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blue copper proteins (456) 456
biochemistry & molecular biology (397) 397
blue copper protein (282) 282
crystal-structure (211) 211
chemistry, inorganic & nuclear (202) 202
models, molecular (165) 165
oxidation-reduction (160) 160
azurin - chemistry (148) 148
index medicus (148) 148
azurin (141) 141
chemistry, multidisciplinary (139) 139
proteins (133) 133
protein conformation (128) 128
copper - chemistry (126) 126
electron transport (126) 126
biophysics (124) 124
research (122) 122
binding sites (120) 120
plastocyanin (119) 119
analysis (115) 115
electron-transfer (115) 115
pseudomonas-aeruginosa azurin (108) 108
electron transfer (105) 105
kinetics (104) 104
amino acid sequence (99) 99
chemistry, physical (99) 99
electrochemistry (95) 95
molecular sequence data (95) 95
active-site (92) 92
blue-copper proteins (91) 91
poplar plastocyanin (91) 91
ligands (84) 84
metalloproteins - chemistry (84) 84
thermodynamics (82) 82
copper - metabolism (77) 77
hydrogen-ion concentration (77) 77
bacterial proteins - chemistry (76) 76
pseudomonas-aeruginosa (73) 73
copper (72) 72
azurin - metabolism (69) 69
paracoccus-denitrificans (69) 69
resolution (69) 69
nitrite reductase (66) 66
spectroscopy (65) 65
cytochrome-c (64) 64
chemical properties (62) 62
angstrom resolution (61) 61
electronic-structure (60) 60
metalloproteins (59) 59
azurin - genetics (57) 57
electron spin resonance spectroscopy (56) 56
electron-transfer reactions (56) 56
escherichia-coli (54) 54
crystallography, x-ray (53) 53
plastocyanin - chemistry (52) 52
spinach plastocyanin (52) 52
microbiology (51) 51
blue copper (50) 50
chemistry (49) 49
bacterial proteins - metabolism (48) 48
site (47) 47
physics, atomic, molecular & chemical (46) 46
cytochrome c (45) 45
oxidation (45) 45
site-directed mutagenesis (45) 45
alcaligenes-denitrificans (43) 43
rusticyanin (43) 43
structure (43) 43
azurin - analogs & derivatives (42) 42
mutagenesis, site-directed (42) 42
reduction (42) 42
usage (42) 42
cell biology (41) 41
crystal-structure analysis (41) 41
methylamine dehydrogenase (41) 41
amicyanin (40) 40
article (40) 40
laccase (40) 40
crystallography (39) 39
electrons (39) 39
stellacyanin (39) 39
complexes (38) 38
life sciences (38) 38
purification (38) 38
spectrophotometry (38) 38
thiobacillus-ferrooxidans (38) 38
alcaligenes-faecalis s-6 (37) 37
cytochrome-c-oxidase (37) 37
nuclear-magnetic-resonance (37) 37
reorganization energy (37) 37
density-functional theory (36) 36
protein binding (36) 36
amino-acid-sequence (35) 35
biochemical research methods (35) 35
models, chemical (34) 34
bacterial proteins - genetics (33) 33
metalloproteins - metabolism (33) 33
plant proteins - chemistry (33) 33
protein (33) 33
base sequence (32) 32
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Journal Article
01/1970, ISBN 0471649627, 68
This chapter contains sections titled: Introduction The Coordination Chemistry and Spectroscopic Properties of the Common Ions of Copper The Forms of Copper in... 
“epr‐nondetectable” copper | “blue” & “nonblue” cupric ions | coordination chemistry | “blue” copper‐containing oxidases | spectroscopic properties
Book Chapter
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/1974, Volume 71, Issue 12, pp. 4684 - 4687
The intrinsic fluorescence of laccase (p-diphenol:O oxidoreductase, EC 1.10.3.2), emitted by its tyrosinyl and tryptophanyl residues, underwent significant... 
Enzymes | Oxygen | Wavelengths | Emission spectra | Fluorescence | Titration | Wave excitation | Copper | Rapid quenching | Energy transfer
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/1974, Volume 71, Issue 4, pp. 1339 - 1341
Journal Article
Bioinorganic Chemistry, ISSN 0006-3061, 1974, Volume 4, Issue 1, pp. 79 - 91
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/1974, Volume 71, Issue 12, pp. 4684 - 4687
The intrinsic fluorescence of laccase ( p -diphenol:O 2 oxidoreductase, EC 1.10.3.2), emitted by its tyrosinyl and tryptophanyl residues, underwent significant... 
Fluorescence | Spectrometry, Fluorescence | Protein Conformation | Oxidation-Reduction | Copper | Catechol Oxidase - metabolism | redox-related quenching | Biological Sciences | Biochemistry | “blue” copper proteins
Journal Article
BBA - Enzymology, ISSN 0005-2744, 06/1979, Volume 568, Issue 2, pp. 307 - 320
Stopped-flow kinetic studies of the anaerobic reduction of Rhus vernicifera laccase (monophenol, dihydroxyphenylalanine:oxygen oxidoreductase, EC 1.14.18.1)... 
Hydroquinone | Laccase blue copper | Electron transfer
Journal Article
FEBS Letters, ISSN 0014-5793, 1982, Volume 147, Issue 2, pp. 220 - 224
Absorption, circular dichroism, electron spin resonance and resonance Raman spectra of a blue copper protein, plantacyanin from cucumber peel have been... 
Plantacyanin | Circular dichroism spectrum | Redox potential | Amino acid analysis | Resonance Raman spectrum | Blue copper protein
Journal Article
Chemical and Pharmaceutical Bulletin, ISSN 0009-2363, 1983, Volume 31, Issue 1, pp. 337 - 340
Dihydrogeodin oxidase (DHGO), an enzyme catalyzing regio- and stereo-specific intramolecular phenol oxidative coupling reaction of dihydrogeodin to give... 
Aspergillus terreus | phenol oxidative coupling | (+)-geodin | blue copper | dihydrogeodin | protein
Journal Article
FEBS Letters, ISSN 0014-5793, 1984, Volume 171, Issue 2, pp. 257 - 261
Which cysteine of apostellacyanine reacts with 4‐vinylpyridine in 6 M guanidine—HCl depends upon the pH. We infer that a disulfide switch occurs at higher pH... 
Blue copper | Stellacyanin | Cysteine | Switching | Disulfide | Sequence homology | Disulfides - analysis | Amino Acid Sequence | Plant Proteins - analysis | Cysteine - analysis | Metalloproteins - analysis
Journal Article
YAKUGAKU ZASSHI, ISSN 0031-6903, 1985, Volume 105, Issue 3, pp. 199 - 209
Biometallochromophores are involve in some fundamental biological processes such as electron strage and transfer (Fe, Cu), dioxygen binding and activation (Mn,... 
bleomycin | ferredoxin | DNA cleavage | blue copper protein | Mn (III)-containing acid phosphatase | glutathione-Cu (II) complex | phytosiderophore | biometallochromophore
Journal Article
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology, ISSN 0167-4838, 1985, Volume 827, Issue 3, pp. 320 - 326
A soluble copper-containing protein with p-phenylenediamine oxidase activity was purified from Nitrosomonas europaea by flat-bed isoelectric focusing and... 
Copper protein | ESR | N. europaea | Blue copper oxidase
Journal Article
FEBS Letters, ISSN 0014-5793, 1986, Volume 197, Issue 1, pp. 301 - 304
Journal Article
Journal of Bacteriology, ISSN 0021-9193, 01/1987, Volume 169, Issue 12, pp. 5648 - 5652
The gene encoding a blue copper protein (a member of the pseudoazurins) of 123 amino acid residues, containing a single type I Cu super(2+) ion, was cloned... 
nucleotide sequence | amino acid sequence | genes | Alcaligenes faecalis | blue copper protein | cloning | gene expression
Journal Article
Plant and cell physiology, ISSN 0032-0781, 07/1987, Volume 28, Issue 5, pp. 825 - 831
Plastocyanin obtained from an aquatic higher plant, Brazilian elodea, was characterized by electronic absorption, CD, and EPR spectroscopy. The blue copper... 
Aquatic higher plant | Plastocyanin | Copper protein | Brazilian elodea | Egeria densa | Blue copper protein | PLANT SCIENCES | CELL BIOLOGY
Journal Article
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology, ISSN 0167-4838, 1987, Volume 912, Issue 3, pp. 329 - 337
Blue and non-blue states of the copper center in copper-substituted alcohol dehydrogenase (EC 1.1.1.1) can be attained by coenzyme binding and / or ligand... 
Charge transfer spectra | Copper centre | Alcohol dehydrogenase | ESR | Horse liver | Blue copper protein
Journal Article
Zeitschrift fur Naturforschung - Section C Journal of Biosciences, ISSN 0939-5075, 12/1987, Volume 42, Issue 11-12, pp. 1358 - 1360
Journal Article
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