Multicopper oxidases and oxygenases

Electron transfers in chemistry and biology

Marcus, R. A., & Sutin, N. (1985) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(85)90014-x · Cited by 8,032 · see citing works

Structural and Functional Aspects of Metal Sites in Biology

Holm, R. H., Kennepohl, P., & Solomon, E. I. (1996) · Chemical Reviews · doi:10.1021/cr9500390 · Cited by 2,536 · see citing works

The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å

Tomitake Tsukihara, A., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa‐Itoh, K., Nakashima, R., Yaono, R., & Yoshikawa, S. (1996) · Science · doi:10.1126/science.272.5265.1136 · Cited by 2,102 · see citing works

Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans

Iwata, S., Ostermeier, C., Ludwig, B., & Michel, H. (1995) · Nature · doi:10.1038/376660a0 · Cited by 2,006 · see citing works

The structure and function of fungal laccases

Thurston, C. F. (1994) · Microbiology · doi:10.1099/13500872-140-1-19 · Cited by 1,941 · see citing works

Structures of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 Å

Tomitake Tsukihara, A., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa‐Itoh, K., Nakashima, R., Yaono, R., & Yoshikawa, S. (1995) · Science · doi:10.1126/science.7652554 · Cited by 1,415 · see citing works

Oxidation of non‐phenolic substrates

Bourbonnais, R., & Paice, M. G. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80298-w · Cited by 1,346 · see citing works

Polyphenol oxidases in plants

Mayer, A. M., & Harel, E. (1979) · Phytochemistry · doi:10.1016/0031-9422(79)80057-6 · Cited by 1,259 · see citing works

Iron and infection

Weinberg, E. D. (1978) · Microbiological Reviews · doi:10.1128/mmbr.42.1.45-66.1978 · Cited by 1,254 · see citing works

Heme/Copper Terminal Oxidases

Ferguson-Miller, S. M., & Babcock, Ǵ. (1996) · Chemical Reviews · doi:10.1021/cr950051s · Cited by 1,161 · see citing works

Oxygen activation and the conservation of energy in cell respiration

Babcock, Ǵ., & Wikström, M. K. F. (1992) · Nature · doi:10.1038/356301a0 · Cited by 1,126 · see citing works

X-ray absorption edge determination of the oxidation state and coordination number of copper. Application to the type 3 site in Rhus vernicifera laccase and its reaction with oxygen

Kau, L. S., Spira, D. J., Penner‐Hahn, J. E., Hodgson, K. O., & Solomon, E. I. (1987) · Journal of the American Chemical Society · doi:10.1021/ja00255a032 · Cited by 1,048 · see citing works

Electronic structures of active sites in copper proteins: contributions to reactivity

Solomon, E. I., Baldwin, M. J., & Lowery, M. D. (1992) · Chemical Reviews · doi:10.1021/cr00012a003 · Cited by 896 · see citing works

Copper-Dioxygen Complexes. Inorganic and Bioinorganic Perspectives

Kitajima, N., & Moro‐oka, Y. (1994) · Chemical Reviews · doi:10.1021/cr00027a010 · Cited by 876 · see citing works

Mechanisms Whereby Mononuclear Copper Proteins Functionalize Organic Substrates

Klinman, J. P. (1996) · Chemical Reviews · doi:10.1021/cr950047g · Cited by 840 · see citing works

Novel thioether bond revealed by a 1.7 Å crystal structure of galactose oxidase

Ito, N., Phillips, S. E. V., Stevens, C., Ogel, Z. B., McPherson, M. J., Keen, J. N., Yadav, K. D. S., & Knowles, P. F. (1991) · Nature · doi:10.1038/350087a0 · Cited by 763 · see citing works

Oxidation of Phenols, Anilines, and Benzenethiols by Fungal Laccases: Correlation between Activity and Redox Potentials as Well as Halide Inhibition

Xu, F. (1996) · Biochemistry · doi:10.1021/bi952971a · Cited by 730 · see citing works

A permease-oxidase complex involved in high-affinity iron uptake in yeast.

Stearman, R., Yuan, D. S., Yamaguchi-Iwai, Y., Klausner, R. D., & Dancis, A. (1996) · Science · doi:10.1126/science.271.5255.1552 · Cited by 683 · see citing works

The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.

Osaki, S., Johnson, D. A., & Frieden, E. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96527-0 · Cited by 679 · see citing works

The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.

Askwith, C., Eide, D., Van Ho, A., Bernard, P. S., Li, L., Davis-Kaplan, S., Sipe, D. M., & Kaplan, J. (1994) · Cell · doi:10.1016/0092-8674(94)90346-8 · Cited by 670 · see citing works

A new model for dioxygen binding in hemocyanin. Synthesis, characterization, and molecular structure of the .mu.-.eta.2:.eta.2 peroxo dinuclear copper(II) complexes, [Cu(HB(3,5-R2pz)3)]2(O2) (R = isopropyl and Ph)

Kitajima, N., Fujisawa, K., Fujimoto, C., Moro‐oka, Y., Hashimoto, S., Kitagawa, T., Toriumi, K., Tatsumi, K., & Nakamura, A. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00030a025 · Cited by 640 · see citing works

Encyclopedia of inorganic chemistry

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Reversible Cleavage and Formation of the Dioxygen O-O Bond Within a Dicopper Complex

Halfen, J. A., Mahapatra, S., Wilkinson, E. C., Kaderli, S., Young, V. G., QUE, L. J., Zuberbühler, A. D., & Tolman, W. B. (1996) · Science · doi:10.1126/science.271.5254.1397 · Cited by 545 · see citing works

Microbial growth on C[1] compounds

Murrell, J. C., & Kelly, D. P. (1993) · Intercept eBooks · Cited by 497 · see citing works

Ligand substitution processes

Jørgensen, C. K. (1966) · Journal of the Franklin Institute · doi:10.1016/0016-0032(66)90569-2 · Cited by 472 · see citing works

Refined crystal structure of ascorbate oxidase at 1.9 Å resolution

Messerschmidt, A., Ladenstein, R., Huber, R., Bolognesi, M., Avigliano, L., Petruzzelli, R., Rossi, A., & Finazzi‐Agrò, A. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90583-6 · Cited by 471 · see citing works

Physicochemical and Kinetic Properties of Mushroom Tyrosinase

Duckworth, H. W., & Coleman, J. E. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77137-3 · Cited by 468 · see citing works

Bioinorganic chemistry of copper

(1994) · International Journal of Biochemistry · doi:10.1016/0020-711x(94)90038-8 · Cited by 458 · see citing works

The biochemistry of methylotrophs

Reeve, J. N. (1983) · Trends in biotechnology · doi:10.1016/0167-7799(83)90026-4 · Cited by 448 · see citing works

Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus.

Kwon, B. S., Haq, A. K., Pomerantz, S. H., & Halaban, R. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.21.7473 · Cited by 438 · see citing works

The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin Modelling and structural relationships

Messerschmidt, A., & Huber, R. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15311.x · Cited by 438 · see citing works

The determination of structural properties of dimeric transition metal ion complexes from epr spectra

SMITH, T. D., & Pilbrow, J. R. (1974) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(00)80255-6 · Cited by 428 · see citing works

X-ray crystal structure of the blue oxidase ascorbate oxidase from Zucchini

Messerschmidt, A., Rossi, A., Ladenstein, R., Huber, R., Bolognesi, M., Gatti, G., Marchesini, A., Petruzzelli, R., & Finazzi‐Agrò, A. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90498-1 · Cited by 423 · see citing works

Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences

Magnus, K. A., Hazes, B., Ton‐That, H., Bonaventura, C., Bonaventura, J., & Hol, W. G. J. (1994) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340190405 · Cited by 398 · see citing works

A Laccase Associated with Lignification in Loblolly Pine Xylem

Bao, W., O'Malley, D. M., Whetten, R. W., & Sederoff, R. R. (1993) · Science · doi:10.1126/science.260.5108.672 · Cited by 395 · see citing works

Reactions of cytochrome oxidase with oxygen and carbon monoxide

GIBSON, Q., & Greenwood, C. (1963) · Biochemical Journal · doi:10.1042/bj0860541 · Cited by 391 · see citing works

.mu.-.eta.2:.eta.2-Peroxo binuclear copper complex, [Cu(HB(3,5-(Me2CH)2pz)3)]2(O2)

Kitajima, N., Fujisawa, K., Moro‐oka, Y., & Toriumi, K. (1989) · Journal of the American Chemical Society · doi:10.1021/ja00206a062 · Cited by 388 · see citing works

Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution

Volbeda, A., & Hol, W. G. J. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90276-3 · Cited by 377 · see citing works

Protein Control of Redox Potentials of Iron−Sulfur Proteins

Stephens, P. J., Jollie, D. R., & Warshel, A. (1996) · Chemical Reviews · doi:10.1021/cr950045w · Cited by 372 · see citing works

Functional intermediates in the reaction of membrane-bound cytochrome oxidase with oxygen.

Chance, B., Saronio, C., & Leigh, J. S. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40634-0 · Cited by 369 · see citing works

The role of ceruloplasmin in iron metabolism.

Roeser, H. P., Lee, G. R., Nacht, S., & Cartwright, G. E. (1970) · Journal of Clinical Investigation · doi:10.1172/jci106460 · Cited by 365 · see citing works

The Tyrosine Hydroxylase Activity of Mammalian Tyrosinase

Pomerantz, S. H. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96973-5 · Cited by 359 · see citing works

The X-ray structure of human serum ceruloplasmin at 3.1 Å: nature of the copper centres

Zaitseva, I., Zaitsev, V., Card, G. L., Ka, M., Bax, B. D., Ralph, A. C., & Lindley, P. F. (1996) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050018 · Cited by 355 · see citing works

Crystal Structure of a Free Radical Enzyme, Galactose Oxidase

Ito, N., Phillips, S. E. V., Yadav, K. D. S., & Knowles, P. F. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1335 · Cited by 354 · see citing works

Lignification in Trees: Indication of Exclusive Peroxidase Participation

Harkin, J. M., & Obst, J. R. (1973) · Science · doi:10.1126/science.180.4083.296 · Cited by 352 · see citing works

Synthetic models for binuclear copper proteins

Sorrell, T. N. (1989) · Tetrahedron · doi:10.1016/0040-4020(89)80033-x · Cited by 335 · see citing works

Physiology of the insect epidermis

Binnington, K. C., & Retnakara, A. (1991) · Cited by 333 · see citing works

Copper-mediated hydroxylation of an arene: model system for the action of copper monooxygenases. Structures of a binuclear copper(I) complex and its oxygenated product

Karlin, K. D., Hayes, J. C., Gultneh, Y., Cruse, R. W., McKown, J. W., Hutchinson, J. P., & Zubieta, J. A. (1984) · Journal of the American Chemical Society · doi:10.1021/ja00319a036 · Cited by 322 · see citing works

OXYGEN TRANSFER AND ELECTRON TRANSPORT BY THE PHENOLASE COMPLEX1

Mason, H. S., Fowlks, W. L., & Peterson, E. R. (1955) · Journal of the American Chemical Society · doi:10.1021/ja01615a088 · Cited by 313 · see citing works

The importance of phenol oxidase activity in lignin degradation by the white-rot fungus Sporotrichum pulverulentum

Ander, P., & Eriksson, K. (1976) · Archives of Microbiology · doi:10.1007/bf00425105 · Cited by 312 · see citing works

Bioinorganic Chemistry of Copper

Karlin, K. D., & Tyeklár, Z. (1993) · Springer eBooks · doi:10.1007/978-94-011-6875-5 · Cited by 312 · see citing works

Substrate analog binding to the coupled binuclear copper active site in tyrosinase

Wilcox, D. E., Porras, A. G., Hwang, Y. T., Lerch, K., Winkler, M. E., & Solomon, E. I. (1985) · Journal of the American Chemical Society · doi:10.1021/ja00299a043 · Cited by 312 · see citing works

Crystal structure of deoxygenated limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation

Hazes, B., Kalk, K. H., Hol, W. G. J., Magnus, K. A., Bonaventura, C., Bonaventura, J., & Dauter, Z. (1993) · Protein Science · doi:10.1002/pro.5560020411 · Cited by 309 · see citing works

Genetic Evidence that Ferric Reductase Is Required for Iron Uptake in Saccharomyces cerevisiae

Dancis, A., Klausner, R. D., Hinnebusch, A. G., & Barriocanal, J. G. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.5.2294-2301.1990 · Cited by 305 · see citing works

Oxidation-reduction potentials of the electron acceptors in laccases and stellacyanin

Reinhammar, B. (1972) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(72)90045-x · Cited by 299 · see citing works

Polyphenol oxidase inAzospirillum lipoferumisolated from rice rhizosphere: Evidence for laccase activity in non-motile strains ofAzospirillum lipoferum

Givaudan, A., Effosse, A., Faure, D., Potier, P., Bouillant, M. L., & Bally, R. (1993) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1993.tb06100.x · Cited by 298 · see citing works

Spectroscopy of Binuclear Dioxygen Complexes

Solomon, E. I., Tuczek, F., Root, D. E., & Brown, C. A. (1994) · Chemical Reviews · doi:10.1021/cr00027a013 · Cited by 298 · see citing works

X-ray absorption spectroscopic studies of the blue copper site: metal and ligand K-edge studies to probe the origin of the EPR hyperfine splitting in plastocyanin

Shadle, S. E., Penner‐Hahn, J. E., Schugar, H. J., Hedman, B., Hodgson, K. O., & Solomon, E. I. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00055a057 · Cited by 297 · see citing works

Laccase from Sycamore Maple (Acer pseudoplatanus) Polymerizes Monolignols

Sterjiades, R., Dean, J. F. D., & Eriksson, K. L. (1992) · PLANT PHYSIOLOGY · doi:10.1104/pp.99.3.1162 · Cited by 296 · see citing works

Laccase-mediated detoxification of phenolic compounds

Bollag, J., Shuttleworth, K. L., & Anderson, D. (1988) · Applied and Environmental Microbiology · doi:10.1128/aem.54.12.3086-3091.1988 · Cited by 293 · see citing works

Enzymatic Browning and Its Prevention

Lee, C. Y., & Whitaker, J. R. (1995) · ACS symposium series · doi:10.1021/bk-1995-0600 · Cited by 289 · see citing works

Sequence of the gene coding for ammonia monooxygenase in Nitrosomonas europaea

McTavish, H., Fuchs, J. A., & Hooper, A. B. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.8.2436-2444.1993 · Cited by 289 · see citing works

Large Scale Production and Purification of Laccase from Cultures of the Fungus Polyporus versicolor and some Properties of Laccase A.

Fåhræus, G., Reinhammar, B., Ferm, R., Hemmingsson, S., Kullberg, L., Blinc, R., Paušak, S., Ehrenberg, L. G., & Dumanovic, J. (1967) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.21-2367 · Cited by 288 · see citing works

Purification and properties of laccase and stellacyanin from Rhus vernicifera

Reinhammar, B. (1970) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(70)90059-9 · Cited by 277 · see citing works

Studies of the heme components of cytochrome c oxidase by EPR spectroscopy

GELDER, B. F. V., & Beinert, H. (1969) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(69)90219-9 · Cited by 273 · see citing works

Electronic structure of plastocyanin: excited state spectral features

Gewirth, A. A., & Solomon, E. I. (1988) · Journal of the American Chemical Society · doi:10.1021/ja00220a015 · Cited by 261 · see citing works

Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)

Zahn, J. A., & DiSpirito, A. A. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.4.1018-1029.1996 · Cited by 259 · see citing works

Substrate Specificities of the Soluble and Particulate Methane Mono-oxygenases of Methylosinus trichosporium OB3b

Burrows, K. J., Cornish, A., Scott, D., & Higgins, I. J. (1984) · Microbiology · doi:10.1099/00221287-130-12-3327 · Cited by 252 · see citing works

The FET3 Gene Product Required for High Affinity Iron Transport in Yeast Is a Cell Surface Ferroxidase

Silva, D. M. D., Askwith, C. C., Eide, D. J., & Kaplan, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.3.1098 · Cited by 246 · see citing works

Particulate methane monooxygenase genes in methanotrophs

Semrau, J. D., CHISTOSERDOV, A. Y., Lebrón, J. A., Costello, A. M., Davagnino, J., Kenna, E. M., Holmes, A. J., Finch, R., Murrell, J. C., & Lidstrom, M. E. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.11.3071-3079.1995 · Cited by 242 · see citing works

Suicidal inactivation and labelling of ammonia mono-oxygenase by acetylene

Hyman, M. R., & Wood, P. M. (1985) · Biochemical Journal · doi:10.1042/bj2270719 · Cited by 236 · see citing works

Electronic structure and bonding of the blue copper site in plastocyanin

Penfield, K., Gewirth, A. A., & Solomon, E. I. (1985) · Journal of the American Chemical Society · doi:10.1021/ja00301a024 · Cited by 234 · see citing works

Analysis of a kinetic model for melanin biosynthesis pathway.

Rodríguez‐López, J. N., Tudela, J., Varón, R., García‐Carmona, F., & Garcı́a-Cánovas, F. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50597-x · Cited by 229 · see citing works

Chemical and spectroscopic studies of the binuclear copper active site of Neurospora tyrosinase: comparison to hemocyanins

Himmelwright, R. S., Eickman, N. C., LuBien, C. D., Solomon, E. I., & Lerch, K. (1980) · Journal of the American Chemical Society · doi:10.1021/ja00544a031 · Cited by 226 · see citing works

Interaction of Ammonia Monooxygenase from Nitrosomonas europaea with Alkanes, Alkenes, and Alkynes

Hyman, M. R., Murton, I. B., & Arp, D. J. (1988) · Applied and Environmental Microbiology · doi:10.1128/aem.54.12.3187-3190.1988 · Cited by 225 · see citing works

Degradation mechanisms of phenolic β-1 lignin substructure model compounds by laccase of Coriolus versicolor

Kawai, S., Umezawa, T., & Higuchi, T. (1988) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(88)90172-5 · Cited by 224 · see citing works

Oxidases and Related Redox Systems

Guiseppi-Eile, A. (1989) · Journal of the American College of Toxicology · doi:10.3109/10915818909018066 · Cited by 223 · see citing works

X-ray Structures and Mechanistic Implications of Three Functional Derivatives of Ascorbate Oxidase from Zucchini

Messerschmidt, A., Luecke, H., & Huber, R. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1215 · Cited by 221 · see citing works

Oxytyrosinase

Jolley, R. L., Evans, L. H., Makino, N., & Mason, H. S. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43035-4 · Cited by 219 · see citing works

The role of of laccase in lignification

O'Malley, D. M., Whetten, R. W., Bao, W., Chen, C.-L., & Sederoff, R. R. (1993) · The Plant Journal · doi:10.1046/j.1365-313x.1993.04050751.x · Cited by 217 · see citing works

The active site of galactose oxidase.

Whittaker, M. M., & Whittaker, J. W. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68751-4 · Cited by 216 · see citing works

Spectroscopic and Theoretical Description of the Electronic Structure of S = 3/2 Iron-Nitrosyl Complexes and Their Relation to O2 Activation by Non-Heme Iron Enzyme Active Sites

Brown, C. A., Pavlosky, M. A., Westre, T. E., Zhang, Y., Hedman, B., Hodgson, K. O., & Solomon, E. I. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00107a015 · Cited by 216 · see citing works

Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule.

Takahashi, N., Ortel, T. L., & Putnam, F. W. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.2.390 · Cited by 210 · see citing works

14C2H2- and 14CO2-labeling studies of the de novo synthesis of polypeptides by Nitrosomonas europaea during recovery from acetylene and light inactivation of ammonia monooxygenase.

Hyman, M. R., & Arp, D. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45979-0 · Cited by 202 · see citing works

The Effect of Copper Ions on Membrane Content and Methane Monooxygenase Activity in Methanol-grown Cells of Methylococcus capsulatus (Bath)

PRIOR, S. D., & Dalton, H. (1985) · Microbiology · doi:10.1099/00221287-131-1-155 · Cited by 199 · see citing works

Biological Applications of Electron Spin Resonance

Dodd, N. J. F. (1973) · International Journal of Radiation Biology and Related Studies in Physics Chemistry and Medicine · doi:10.1080/09553007314550901 · Cited by 197 · see citing works

Phenoxazinone synthase: mechanism for the formation of the phenoxazinone chromophore of actinomycin

Barry, C. E., Nayar, P. G., & Begley, T. P. (1989) · Biochemistry · doi:10.1021/bi00441a026 · Cited by 197 · see citing works

Purification and Characterization of a Tyrosinase from Streptomyces glaucescens

Lerch, K., & Ettlinger, L. (1972) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1972.tb02549.x · Cited by 193 · see citing works

In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by copper

Ensign, S. A., Hyman, M. R., & Arp, D. J. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.7.1971-1980.1993 · Cited by 192 · see citing works

Extracellular laccases and peroxidases from sycamore maple (Acer pseudoplatanus) cell-suspension cultures

Sterjiades, R., Dean, J. F. D., Gamble, G. R., Himmelsbach, D. S., & Eriksson, K. (1993) · Planta · doi:10.1007/bf00195678 · Cited by 190 · see citing works

The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath).

Nguyen, H., Shiemke, A. K., Jacobs, S. J., Hales, B. J., Lidstrom, M. E., & Chan, S. I. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36565-1 · Cited by 189 · see citing works

Characterization of two allelic forms of Neurospora crassa laccase. Amino- and carboxyl-terminal processing of a precursor.

Germann, U. A., Müller, G., Hunziker, P., & Lerch, K. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)35436-5 · Cited by 188 · see citing works

Laccase and the Deposition of Lignin in Vascular Plants

Dean, J. F. D., & Eriksson, K. L. (1994) · Holzforschung · doi:10.1515/hfsg.1994.48.s1.21 · Cited by 184 · see citing works

A comparative EPR investigation of the multicopper proteins nitrous‐oxide reductase and cytochrome c oxidase

Antholine, W. E., Kastrau, D. H. W., Steffens, G. C. M., Gerhard, B. U. S. E., Zumft, W. G., & Kroneck, P. M. H. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17360.x · Cited by 183 · see citing works

A resonance Raman study of the copper protein, hemocyanin. New evidence for the structure of the oxygen-binding site

Freedman, T. B., Loehr, J. S., & Loehr, T. M. (1976) · Journal of the American Chemical Society · doi:10.1021/ja00426a023 · Cited by 178 · see citing works

Electronic state of heme in cytochrome oxidase III. The magnetic susceptibility of beef heart cytochrome oxidase and some of its derivatives from 7-200 K. Direct evidence for an antiferromagnetically coupled Fe (III)/Cu (II) pair.

Tweedle, M. F., & Wilson, L. J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34362-4 · Cited by 177 · see citing works

Absence of Laccase from Yellow-spored Mutants of Aspergillus nidulans

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Mononuclear Cu–O2 Complexes: Geometries, Spectroscopic Properties, Electronic Structures, and Reactivity

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Lignin Biodegradation with Laccase-Mediator Systems

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Enzymatic Oxidation of Methane

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Recent advances in copper-catalyzed oxidation of organic compounds

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Respiratory Transformation of Nitrous Oxide (N2O) to Dinitrogen by Bacteria and Archaea

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Electrocatalytic Oxygen Reduction to Hydrogen Peroxide: From Homogeneous to Heterogeneous Electrocatalysis

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O2Reduction in Enzymatic Biofuel Cells

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Spectroscopic and Thermodynamic Properties, and Reaction Mechanism of Multicopper Oxidases

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Heme/Copper Terminal Oxidases

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A structural model for type 3 copper in multicopper oxidases

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Catalytic Cycle of Multicopper Oxidases Studied by Combined Quantum- and Molecular-Mechanical Free-Energy Perturbation Methods

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Copper Proteins: Oxidases

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