhibitors Benzylhydrazine and Tranylcypromine. Langley DB, Trambaiolo DM, Duff AP, Dooley DM, Freeman HC, and Guss JM. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64(Pt 7):577-83 (2008).
Enantiomer-Specific Binding of Ruthenium(II) Molecular Wires by the Amine Oxidase of Arthrobacter globiformis. Langley DB, Brown DE, Cheruzel LE, Contakes SM, Duff AP, Hilmer KM, Dooley DM, Gray, HB, Guss, JM, and Freeman HC. J. Am. Chem. Soc. 130(25):8069-78 (2008).
Hydrazine and Amphetamine Binding to Amine Oxidases: Old Drugs With New Prospects. Knowles, P, Kurtis, C, Murray, J, Saysell, C, Tambyrajah, W, Wilmot, C, McPherson, M, Phillips, S, Dooley, D, Brown, D, Rogers, M, and Mure, M. J. Neural. Transm., 114(6): 743-746 (2007).
A Comparative Study of the Binding and Inhibition of Four Copper Containing Amine Oxidases by Azide: Implication for the Role of Copper During the Oxidative Half-Reaction, Juda, GA, Shepard, EM, Elmore, BO, and Dooley, DM. Biochemistry, 45(29), 8788-8800 (2006).
Mechanism-Based Cofactor Derivatization of a Copper Amine Oxidase with an Aromatization-Prone Branched Primary Amine Recruits the Oxidase Activity of the Enzyme to Turn Inactivator into Substrate, Qiao, C, Lin, KQ, Shepard , ES, Dooley, DM, and Sayre, LM. J. Amer. Chem. Soc., 128(18), 6206-19 (2006).
Reversible Inhibition of Copper Amine Oxidase Activity by Channel-blocking Ruthenium(II) and Rhenium(I) Molecular Wires. Contakes, S.M ., Juda, G.A., Langley, D.B., Halpern-Manners, N.W., Duff, A.P., Dunn, A.R., Gray, H.G., Dooley, D.M., Guss, J.M., and Freeman, H.C. PNAS , 102(38), 13451-13456, (2005).
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 E.coli Amine Oxidase. Mure, M., Brown, D.E., Saysell, C., Rogers, M.S., Wilmot, C.M., Kurtis, C. R., McPherson, M.J., Phillips, S.E.V., Knowles, P.F., and Dooley, D.M., Biochemistry, 44(5), 1568-1582, (2005).
Active Site Rearrangement of the 2-Hydrazinopyridine Adduct in E.coli Amine Oxidase to an Azo Cu(II) Chelate Form: A Key Role for Y369 in Controlling the Mobility of the TPQ-2HP Adduct. Mure, M., Kurtis, C.R., Brown, D.E., Rogers, M.S., Tambyrajah, W.S., Saysell, C., Wilmot, C.M., Phillips, S.E.V., Knowles, P.F., Dooley, D.M., and McPherson, M.J., Biochemistry, 44(5), 1583-1594, (2005).
Using Xenon as a Probe for Dioxygen-Binding Sites in Copper Amine Oxidases. Duff, A.P., Trambaiola, D.M., Cohen, A.E., Ellis, P.J., Juda, G.A., Shepard, E.M., Langley, D.B., Dooley, D.M., Freeman, H.C., and Guss, J.M., J. Mol. Biol., 344, 599-607, (2004).
Differential Inhibition of Six Copper Amine Oxidases by a Family of 4-(aryloxy)-2-butynamines: Evidence for a New Mode of Inactivation. O’Connell, K.M., Langley, D.B., Shepard, E.M., Duff, A.P., Jeon, H., Sun, G., Freeman, H.C., Guss, J.M., Sayre, L.M., and Dooley, D.M., Biochemistry, 43(34): 10965-10978 (2004).
Cyanide as a Copper and Quinone-Directed Inhibitor of Amine Oxidases from Pea Seedlings (Pisumsativum) and Arthrobacter globiformis: Evidence for Both Copper Coordination and Cyanohydrin Derivatization of the Quinone Cofactor. Shepard, E.M., Juda, G.A., Ling, K.Q. Sayre, L.M., and Dooley, D.M., J. Biol. Inorg. Chem., 9(3): 256-268, (2004).
The Crystal Structure of Pichia pastoris Lysyl Oxidase. Duff, A.P., Cohen, A.E., Ellis, P.J., Kuchar, J.A., Langley, D.B., Shepard, E.M., Dooley, D.M., Freeman, H.C., and Guss, J.M., Biochemistry, 42, 15148-15157, (2003).
Gold Electrodes Wired for Coupling with the Deeply Buried Active Site of Arthrobacter globiformis Amine Oxidase. Hess, C.R., Juda, G.A., Dooley, D.M., Amii, R.N., Hill, M.G., Winkler, J.R., and Gray, H.B. J. Amer. Chem. Soc., 125(24): 7156-7, (2003).
Inhibition of Six Copper-Containing Amine Oxidases by the Antidepressant Drug Tranylcypromine, Shepard, E.M., Heggem, H., Juda, G.A., and Dooley, D.M. Biochim. Biophys. Acta. 1647 (1-2): 252-9, (2003).
Crystallization of Pichia pastoris Lysyl Oxidase, Lee, M., Willingham, K., Langley, D., Maher, M.J., Cohen, A.E., Ellis, P.J., Kuchar, J.A., Dooley, D.M., Freeman, H.C., and Guss, J.M., Acta. Crystallogr. D Biol. Crystallogr., 58 (Pt 12): 2177-9 (2002).
Towards the Development of Selective Amine Oxidase Inhibitors. Mechanism-Based Inhibition of Six Copper-Containing Amine Oxidases, Shepard, E.M., Smith, J.A., Elmore, B.O., Kuchar, J.A., Sayre, L.M and Dooley, D.M., Eur. J. Biochem., 269 (15): 3645-58 (2002).
3-Pyrrolines are Mechanism-Based Inactivators of the Quinone-Dependent Amine Oxidases, but only Substrates of the Flavin-Dependent Amine Oxidases. Lee, Y., Ling KQ, Lu, X., Silverman, R., Shepard, E. M., Dooley, D. M., and Sayre, L. M., J. Amer. Chem. Soc., 124 (41): 12135-43 (2002).
Rates of Oxygen and Hydrogen Exchange as Indicators of TPQ Cofactor Orientation in Amine Oxidases, Green, E.L., Nakamura, N., Dooley, D.M., Klinman, J.P, Sanders-Loehr, J., Biochemistry., 41, 687-96 (2002).
Human Kidney Diamine Oxidase: Heterologous Expression, Purification, and Characterization, Elmore, B.O., Bollinger, J.A., and Dooley, D.M., J. Biol. Inorg. Chem., 7 (6): 565-79 (2002).
Construction, Overexpression, and Purification of Arthrobacter globiformis Amine Oxidase-Strep-tag II Fusion protein, Juda, G.A., Bollinger, J.A., and Dooley, D.M., Protein. Expr. Purif. 22, 455-61, (2001).
Critical Commentary on “Visualization of Dioxygen Bound to Copper During Enzyme Catalysis, by C. M. Wilmot, J. Hajdu, M. J. McPherson, P. F. Knowles, and S. E. V. Phillips”, by B.O., Elmore, B.O., and D.M., Dooley., ChemTracts-Inorganic Chemistry, 14, 243-251 (2001).
Catalytic Turnover of Substrate Benzylamines by the Quinone-Dependent Plasma Amine Oxidase Leads to H 2O 2-Dependent Inactivation. Evidence for Generation of a Cofactor-Derived Benzoxazole, Lee, Y., Shepard, E. M., Smith, J.A., Dooley, D.M., and Sayre, L.M., Biochemistry, 40, 822-829 (2001).
Cloning, Sequence Analysis, and Characterization of the “Lysyl Oxidase” from Pichia pastoris, Kuchar, J.A., and Dooley, D.M., J. Inorg. Biochem., 83, 193-204 (2001).
Structure and Biogenesis of Topaquinone and Related Cofactors, David M. Dooley, J. Biol. Inorg. Chem., 4, 1-11 (1999).
Stoichiometry of the Topa Quinone Biogenesis Reaction in Copper Amine Oxidases, Ruggiero, C.E., and Dooley, D.M., Biochemistry, 38, 2892-2898 (1999).
Copper-containing Oxidases, McGuirl, M.A., and Dooley, D.M., Current Opinion in Chemical Biology, 3:138-144 (1999).
Structures of the Cu(I) and Cu(II) Forms of Amine Oxidases from X-ray Absorption Spectroscopy, D.M. Dooley, R.A. Scott, P.F. Knowles, C.M. Colangelo, M.A. McGuirl, and D.E. Brown, J. Amer. Chem. Soc., 120 2599-2605 (1998).
Crystal Structures of the Copper-Containing Amine Oxidase from Arthrobacter Globiformis in the Holo- and Apo-Forms: Implications for the Biogenesis of Topa Quinone, M. C. J. Wilce, D. M. Dooley, H. C. Freeman, J. M. Guss, H. Matsunami, W. S. McIntire, C. E. Ruggiero, K. Tanizawa, and H. Yamaguchi, Biochemistry, 36, 16116-16133, (1997).
Cyanide as a Copper-Directed Inhibitor of Amine Oxidases: Implications for the Mechanism of Amine Oxidase, M. A. McGuirl, D. E. Brown, and D. M. Dooley, J. Biol. Inorg. Chem., 2, 336-342 (1997).
Mechanistic Studies of Topa Quinone Biogenesis in Phenylethylamine Oxidase, C. E. Ruggiero, J. A. Smith, K. Tanizawa, and D. M. Dooley, Biochemistry, 36, 1953-1959 (1997).
Identification of the Quinone Cofactor in a Lysyl Oxidase from Pichia pastoris, J. E. Dove, A. J. Smith, J. Kuchar, D. E. Brown, D. M. Dooley, and J. P. Klinman, FEBS Lett. 398, 231-234 (1996).
Crystal Structure of a Eukaryotic (Pea Seedling) Copper-Containing Amine Oxidase at 2.2 Å Resolution, V. Kumar, D. M. Dooley, H. C. Freeman, J. M. Guss, I. Harvey, M. A. McGuirl, M. C. J. Wilce, and V. M. Zubak, Structure, 4, 943-955 (1996).
Intramolecular Electron Transfer in the Oxidation of Amines by Methylamine Oxidase from Arthrobacter P1, D. M. Dooley and D. E. Brown, J. Biol. Inorg. Chem., 1, 205-209 (1996).
Resonance Raman Spectroscopy of Quinoproteins, D. E. Brown and D. M. Dooley in "Methods in Enzymology" (J. P. Klinman, Ed.) Academic Press, New York, 258, 132-140 (1995).
Detection of Reaction Intermediates in Topa Quinone Enzymes, D. M. Dooley and C. Hartmann, in "Methods in Enzymology" (J. P. Klinman, Ed.) Academic Press, New York, 258, 69-90 (1995).
Commentary on: Copper Amine Oxidase: Heterologous Expression, Purification, and Characterization of an Active Enzyme in Saccharomyces cerevisiae, (Biochemistry, 1994, 33, 7647); and Generation of the Topa Quinone Cofactor in Bacterial Monoamine Oxidase by Cupric Ion-Dependent Autoxidation of a Specific Tyrosyl Residue, (FEBS Lett., 1994, 351, 360); D. M. Dooley, Chemtracts-Inorganic Chem., 6, 114-120 (1994).
Mechanistic Studies of Copper/Topa Amine Oxidases, D. M. Dooley, D. E. Brown, M. A. McGuirl, and L. J. Sears, Biochemistry of Vitamin B 6 and PQQ, 253-257 (1994).
Purification and Characterization of Pea Seedling Amine Oxidase for Crystallization Studies, M. A. McGuirl, C. D. McCahon, K. A. McKeown, and D. M. Dooley, Plant Physiol, 106, 1205-1211 (1994).
Amine Oxidases, P. F. Knowles and D. M. Dooley in "Metal Ions in Biological Systems" (H. Sigel & A. Sigel, Eds.) Marcel Dekker, New York, 361-403 (1994).
Purification and Active-Site Characterization of Equine Plasma Amine Oxidase, S. R. Carter, M. A. McGuirl, D. E. Brown and D. M. Dooley, J. Inorg. Biochem., 56, 127-141 (1994).
Structure of the Topa-semiquinone Catalytic Intermediate of Amine Oxidase as Revealed by Magnetic Interactions with Exchangeable 2H and 1H Nuclei, K. Warncke, G. T. Babcock, D. M. Dooley, M. A. McGuirl and J. McCracken, J. Amer. Chem. Soc., 116, 4028-4037 (1994).
Intramolecular Electron Transfer Rate Between Active-site Copper and Topa Quinone in Pea Seedling Amine Oxidase, P. N. Turowski, M. A. McGuirl and D. M. Dooley, J. Biol. Chem., 268, 17680-17682 (1993).
Structure and Reactivity of Copper-Containing Amine Oxidases, D. M. Dooley, D. E. Brown, A. W. Clague, J. N. Kemsley, C. D. McCahon, M. A. McGuirl, P. N. Turowski, W. S. McIntire, J. A. Farrar and A. J. Thomson in "Bioinorganic Chemistry of Copper" (K. D. Karlin and Z. Tyeklar, Eds.) Chapman & Hall, New York, 459-470 (1993).
Crystallization and Preliminary Crystallographic Characterization of the Copper-Containing Amine Oxidase from Pea Seedlings, V. Vignevich, D. M. Dooley, J. M. Guss, I. Harvey, M. A. McGuirl and H. C. Freeman, J. Mol. Biol. 229, 243-245 (1993).
Resonance Raman Spectroscopy of Quinoproteins, D. M. Dooley and D. E. Brown in "Principles and Applications of Quinoproteins" (V. L. Davidson, Ed.) Dekker, New York, 275-305 (1993).
Pulsed EPR Studies of the Semiquinone State of Copper-Containing Amine Oxidases, J. McCracken, J. Peisach, C. E. Cote, M. A. McGuirl and D. M. Dooley, J. Amer. Chem. Soc. 114, 3715-3720 (1992).
The Tyrosine Codon Corresponds to 6-Hydroxydopa at the Active Site of Copper Amine Oxidases, D. Mu, S. M. Janes, A. J. Smith, D. E. Brown, D. M. Dooley and J. P. Klinman, J. Biol. Chem. 267, 7979-7982 (1992).
Evidence for Copper and 3,4,6-trihydroxyphenylalanine Quinone Cofactors in an Amine Oxidase from the Gram-Negative Bacterium Escherichia Coli K-12, R. A. Cooper, P. F. Knowles, D. E. Brown, M. A. McGuirl and D. M. Dooley, Biochem. J. 288, 337-340 (1992).
Identification of Topaquinone and its Consensus Sequence in Copper Amine Oxidases, S. M. Janes, M. M. Palcic, C. H. Scaman, A. J. Smith, D. E. Brown, D. M. Dooley, M. Mure and J. P. Klinman, Biochemistry 31, 12147-12154 (1992).
Status of the Cofactor Content of Copper Oxidative Enzymes, J. P. Klinman, D. M. Dooley, H. Duine, P. F. Knowles, B. Mondovi and J. J. Villafranca, FEBS Lett. 282, 1-4 (1991).
The Organic Cofactor in Copper-Containing Amine Oxidases: Resonance Raman Spectra Are Consistent with the Presence of Topa Quinone (6-Hydroxy dopa Quinone) in the Active Site, D. E. Brown, M. A. McGuirl, D. M. Dooley, S. M. Janes, D. Mu and J. P. Klinman, J. Biol. Chem. 266, 4049-4051 (1991).
A Cu(I)-Semiquinone State in Substrate-Reduced Amine Oxidases, D. M. Dooley, M. A. McGuirl, D. E. Brown, P. N. Turowski, W. S. McIntire and P. F. Knowles, Nature 349, 262-264 (1991).
Coordination Chemistry of Copper-Containing Amine Oxidases: Nuclear Magnetic Relaxation Dispersion (NMRD) Studies of Solvent Water Exchange, Inhibitor and Substrate Binding, and Protein Association, D. M. Dooley, M. A. McGuirl, C. E. Cote, P. F. Knowles, M. Spiller, R. D. Brown, III and S. H. Koenig, J. Amer. Chem. Soc. 113, 754-761 (1991).
Characterization of the Active Site of Arthrobacter P1 Methylamine Oxidase: Evidence for Copper-Quinone Interactions, D. M. Dooley, W. C. McIntire, M. A. McGuirl, C. E. Cote and J. L. Bates, J. Amer. Chem. Soc. 112, 2782-2789 (1990).
Methylamine Oxidase from Arthrobacter P1 as a Prototype of Eukaryotic Plasma Amine Oxidase and Diamine Oxidase, W. S. McIntire, D. M Dooley, M. A. McGuirl, C. E. Cote and J. L. Bates, J. Neural Transm. 32, 315-318 (1990).
Studies on the Active Site of Pig Plasma Amine Oxidase, D. Collison, P. F. Knowles, F. E. Mabbs, F. X. Rius, I. Singh, D. M. Dooley, C. E. Cote and M. A. McGuirl, Biochem. J. 264, 663-669 (1989).
Copper-PQQ Interactions in Amine Oxidases, D. M. Dooley, C. E. Cote, M. A. McGuirl, J. L. Bates, J. B. Perkins, R. S. Moog, I. Singh, P. F. Knowles and W. C. McIntire in "PQQ and Quinoproteins" (J. A. Jongejan and J. A. Duine, Eds.) Kluwer Academic Publishers, 307-316 (1989).
Active Site Structures of Copper-Containing Oxidases, P. F. Knowles, I. Singh, K. S. S. Yadav, F. E. Mabbs, D. Collison, C. E. Cote, D. M. Dooley and M. A. McGuirl in "PQQ and Quinoproteins" (J. A. Jogejan and J. A. Duine, Eds.) Kluwer Academic Publishers, 283-288 (1989).
Spectroscopic Studies of the Active Sites in Copper-Containing Amine Oxidases, D. M. Dooley, Pharm. Res. Commun. 20, 151-152 (1988).
Copper X-ray Absorption Spectroscopic Studies of the Bovine Plasma Amine Oxidase-Sulfide Complex, R. A. Scott, C. E. Cote and D. M. Dooley, Inorg. Chem. 27, 3859-3861 (1988).
The Generation of an Organic Free Radical in Substrate-Reduced Pig Kidney Diamine Oxidase-Cyanide, D. M. Dooley, M. A. McGuirl, J. Peisach and J. McCracken, FEBS Lett. 214, 274-278 (1987).
Cu(II) Coordination Chemistry of Amind Oxidases: Pulsed EPR Studies of Histidine Imidazole, Water, and Exogenous Ligand Coordination, J. McCracken, J. Peisach and D. M. Dooley, J. Amer. Chem. Soc. 109, 4064-4072 (1987).
The Organic Cofactor in Plasma Amine Oxidase: Evidence for Pyrroloquinolinequinone and Against Pyridoxal Phosphate, P. F. Knowles, K. B. Pandeya, F. X. Rius, C. M. Spencer, R. S. Moog, M. A. McGuirl and D. M. Dooley, Biochem. J. 241, 603-608 (1987).
Spectroscopic Studies of Pig Kidney Diamine Oxidase-Anion Complexes, D. M. Dooley and M. A. McGuirl, Inorg. Chim. Acta 123, 231-236 (1986).
Evidence for Methoxatin (Pyrroloquinolinequinone) as the Cofactor in Bovine Plasma Amine Oxidase from Resonance Raman Spectroscopy, R. S. Moog, M. A. McGuirl, C. E. Cote and D. M. Dooley, Proc. Natl. Acad. Sci. (USA) 83, 8435-8439 (1986).
X-ray Absorption Spectroscopic Studies of the Cu(II) Sites in Bovine Plasma Amine Oxidase, R. A. Scott and D. M. Dooley, J. Amer. Chem. Soc. 107, 4348-4350 (1985).
Cu(II) Coordination Chemistry in Beef Plasma Amine Oxidase: Azide and Thiocyanate Binding. Dooley, D.M., and Cote, C.E. Inorg. Chem. 24, 3996-4000 (1985).
Inactivation of Beef Plasma Amine Oxidase by Sulfide, D. M. Dooley and C. E. Cote, J. Biol. Chem. 259, 2923-2926 (1984).
Inhibition of Copper-Containing Amine Oxidases by Cu(II) Complexes and Anions, D. M. Dooley, C. E. Cote and K. C. Golnik, J. Mol. Catalysis 23, 243-253 (1984).
Inhibition of Amine Oxidases by Cu(II) Complexes and Anions: Mechanistic Implications, D. M. Dooley, C. E. Cote and K. C. Golnik, Inorg. Chim. Acta 79, 52-53 (1983).
Spectroscopic and Kinetics Studies of the Inhibition of Pig Kidney Diamine Oxidase by Anions, D. M. Dooley and K. C. Golnik, J. Biol. Chem. 258, 4245-4248 (1983).
Inhibition of Beef Plasma Amine Oxidase by Superoxide Dismutase Active Copper Complexes, D. M. Dooley and T. S., Coolbaugh, Biochem. Biophys. Res. Comm. 96 (2), 823-830 (1980).

Lysyl Oxidase Publications

The Formation of Lysyl Tyrosylquinone (LTQ) is a Self-Processing Reaction. Expression and Characterization a Drosophila Lysyl Oxidase. Bollinger, J.A., Brown, D.E., and Dooley, D.M., Biochemistry, 44(35), 11708-11714, (2005).
Drosophila Lysyl Oxidases DmLOX-1 and DmLOX-2 are Differentially Expressed and Active DmLOX-1 Influences Gene Expression and Development. Molnar, J., Ujfaldi, Z., Fong, S.F.T., Bollinger, J.A., Waro, G., Fogelgren, B., Dooley, D., Mink, M., and Csiszar, K., J. Biol. Chem., 280(44), 22977-22985, (2005).
A Crosslinked Cofactor in Lysyl Oxidase: Redox Function for Amino Acid Side Chains, S.X. Wang, M. Mure, K. F. Medzihradsky, A. L. Burlingame, D. E. Brown, D. M. Dooley, A. J. Smith, H. M. Kagan, and J. P. Klinman, Science, 273, 1078-1084 (1996).
Evidence for Pyrroloquinolinequinone as the Carbonyl Cofactor in Bovine Aorta Lysyl Oxidase from Absorption and Resonance Raman Spectroscopy, P. R. Williamson, R. S Moog, D. M. Dooley and H. M. Kagan, J. Biol. Chem. 261, 16302-16305 (1986).

Nitrous Oxide Reductase Publications

Non-covalent interaction in blue copper proteins probed by Met16 mutation and electronic resonance Raman spectroscopy of Achromobacter cyclosclastes pseudoazurin. Fitzpatrick MB, Obara Y, Fujita K, Brown DE, Dooley DM, Kohzuma T, Czernuszewicz RS. J. Ionorg. Biochem 104(3):250-60 (2010).
Anaerobic Purification, Characterization, and Preliminary Mechanistic Study of Recombinant Nitrous Oxide Reductase from Achromobacter cycloclastes. Fujita, K, Chan, JM, Bollinger, JA, Moenne-Loccoz, ML, and Dooley, DM. J. Biol. Inorg, Chem., 101(11-12):1836-44 (2007).
Spectroscopic, Computational, and Kinetic Studies of the μ(4)-Sulfide-Bridged Tetranuclear Cu(Z) Cluster in N(2)O Reductase: pH Effect on the Edge Ligand and Its Contribution to Reactivity. Ghosh S, Gorelsky SI, George SD, Chan JM, Cabrito I, Dooley DM, Moura JJ, Moura I, and Solomon EI., JACS. (2007) http://dx.doi.org/10.1021/ja068059e
Insights into the Mechanism of N 2O Reduction by Reductively Activated N 2O Reductase from Kinetics and Spectroscopic Studies of pH Effects. Fujita, K, and Dooley, DM. Inorganic Chemistry, 46(3): 613-615 (2007).

Structural Studies of NosL, an Accessory Protein of Nitrous Oxide Reductase: Insights from Structural Homology with MerB, a Mercury Resistant Protein. Taubner, LM, McGuirl, MA, Dooley , DM, and Copié, V. Biochemistry 45(40) 12240-52, (2006).
Reductively Activated Nitrous Oxide Reductase Reacts Directly with Substrate. Chan, J.M., Bollinger, J.A., Grewell, C.L., and Dooley, D.M., J. Amer. Chem. Soc., 126(10): 3030-3031, (2004).
1 H, 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. Taubner, L.M., McGuirl, M.A., Dooley, D.M., and Copie, V.J., J. Biomol. NMR.., 29(2): 211-2, (2004).
Characterization of the Copper-Sulfur Chromophores in Nitrous Oxide Reductase by Resonance Raman Spectroscopy: Evidence for Sulfur Coordination in the Catalytic Cluster. Alvarez, M.L., Ai, J., Zumft, W., Sanders-Loehr, J., and Dooley, D.M., J. Amer. Chem. Soc., 123, 576-587 (2001).
Expression, Purification, and Characterization of NosL, a Novel Cu(I) Protein of the Nitrous Oxide Reductase (nos) Gene Cluster, McGuirl, M.A., Bollinger, J.A., and Dooley, D.M., J. Biol. Inorg. Chem., 6, 189-195 (2001)
The Catalytic Center in Nitrous Oxide Reductase, Cu Z, is a Copper-Sulfide Cluster, Rasmussen, T., Berks, B.C., Sanders-Loehr, J., Dooley, D.M., Zumft, W., and Thomson, A.J., Biochemistry, 39, 12753-12756 (2000).

1 H NMR studies on the CuA center of nitrous oxide reductase from Pseudomonas stutzeri. Holz, R.C., Alvarez, M.L., Zumft, W.G., and Dooley, D.M., Biochemistry, 38(34):11164-11171, (1999).

The nos (Nitrous Oxide Reductase) Gene Cluster from the Soil Bacterium Achromobacter Cycloclastes: Cloning, Sequence Analysis, and Expression, M.A. McGuirl, L. K. Nelson, J. A. Bollinger, Y.-K. Chan, and D. M. Dooley, J. Inorg. Biochem., 70, 155-169 (1998).

Exogenous Ligand Binding to Pseudomonas stutzeri Nitrous Oxide Reductase, D. M. Dooley, M. Alvarez, A. C. Rosenzweig, and R. S. Hollis, Inorg. Chim. Acta, 242, 239-244 (1996).

Commentary on: Metal-Metal Bonding in Biology: EXAFS Evidence for a 2.5 Å Copper-Copper Bond in the Cu A Center of Cytochrome Oxidase (Biochemistry, 1994, 33, 10401-10407), M. L. Alvarez and D. M. Dooley, Chemtracts-Inorganic Chem., 7, 19-26 (1995).

Copper Proteins with Type 2 Sites and Copper-Containing Enzymes in Denitrification, D. M. Dooley in "Encyclopedia of Inorganic Chemistry" (R. B. King, Ed.) Wiley, New York (1994).

A Model of the Copper Centres of Nitrous Oxide Reductase (Pseudomonas stutzeri), J. A. Farrar, A. J. Thomson, M. R. Cheesman, D. M. Dooley and W. G. Zumft, FEBS Lett. 294, 1,2, 11-15 (1991).

Magnetic Properties of Pseudomonas stutzeri Nitrous Oxide Reductase, D. M. Dooley, J. A. Landin, A. C. Rosenzweig, W. G. Zumft and E. P. Day, J. Amer. Chem. Soc. 113, 8978-8980 (1991).

Spectroscopic Studies of the Copper Sites in Pseudomonas stutzeri N 2O Reductase, D. M. Dooley, M. A. McGuirl, A. C. Rosenzweig, J. A. Landin, R. A. Scott, W. G. Zumft, F. Devlin and P. J. Stephens, Inorg. Chem. 30, 3006-3011 (1991).

Pseudomonas stutzeri N 2O Reductase Contains Cu A-Type Sites, R. A. Scott, W. G. Zumft, C. L. Coyle and D. M. Dooley, Proc. Natl. Acad. Sci (USA) 86, 4028-4089 (1989).

Resonance Raman Spectra of the Copper-Sulfur Chromophores in "Achromobacter Cycloclastes" Nitrite Reductase, D. M. Dooley, R. S. Moog and J. LeGall, J. Biol. Chem. 263, 14625-14628 (1988).

Nitrous Oxide Reductase, Spectroscopy and Molecular Biology, W. G. Zumft, A. Viebrock, J. Riester, P. M. H. Kroneck, D. M. Dooley and C. L. Coyle, J. Royal Netherlands Chem. Soc. 106, 352 (1987).

Characterization of the Copper Sites in Pseudomonas perfectomarina N 2O Reductase by Resonance Raman Spectroscopy, D. M. Dooley, R. S. Moog and W. G. Zumft, J. Amer. Chem. Soc. 109, 6730-6735 (1987).

Galactose Oxidase Publications

Cross-link Formation of the Cysteine 228-Tryosine 272 Catalytic Cofactor of Galactose Oxidase Does Not Require Dioxygen. Rogers, MS, Hurtado-Guerro R, Firbank SJ, Halcrow MA, Dooley DM, Phillips SE, Knowles PF, McPherson MJ. Biochemistry. 47(39):10428-39 (2008).
Systematic Development of Computational Models for the Catalytic Site in Galactose Oxidase: Impact of Outer-Sphere Residues on the Geometric and Electronic Structures. Rokhsana D, Dooley DM, Szilagyi RK. J. Biol. Inorg. Chem. Mar;13(3):371-83 (2008).
The Stacking Tryptophan of Galactose Oxidase: A Second Coordination Sphere Residue That Has Profound Effects on Tyrosyl Radical Behavior and Enzyme Catalysis. Rogers, MS, Tyler, EM, Akyumani, N, Kurtis, CR, Spooner, K, Deacon, SE, Tamber, S, Firbank, SJ, Mahmoud, K, Knowles, PK, Phillips, SEV, McPherson, MJ and Dooley, DM. Accepted in Biochemistry (2007).

Structure of the Oxidized Active Site of Galactose Oxidase from Realistic In Silico Models. Rokhsana, D, Dooley, DM, and Szilagyi, RK. J. Amer. Chem. Soc, 128(49):15550-15551 (2006).

Cofactor Processing in Galactose Oxidase. Firbank, S.J., Rogers, M.S., Hurtado-Guerrero, R., Dooley, D.M., Halcrow, M.A., Phillips, S.E., Knowles, P.F., and McPherson, M.J. Biochem. Soc. Trans. 31(3): 506-9 (2003).

Copper-Tyrosyl Radical Enzymes, Rogers, M.S., and Dooley, D.M. Curr. Opin. Chem. Biol. 7 (2): 189-96 (2003).

Post Translationally Modified Tyrosines from Galactose Oxidase and Cytochrome c Oxidase, Rogers, M.S., and Dooley, D.M., Advances in Protein Chemistry, 58, 387-436 (2001).

Crystal Structure of the Precursor of Galactose Oxidase: An Unusual Self-Processing Enzyme. Firbank, S.J., Rogers, M.S., Wilmot, C.M., Dooley, D.M., Halcrow, M.A., Knowles, P.F., McPherson, M.J., and Phillips, S.E.V., Proc. Natl. Acad. Sci., 98, 12932-12937 (2001).

Galactose Oxidase Pro-sequence Cleavage and Cofactor Assembly Are Self-Processing Reactions, Rogers, M.S., Baron, A.J., McPherson, M.J., Knowles, P.F., and Dooley, D.M., J. Am. Chem. Soc., 122, 990-991 (2000).

Characterization of the Active Site of Galactose Oxidase and Its Active Site Mutational Variants Y495F/H/K and W290H by Circular Dichroism Spectroscopy, M.S. Rogers, P.F. Knowles, A.J. Baron, M.J. McPherson, and D.M. Dooley, Inorg, Chim. Acta, 275-276, 175-181 (1998).

Spectroscopic Studies of the Active Site of Galactose Oxidase, P. F. Knowles, R. D. Brown III, S. H. Koenig, S. Wang, R. A. Scott, M. A. McGuirl, D. E. Brown, and D. M. Dooley, Inorg. Chem., 34, 3895-3902 (1995).

Structure and Mechanism of Galactose Oxidase: the Free Radical Site, A. J. Baron, C. Stevens, C. Wilmot, K. D. Seneviratne, V. Blakeley, D. M. Dooley, S. E. V. Phillips, P. F. Knowles, and M. J. McPherson, J. Biol. Chem., 269, 25095-95105 (1994).

Misc

Spectroscopic Identification of Heme Axial Ligans in HtsA that are involved in Heme Acquisition by Streptococcus pyogenes Ran Y, Liu M, Zhu H, Nygaard TK, Brown DE, Fabian M, Dooley DM, Lei B. Biochemistry. 49(13):2834-42 (2010).
Pathway for heme uptake from human methemoglobin by the iron-regulated surface determinants system of Staphylococcus aureus. Zhu H, Xie G, Liu M, Olson JS, Fabian M, Dooley DM, Lei B. J. Biol. Chem. 283(26):18450-60 (2008).
Direct hemin transfer from IsdA to IsdC in the iron-regulated surface determinant (Isd) heme acquisition system of Staphylococcus aureus. Liu M, Tanaka WN, Zhu H, Xie G, Dooley DM, and Lei B. J. Biol. Chem. 283(11), 6668-6676 (2008).
Bis-methionine ligation to heme iron in the streptococcal cell surface protein Shp facilitates rapid hemin transfer to HtsA of the HtsABC transporter. Ran Y, Zhu H, Liu M, Fabian M, Olson JS, Aranda R IV, Phillips G Jr., Dooley DM, and Lei B. J. Biol. Chem., 282, (43): 31380-31388, (2007)
The Coordination Chemistry of Copper-Containing Metalloproteins, D. M. Dooley, Life Chemistry Reports 5, 91-154 (1987).

Critical Commentary on: “Amidation of Bioactive Peptides: The Structure of the Peptidylglycine a -Hydroxylating Monooxygenase by Prigge, S.T., Kolhekar, A.S., Eipper, B.A., Mains, E.S., and Amzel, L.M., Science 278, 1300-1305 (1997),” McGuirl, M.A., and Dooley, D.M., ChemTracts-Inorganic Chemistry, 11, 911-917 (1998).
Coenzyme PQQ, D. M. Dooley in "McGraw-Hill Yearbook of Science and Technology, 1994" (S. P. Parker, Ed.) McGraw-Hill, New York, 85-87 (1993).

Resonance Raman Spectroscopy of Methylamine Dehydrogenase from Bacterium W3A1, W. S. McIntire, D. E. Brown, J. L. Bates and D. M. Dooley, Biochemistry 30, 125-133 (1991).

Recent Advances in the Magnetic Circular Dichroism Spectroscopy of Iron Porphyrins and Heme Proteins, J. H. Dawson and D. M. Dooley in "Iron Porphyrins, Part Three" (A. B. P. Lever and H. B. Gray, Eds.) VCH Publishers, 93-136 (1989).

Magnetic Circular Dichroism Spectroscopy of Iron Porphyrins and Hemeproteins, J. H. Dawson and D. M. Dooley in "Iron Porphyrins, Part Three" (A. B. P. Lever and H. B. Gray, Eds.) VCH Publishers, 1-87 (1989).

Azide and Fluoride Binding to E. Coli Iron Superoxide Dismutase as Studied by Solvent Nuclear Magnetic Relaxation Dispersion, D. M. Dooley, T. F. Jones, J. L. Karas, M. A. McGuirl, R. D. Brown, III and S. H. Kosnig, J. Amer. Chem. Soc. 109, 721-725 (1987).

Reactions of H 2O 2 with the Iron Containing Superoxide Dismutase from E. Coli, D. M. Dooley, J. L. Karas, T. F. Jones, S. B. Smith and C. E. Cote, Inorg. Chem. 25, 4761-4766 (1986).

Thermodynamics of Azide and Thiocyanate Binding to Bovine Copper-Zinc Super-oxide Dismutase, D. M. Dooley and M. A. McGuirl, Inorg. Chem. 25, 1261-1264 (1986).

Thermodynamics of Ligand Substitution Reactions of Tetragonal Cu(II) Sites in Proteins, D. M. Dooley, M. A. McGuirl and P. A. Mix, in "Biological and Inorganic Copper Chemistry" (J. Zubieta and K. Karlin, Eds.) Vol 1, Adenine Press, Guilderland, 97-103 (1986).

Applications of Magnetic Circular Dichroism Spectroscopy in Bioinorganic Chemistry: Copper, Rare-Earth Ions, Cobalt and Non-Heme Iron Systems, D. M. Dooley and J. H. Dawson, Coord. Chem. Rev. 60, 1-66 (1984).

Photo-oxidation of bis(maleonitriledithiolate) Complexes [M(S 2C 2(CN) 2) 2] 2 (M=Ni,Pd,Pt,Co,Cu), D. M. Dooley and B. M. Patterson, Inorg. Chem. 21, 4330-4332 (1982).

Purification and Properties of Bovine Ceruloplasmin, D. M. Dooley, C. E. Cote, T. S. Coolbaugh and P. L. Jenkins, FEBS Lett. 131, 363-365 (1981).

Coordination Environment and Fluoride Binding of Type 2 Copper in the Blue Copper Protein Ascorbate Oxidase, J. H. Dawson, D. M. Dooley and H. B. Gray, Proc. Nat. Acad. Sci. (USA) 77, 5028-5031 (1980).

Spectroscopic Studies of Ascorbate Oxidase. Electronic Structures of the Blue Copper Sites, D. M. Dooley, J. H. Dawson, P. J. Stephens, and H. B. Gray, Biochemistry 20, 2024-2028 (1981).

Spectroscopic Studies of Stellacyanin, Plastocyanin, and Azurin. Electronic Structure of Blue Copper Sites, E. I. Solomon, J. W. Hare, D. M. Dooley, J. H. Dawson, P. J. Stephens and H. B. Gray, J. Amer. Chem. Soc. 102, 168-178 (1980).

Spectroscopic Studies of Ceruloplasmin. Electronic Structures of the Copper Sites, J. H. Dawson, D. M. Dooley, P. J. Stephens and H. B. Gray, J. Amer. Chem. Soc. 101, 5046-5053 (1979).

Molecular Structure and Magnetic Properties of the Chloro Bridged Dimer, Chloro [hydrotris (1-pyrazoyl) borato] Copper (II). Observation of a Ferromagnetic Ground State, S. G .N. Foundhill, D. M. Roundhill, D. R. Bloomquist, C. Landes, R. D. Willet, D. M. Dooley and H. B. Gray, Inorg. Chem. 18, 831-835 (1979).

Spectroscopic Studies of Rhus Vernificifera and Polyporus versicolor Laccase Electronic Structures of the Copper Sites, D. M. Dooley J. Rawlings, J. H. Dawson, P. J. Stephens and H. B. Gray, J. Amer. Chem. Soc. 101, 5038-5046 (1979).

Coordination Environment and Fluoride Binding of Type 2 Copper in the Blue Copper Oxidase Ceruloplasmin, J. H. Dawson, D. M. Dooley and H. B. Gray, Proc. Nat. Acad. Sci. (USA) 75, 4078-4081 (1978).

Magnetic Susceptibility Studies of Laccase and Oxyhemocyanin, D. M. Dooley, R. A. Scott, J. Ellinghaus, E. I. Solomon and H. B. Gray, Proc. Nat. Acad. Sci. (USA) 75, 3019-3022 (1978).

Structure and Electron Transfer Reactions of Blue Copper Proteins, H. B. Gray, C. L. Coyle, D. M. Dooley, P. J. Grunthaner, J. W. Hare, R. A. Holwerda, J. V. McArdle, D. R. McMillan, J. Rawlings, R. C. Rosenberg, N. Sailasuta, E. I. Solomon, P. J. Stephens, S. Wherland and J. Qurzbach, ACS Symp. Series 162 (1977).

Sulfur 2P Photoelectron Spectrum of Limulus Oxyhemocyanin. Reply to Observations on the ESCA Spectra of Plastocyanins, J. A. Wurzbach, P. J. Grunthaner, D. M. Dooley, H. B. Gray, F. J. Grunthaner, R. R. Gay and E. I. Solomon, J. Amer. Chem. Soc. 99, 1257 (1977).

Susceptibility Studies of Laccase and Oxyhemocyanin Using an Ultrasensitive Mangetometer. Antiferromagnetic Behavior of the Type 3 Copper in Rhus Laccase, E. I. Solomon, D. M. Dooley, R. H. Wang, H. B. Gray, M. Cerdonio, F. Mogno and G. L. Romani, J. Amer. Chem. Soc. 98, 1029 (1976).