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contains 0.5 mol of copper per mol of enzyme
-
monomeric units contains two atoms
-
enzyme shows a copper-to-protein ratio of 1.08
-
enzyme shows a copper-to-protein ratio of 1.08
-
copper content: 1.2 mol of Cu per mol of wild-type enzyme, 0.96 mol of Cu per mol of mutant enzyme W290F, 1 mol Cu per mol of mutant enzyme W290G, 1.3 mol of Cu per mol of mutant enzyme W290H
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galactose oxidase is a copper-dependent enzyme that accomplishes 2e- substrate oxidation by pairing a single copper with an unusual cysteinylated tyrosine (Cys-Tyr) redox cofactor. The active site of GO contains only a single Cu . Post-translational biogenesis of Cys-Tyr is copper- and O2-dependent, resulting in a self-processing enzyme system. Cu(I) and Cu(II) enzyme states, Cu(I) active site modeling: on model uses the crystal structure of apo pre-processed GO (PDB ID 2VZ1) with Cu(I) manually added as the starting structure, while the other uses the crystal structure of processed Cu(II)-GO (PDB ID 1GOF) with the Cys-Tyr crosslink manually removed. In both cases, the model includes Cys228, Tyr272, Tyr495, His496 and His581 residues. Cu(I) activation mechanism, overview
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a copper-containing enzyme with a dinuclear copper centre
-
the copper centers in the protein are directly involved in the catechol oxidation
-
10 mM increase activity by 17%, 0.1 mM increase activity by 100%
-
16 gatom per mol, laccase I, 4 gatom per mol, laccases II, III, study of copper centers
-
3.3 mol copper per mol of protein, type I copper
-
4 atoms per protein molecule, a type I CuII, a type II CuII and a type III binuclear CuII
-
50% of copper is paramagnetic, type 1 Cu2+ and type 2 Cu2+
-
a blue copper-containing oxidoreductase
-
chemical and spectral studies of binuclear copper site
-
contains 4 copper atoms per protein molecule
-
contains six copper atoms per polypeptide chain and displays optical and electron paramagnetic resonance spectra consistent with the presence of type 1, type 2, and type 3 copper centers. The addition of copper leads to immediate and reversible changes in the optical and electron paramagnetic resonance spectra of the protein, as well as decreased thermal stability of the enzyme and stimulates both the phenoloxidase and ferroxidase activities
-
copper content of recombinant CotA laccase from Bacillus subtilis produced by Escherichia coli cells is shown to be strongly dependent on the presence of copper and oxygen in the culture media. In copper-supplemented media, a switch from aerobic to microaerobic conditions leads to the synthesis of a recombinant holoenzyme, while the maintenance of aerobic conditions results in the synthesis of a copper-depleted population of proteins. Strikingly, cells grown under microaerobic conditions accumulate up to 80fold more copper than aerobically grown cells. In vitro copper incorporation into apoenzymes is monitored by optical and electron paramagnetic resonance spectroscopy. This analysis reveals that copper incorporation into CotA laccase is a sequential process, with the type 1 copper center being the first to be reconstituted, followed by the type 2 and the type 3 copper centers
-
copper multi-copper oxidase
-
copper-containing enzyme
-
electron paramagnetic resonance studies
-
ENDOR (i.e. electron nuclear double resonance) studies
-
four copper atoms per molecule, spectroscopic properties are typical of blue copper oxidase. Presence of copper is essential for CueO-dependent oxidation of 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) and p-phenylenediamine
-
low copper occupancy in apo-CueO and slow copper reconstitution process in CueO with exogenous copper are demonstrated. These observations well explain the copper dependence of CueO oxidase activity
-
mechanism of copper incorporation in CueO is sequential, with type 1 copper being the first to be reconstituted, followed by type 2 and type 3 sites. The copper content of the purified protein is routinely 0.5-0.6 Cu atoms/protein molecule
-
multi-copper containing oxidase
-
multicopper oxidase. The apoenzyme is inactive. Incubation with CuSO4 allows a 43fold increase of the specific activity yielding a metallo-enzyme
-
preparation of Cu-depleted enzyme
-
preparation of type II-depleted enzyme
-
temperature dependence of reduction potential
-
the affinity of site T4 for CuII shows a KD of 0.0055 microM
-
the enzyme is denatured in the presence of a number of denaturing agents and refolded back to functional state with copper. In the folding experiments under alkaline conditions, zinc can replace copper in restoring 100% of laccase activity indicating the non-essential role of copper in this laccase
-
the enzyme is modified posttranslationally, including removal of 31 amino acid residues from its N terminus, addition of glycan residues (glycosylation), and apparent coordination of four copper atoms into three types of copper-binding sites
-
trinuclear and mononuclear copper center
-
two paramagnetic copper centers per protein molecule
-
Type I and type II copper center
-
X-ray absorption edge study of type I, type II and binuclear type III copper center
-
X-ray absorption spectra, possible copper-copper interaction
-
10 copper atoms per enzyme molecule
-
10-12 atoms of copper per enzyme molecule of 140000 Da
-
4 copper atoms per subunit, mononuclear blue copper in domain 3 and trinuclear copper between domain 1 and 3
-
8 atoms of copper per enzyme molecule of 132000 Da
-
8 atoms of copper per enzyme molecule of 140000 Da
-
a multicopper protein, 6 atoms of copper per enzyme molecule
-
coordination environment of type 2 copper
-
each subunit has 4 copper atoms bound as mononuclear and trinuclear species, mononuclear copper representing the type I copper is located in the 3 domain
-
electronic structure of blue copper sites
-
enzyme contains a set of 1 type I, 1 type II and a pair of type III copper ions at its active site
-
enzyme contains type I, type II and type III copper atoms in the ratio 1/2/2, 4 copper atoms/enzyme
-
evidence that the coordination environment and electronic structure of the type 1 copper is similar to those of plastocyanin and azurin
-
measurement of intramolecular electron transfer between type I and type III copper centers in the multi-copper enzyme
-
native enzyme contains two type 1, two type 2 and four type 3 copper ions
-
principal active site comprised of one type I, one type II and a pair of type III coppers
-
the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate
-
type 2 copper may be part of the ascorbate binding site
-
type I and trinuclear type II copper center
-
1.2 mol per mol protein
-
1 atom of Cu per molecule of enzyme
-
single Cu(II) ion in active site
-
1-1.6 mol per mol enzyme, nonblue type 2 Cu2+ protein
-
contains 0.9 copper atoms per protein
-
probably belongs to the nonblue class, two atoms per molecule of enzyme
-
0.4 atoms of Fe per 89000 Da enzyme. Removal of copper does not correlate with loss of activity
-
variable amounts of copper: 0.2-0.5 mol per mol of enzyme
-
contains 0.048 mol of Cu per mol of enzyme
-
0.33 mol per mol of enzyme
-
contains 2 gatom of copper per mol of enzyme
-
contains copper in significant quantity
-
enzyme contains 2 copper moieties
-
only trace amounts of copper
-
ratio of copper to heme is less than 0.03
-
copper content is 0.12 atoms per monomer
-
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview
-
0.03 atoms per 42000 g/mol peptide
-
1 mol of Cu2+ per mol of enzyme
-
copper does not support enzyme activity and can be removed by dithiothreitol
-
electron paramagnetic resonance spectroscopy indicates a type II copper-containing enzyme
-
less than 0.01 copper atoms per 50000 Da subunit
-
copper type II ascorbate-dependent monooxygenase with two Cu2_monooxygen domains
-
the enzyme acquires its essential Cu cofactor from copper-transporting ATPase alpha (ATP7A). Dopamine-beta-hydroxylase (DBH)-containing neurons express both ATP7A and copper-transporting ATPase beta (ATP7B). The two transporters are located in distinct cellular compartments and oppositely regulate the export of soluble DBH from cultured neuronal cells under resting conditions. Down-regulation of ATP7A, overexpression of ATP7B, and pharmacological Cu depletion increase DBH retention in cells. In contrast, ATP7B inactivation elevates extracellular DBH
-
dependent on, copper-deficiency decreases the enzyme activity, tissue copper status, overview
-
dicopper enzyme. Copper ions are required not only for the catalytic steps but also for substrate binding and for locking the overall conformation of the enzyme in a configuration that is catalytically active. Absence of copper, or modified copper coordination, has a major effect on the overall flexibility of the enzyme
-
essentially required for activity, 2 atoms bound by 5 conserved His residues and 1 conserved Met residue
-
inter-copper electron transfer, mechanism, structure, 2 copper atoms per enzyme
-
metalloenzyme, required for catalysis, bound at the active site
-
the enzyme contains two mononuclear Cu centers
-
two distinct Cu centers are located in the protein active site. Of the two distinct Cu centers in the protein active site (separated by 11 A), the CuH site, believed to serve primarily as an electron transfer site, is coordinated by three histidines, H107, H108, H172, in a roughly T-shaped geometry. The CuM site, where oxygen binding and hydroxylation occur, has a mixed coordination sphere consisting of two histidines, H242, and H244, and a methionine, M314. Reaction mechanism, overview. Reaction of wild-type enzyme PHM with CO (an oxygen analogue) produces the M-site CO complex, which shows a unique XES spectrum that can be computationally reproduced by including interactions between Cu(I) and the CO ligand. The valence-to-core (VtC) region can serve as a probe of not only ligand speciation, but also offer insight into the coordination geometry, in a fashion similar to XAS pre-edges, and may be sufficiently sensitive to the coordination of exogenous ligands to be useful in the study of reaction mechanisms. Application of X-ray emission spectroscopy to copper proteins via a study of a series of mixed His-Met copper sites where the ligand set varies in a systematic way between the His3 and Met3 limits. The sites are derived from the wild-type peptidylglycine monooxygenase (PHM), two single-site variants which replicate each of its two copper sites (CuM-site and CuH-site), and the transporters CusF and CusB. Structure analysis of copper centers of wild-type and mutant enzymes
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0.1 mM, approx. 3fold activation of isoenzymes I and III
-
0.2% total copper content, probably 1 copper atom per subunit
-
0.21% copper, intra- and extracellular enzyme
-
0.22% copper, probably 4 copper atoms per enzyme molecule
-
1 mM, increase in activity
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1H-NMR spectra, each copper atom is coordinated by the Nepsilon atoms of 3 histidine residues
-
2 atoms of copper per 150000 Da
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2 copper atoms per functional unit of 42000 Da
-
2.1 copper atoms per polypeptide, enzyme form B
-
50% activation of L-dopa oxidation
-
a type 3 copper protein
-
activation at low concentrations, inhibition above 5 mM
-
chemical and spectroscopic studies of binuclear copper site
-
contains 2 copper atoms per subunit
-
copper containing enzyme. Bathochromic shift of selected phenylethanoid glycosides (0.01 mM) in the presence of CuSO4 (0.05 mM)
-
copper transporter ATP7A localizes to melanosomes in wildtype melanocytes. Copper restores in vitro tyrosinase activity in melanosomes of BLOC-1-deficient melanocytes, immunofluorescence microscopy
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correct copper concentration in the growth medium is critical for the expression of this copper containing enzyme. Optimization of the copper concentration and the expression conditions lead to a 10fold increase in the expression level of processed active histidine tagged TYR2
-
enzyme contains 1.9 copper atoms per molecule
-
enzyme contains 2 copper-binding domains
-
enzyme contains a binuclear copper complex at the active site which is responsible for the interaction with phenolic substrates and the binding and activation of molecular O2, depending on the oxidation state of the copper, 3 different forms are known: Met-, oxy-, and deoxytyrosinase
-
extended X-ray absorption fine structure, EXAFS, studies
-
first presention of a complete quantitative analysis of the XANES part of the XAS spectrum of a binuclear copper site
-
inhibitors such as sodium diethyl dithiocarbamate and thiourea, which combine with the copper moiety in the enzyme, are generally potent inhibitors of PPO. The inhibitors are copper-chelating agents and they suppress browning activities in which copper is directly involved in the oxidation of phenolic compounds
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the activator protein ORF378 may facilitate the incorporation of Cu(II) into apotyrosinase
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the active site of the tyrosinase model shows the same structural conformation as in sTyr and ibCO, where two copper ions are coordinated by three histidines each, forming a binuclear type 3 copper site similar to that of the template structure
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two copper ions in the active center of tyrosinase
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an anomalous site modeled as a dinuclear copper cluster. The mononuclear copper site is absent (one His is not conserved), and the zinc replaced by a copper ion
-
contains 2.3 copper ions per 100 kDa protomer
-
contains 20.8 copper ions per 100 kDa protomer
-
contains 4.8 copper ions per 100 kDa protomer
-
contains both mononuclear copper and a copper-containing cluster. Each 200000 Da pMMO complex contains 4.8 copper ions. The purified particulate methane monooxygenase is a mixture of Cu(I) and Cu(II) oxidation states
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regulates the metabolic switch between the methane monooxygenase and the methane monooxygenase-NADH:quinone oxidoreductase complex, also regulates the level of expression of the pMMO and the development of internal membranes
-
the enzyme contains 13 copper ions
-
the enzyme contains a dicopper center
-
the enzyme contains about 2.3 copper ions per 100 kDa protomer the enzyme contains a mixture of Cu+ and Cu2+
-
the enzyme uses copper to oxidize methane. Activity of metal-depleted, membrane-bound enzyme can be restored by copper and not by iron
-
the metal center consists of multiple copper centers, a dicopper center and a mono-copper center. Methane activation occurs at the Cu centers of particulate methane monooxygenase
-
the purified methane-oxidizing complex contains two copper atoms and one non-heme iron atom per mol of enzyme. The copper ion interacts with three or four nitrogenic ligands, EPR-active copper
-
contains a labile copper centre
-
modeling of the CuB and CuC metal-binding sites. The CuB site is found at the bottom of a narrow cleft formed by the interfaces of AmoB and AmoC. The Cu(II) ion is found in a distorted square planar geometry
-
Cu2+ does not dissociate from the protein molecule during unfolding
-
His1 and His96 coordinate the copper cofactor
-
the active site is formed by His37 and His144 that coordinate the copper atom in a T-shaped geometry
-
tight binding activity toward Cu2+ , Kd value 0.0048 mM. Residues His1 and His61 directly coordinate the basic copper cofactor in T-shaped geometry
-
a copper ion is located in the center of the substrate binding surface and coordinated by His1 and His69 and Tyr154
-
copper reduction in LPMO9C leads to structural rearrangements and compaction around the active site
-
Cu2+ does not dissociate from the protein molecule during unfolding
-
reduction of the mononuclear active-site copper by ascorbic acid increases the affinity and the maximum binding capacity of LPMOfor cellulose. The reduced redox state of the active-site copper and not the subsequent formation of the activated oxygen species increase the affinity toward cellulose
-
the active site is formed by His37 and His144 that coordinate the copper atom in a T-shaped geometry
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the active-site copper is preferentially skewed toward the pyranose C1 of the glycosidic linkage over the targeted glycosidic bond
-
the active site is formed by His37 and His144 that coordinate the copper atom in a T-shaped geometry
-
reduction of the mononuclear active-site copper by ascorbic acid increases the affinity and the maximum binding capacity of LPMO for cellulose, reaction of EC 1.14.99.54. The reduced redox state of the active-site copper and not the subsequent formation of the activated oxygen species increase the affinity toward cellulose
-
0.68 mol per mol of subunit
-
2 CuZn-type constitutively expressed enzymes plus one induced by exposure of animals to copper
-
coexpression with yeast copper chaperone, copper supplement of medium, about 1 atom per subunit
-
peculiar axial geometry of copper active sitewith low accessibility to external chelating agents
-
recombinant enzyme, 0.9 mol per mol of subunit, native enzyme, 0.86 mol per mol of subunit
-
wild-type, 0.98 atoms per subunit, mutant H43R, 1.42, mutant A4V, 1.06 atoms per subunit
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a Cu,Zn superoxide dismutase
-
a Cu/Zn superoxide dismutase
-
both small contents of Fe and Cu in the plants lead to an overexpression of the gene encoding the enzyme and enhanced FC-R activity in the plants
-
3.1 atoms per protein molecule
-
an InterPro Scan domain search predicted that Fox1 contains six cupredoxin domains
-
four copper ions are coordinated in two centers comprise the multicopper oxidase active site
-
contains six copper atoms per polypeptide chain and displays optical and electron paramagnetic resonance spectra consistent with the presence of type 1, type 2, and type 3 copper centers. The addition of copper leads to immediate and reversible changes in the optical and electron paramagnetic resonance spectra of the protein, as well as decreased thermal stability of the enzyme and stimulates both the phenoloxidase and ferroxidase activities
-
four copper atoms per molecule, spectroscopic properties are typical of blue copper oxidase. Presence of copper is essential for CueO-dependent oxidation of 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) and p-phenylenediamine, reactions of EC 1.10.3.2
-
in the absence of excess Cu(II), in addition to the normal reduction of the T1 copper, which occurs with a slow rate, a second electron transfer process occurs to an unknown site, possibly the trinuclear cluster, followed by a slow intramolecular electron transfer to T1 copper
-
mechanism of copper incorporation in CueO is sequential, with type 1 copper being the first to be reconstituted, followed by type 2 and type 3 sites. The copper content of the purified protein is routinely 0.5-0.6 Cu atoms/protein molecule
-
the affinity of site T4 for Cu(II) shows a KD of 0.0055 microM
-
contains one copper atom per molecule
-
protein contains a radical-coupled copper complex, a mononuclear Cu(II) center with an axial coordination
-
bimetallic [CuSMoO2] cluster
-
essential, in the [CuSMoO2] cluster
-
Mo/Cu-containing enzyme active site
-
essential for enzyme activity, 1.69 Cu per mol of enzyme dimer
-
protein contains a copper-center
-
contains copper, essential for activity
-
dinuclear heterometal [CuSMo(=O)OH] cluster in the active site
-
synthesis and characterization of dinuclear Mo-Cu complexes relevant to the active site of MoCu-enzyme by X-ray diffraction studies and by reactivity
-
enzyme contains 6 copper atoms
-
6 copper atoms per molecule
-
two copper atoms, CuA and CuB, are located in the active site and each is coordinated by three histidine residues. CuA is coordinated by His87, His108, and His117 residues, while CuB is coordinated by His241, His245 and His275
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1 mol of copper per mol of subunit
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contains 1 mol of copper per subunit
-
2 Cu2+ per protein molecule
-
3.7 copper atoms per enzyme molecule, recombinant enzyme
-
Cu2+ can be removed by KCN, reconstitution of the apoprotein by treating with CuSO4 for 40 h at 4°C and pH 7-8, Cu2+ reconstituted enzyme regains full activity, Fe2+ reconstituts 59,1% activity, Co2+ reconstituts 31% activity and Cd2+ reconstituts 24.5% activity
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four copper atoms per enzyme molecule
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metalloenzyme, 1 atom of copper per enzyme molecule
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multicopper enzyme, contains type 1,2 and 3 copper, authentic and recombinant wild-type enzyme contain 4 copper atoms/protein
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multicopper oxidase contains 4 copper ions per protein molecule. Cu-binding sites are not affected by differences in carbohydrate content and the N-terminal extension of four amino acid residues
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multicopper oxidase, the redox state of type I Cu is an equilibrium state of the oxidized and reduced forms highly depending on pH, possibly by a shift of the radical center between Cu and cys sulfur
-
contains T1 and T2/T3 redox copper centers
-
the active sites of the enzyme comprise four copper atoms
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the enzyme consists of 3 cupredoxin-like domains with 4 copper ions forming two active sites
-
the enzyme contains type I copper and a trinuclear copper center comprised of a type II copper and a pair of type III coppers
-
the enzyme possesses a trinuclear Cu center, which is composed of one T2Cu and a pair of T3Cu atoms, T3aCu and T3bCu
-
2 mol copper /mol FAD, cupric ion can be removed by dialysis against cyanide, copper is not involved in redox reaction
-
copper-dependent amine oxidase
-
enzyme is a copper amino axidase, contains 1 type II copper atom per subunit
-
2 mol copper/mol enzyme dimer
-
2 mol of Cu2+ per dimer
-
3.7 gatom of copper per mol of enzyme
-
bound by three His ligands of the active-site
-
contains 8 Cu2+ per 1200000 Da, Co2+, Zn2+ and Ni2+ can replace Cu2+, no effect of Mn2+
-
copper depleted enzyme can be reconstituted with either Cu2+, Zn2+, Co2+, or Ni2+, 79% of activity is restored with Cu2+, 19% is restored with Co2+, 1.7% with Zn2+ or Ni2+
-
copper involved in enzyme activity
-
copper-containing amine oxidase
-
study of cupric ions by magnetic-resonance and kinetic methods, native enzyme contains 2 tightly bound Cu2+ ions
-
the purified enzyme contains 2.39 mol of copper per mol of subunit
-
only the copper-containing homodimer is capable of rapid reoxidation and the zinc-copper heterodimers are incapable of rapid turnover at either subunit
-
0.063% i.e. 1.5 copper atoms per dimer
-
0.09-0.2 copper atoms per subunit
-
0.5 copper atoms per subunit
-
1.0 gatom of copper per 70000 Da
-
1.5 mol per mol of dimer
-
2 copper atoms per mol of enzyme
-
copper plays a functional role in enzyme activity
-
enzyme binds Cu. It is shown that PSAO exists predominantly in the Cu(I), topaquinone semiquinone state
-
enzyme contains 0.082% copper
-
enzyme contains 2 copper atoms
-
enzyme contains 2 Cu2+ per dimer
-
one atom of copper per mol of enzyme protein
-
removed from enzyme by treatment with diethyldithiocarbamate
-
contains 0.00021 mg Cu/cm
-
metal content: 0.1 mol per mol of enzyme
-
contains 1 mol of copper per subunit
-
might be a copper metalloenzyme
-
2.6 atoms copper per subunit, 2 type 1 Cu and 0.6 type 2 Cu
-
3.2 copper ions per trimer, most probably 3 type 1 and 3 type 2 copper, respectively
-
blue copper enzyme that shows little absorbance in the 460 nm range, purified recombinant nonactivated enzyme contains 1.97 mol Copper/mol enzyme, the CuSO4 activated enzyme contains 5.97 mol copper/mol enzyme i.e. 6 copper atoms per trimer, CuSO4 activation restores type 2 copper centers which are the sites of catalysis
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blue copper enzyme, 1 type 1 and 1 type 2 Cu atoms per subunit
-
contains 2 type 1 copper atoms per molecule but no other types of copper
-
copper atoms are coordinated by H122, C159, H168, and M173 for the type 1 Cu site and H127, H158, and H321 for the type 2 Cu site. The absorption spectrum of NirK displays two peaks at 598 and 449 nm characteristic for type I Cu proteins
-
copper containing nitrite reductase
-
copper-containing nitrite reductase
-
enzyme contains 2 type I copper and 1 type II copper ions
-
enzyme contains type 1 and type 2 copper centers, 6.3 copper atoms per trimer, blue copper enzyme
-
ligands of the type 1 and 2 Cu centers are completely conserved in NiR. They are His253, Cys294, His302, and Met307 for the type 1 Cu center and His258, His293, and His456 for type 2.Asp256 and His405 residues are important for enzyme catalysis by forming a hydrogen bond network on the type 2 Cu center. The EPR spectrum is also characteristic of NirK proteins that contain both type 1 and type 2 copper centers
-
one subunit contains a type 1 copper center, the second subunit a type 2 copper center, activity of copper depleted enzyme can be restored
-
tethering does not enhance the rate of electron delivery from its pendant cytochrome c to the catalytic copper-containing core. Tethering communicates the redox state of the heme to the distant type 2 copper center that helps initiate substrate binding for catalysis. It also tunes copper reduction potentials, suppresses reductive enzyme inactivation, enhances enzyme affinity for substrate, and promotes inter-copper electron transfer
-
the C-terminal cytochrome c domain is located at the surface of the type 1 copper site in the N-terminal domain from the adjacent subunit. The heme-to-Cu distance of 10.6 A is comparable to the transient electron transfer complex of normal Cu-nitrite reductase with cytochrome c
-
the type 1 Cu center functions as electron acceptor from the physiological electron donor azurin I, the type 2 Cu center is involved in binding and reduction of the substrate
-
two His nitrogen atoms (His126 and His174), and two sulfur atoms, one from Cys166 and the other from Met179, coordinate the Cu atom
-
study on reaction of copper(II)-nitrito complexes with tridentate and tetradentate, with either O,O'-bidentate or O-unidentate modes of nitrite binding to the cupric center . Differing modes of nitrite coordination to the copper(II) ion lead to differing kinetic behavior
-
3.2 mol of copper per mol of enzyme, in the as-isolated form. Presence of 0.1 mM enhances enzymic activity by 2fold
-
dependent on. The enzyme nitrous oxide reductase contains two copper sites: a binuclear site known as CuA that functions as an electron transfer site, and an unusual tetranuclear copper sulfide cluster active site, where N2O binds and is reduced. Two forms of this tetranuclear site have been structurally characterized. One, known as CuZ*, has a mu4 sulfide ligand bridging all four coppers and a solvent derived ligand on an open edge (the CuI-CuIV edge) where N2O is proposed to bind. The other form of the cluster, known as CuZ, has an additional mu2 sulfur ligand bridging the CuI-CuIV edge. Raman spectroscopic analysis and computationa modelling of Cu site structure and mechanism, binding and interaction, overview. Protonation state of the mu2 sulfur ligand on the CuI-CuIV edge in 1-hole and 2-hole CuZ
-
form A and B contain 9.0 and 8.2 Cu atoms per dimer, respectively
-
multicopper enzyme, 2 copper centers per subunit, CuA and CuZ
-
N2OR contains two copper centers, CuA, a binuclear mixed-valence center and CuZ, a tetranuclear sulfide-bridged copper cluster
-
the fully reduced all-Cu(I) state of CuZ is the catalytically relevant redox state of N2OR
-
7.0 atoms per dimer, needs 0.001 mM Cu2+ for full activity
-
A monomer carries 2 copper centers: CuA, which is a binuclear mixed-valence center similar to the CuA of cytochrome oxidases,4 and CuZ, a tetranuclear sulfidebridged copper cluster.
-
contains 7.1 atoms per dimer
-
Cu is bound by apo NosL, a coexpressed protein which is necessary for the assembling process of nitrous oxide reductase
-
CuA can exist in two oxidation forms [Cu1.5+ - Cu1.5+] and [Cu1+ - Cu1+]
-
CuA is electron transfer center, CuZ is the catalytic center
-
mu4-sulfide-bridged tetranuclear CuZ cluster
-
N2OR contains two metal centers: a binuclear copper center, CuA, that serves to receive electrons from soluble donors, and a tetranuclear copper-sulfide center, CuZ, at the active site.
-
one dinuclear centre CuA and a copper cluster CuZ in which four copper ions are litigated by seven histidine imidazoles and a bridging inorganic sufide
-
six copper atoms per monomer arranged in two centers named CuA and CuZ, 10.7 atoms per dimer
-
The two copper atoms (CuI and CuIV) at the ligand-binding site of the cluster play a crucial role in the enzymatic function, as these atoms are directly involved in bridged N2O binding.
-
two copper binding sites. The Cu4S active site is ligated by 7 His residues and contains three copper atoms (designated CuI, CuII, and CuIV) that share a plane with the mu4 sulfide ligand and with a solvent-derived ligand that bridges the CuI?CuIV edge, while the fourth copper (CuIII) bound to the mu4S2- is oriented out of this plane. Spectroscopic definition of the resting state of the Cu4S cluster, CuZ* intermediate, in turnover of nitrous oxide. CuZ°, an intermediate form of the Cu4S active site of nitrous oxide reductase (N2OR) is observed in single turnover of fully reduced N2OR with N2O, geometric and electronic structure, overview. CuZ° is a 1-hole (i.e. 3CuICuII) state with spin density delocalized evenly over CuI and CuIV. CuZ° has a terminal hydroxide ligand coordinated to CuIV, stabilized by a hydrogen bond to a nearby lysine residue. CuZ° can be reduced via electron transfer from CuA using a physiologically relevant reductant. Computational modelling of the Cu4S active site built from the atomic coordinates of the crystal structure of PdN2OR, PDB ID 1FWX at 1.6 A resolution, The model includes the active site core (Cu4S), the edge hydroxide, seven ligating histidines, and the second sphere residues Lys397 and Glu435. Spectrocopic Cu binding structure analysis, overview. reduction of CuZ° via electron transfer from CuA in turnover with cytrochrome c552 is faster than the decay of CuZ° to the inactive resting 1-hole CuZ* state of the Cu4S cluster, indicating that N2O reduction by the Cu4S active site of N2OR bypasses the resting 1-hole CuZ* state, which is not reduced by physiologically relevant reductants, instead, the 1-hole CuZ° intermediate is the relevant 1-hole oxidized state of the Cu4S cluster during turnover
-
wild-type 10.5 atoms per protein dimer
-
wild-type 7.2 atoms per protein dimer
-
wild-type 9.9 atoms per protein dimer
-
contains CuA in the small subunit
-
active binding site containing CuB
-
NOR of Roseobacter denitrificans is based on a heme b3-CuB center
-
contains 0.2 mol copper per mol enzyme protein
-
copper : uricase ratio is 1 : 1
-
copper : uricase ratio is 1 : 7
-
enzyme contains 0.15 mol of copper
-
negligible amount of copper
-
neither copper nor iron detected
-
the enzyme contains a CuA center in its small subunit
-
the heterobimetallic active-site heme 2 has a Cu(I) ion juxtaposed to a heme c at a Fe-Cu distance of 4.4 A. While the combination of metals is reminiscent of respiratory hemecopper oxidases, the oxidation-labile Cu(I) centre of MccA does not seem to undergo a redox transition during catalysis. The copper-depleted form II of MccA, the absence of the heterometal allows for a binding mode of sulfite that is similar to the one seen in the siroheme-containing enzymes or in NrfA. In the structure of the Cu-containing, high-activity form I of MccA, all 12 monomers in the asymmetric unit have a ligand bound to heme 2
-
contains 1 mol copper per subunit, in a binuclear complex
-
enzyme from kindney and small intestine
-
native activity is increased 2fold
-
Co(II) and Cu(II) can be reconstituted into the protein with similar stoichiometry
-
1:1 stoichiometry with Co
-
or iron, required. Copper is one of the most abundant metal species within the cells
-
the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site. Distorted Cu(I)-S3 site in the fully active enzyme in solution. Average Cu-S bond length of 2.25 A and a metal neighbor at 2.65 A, consistent with the Cu-Ni distance observed in the crystal structure. Cu-SCoA intermediate in the mechanism of acetyl-CoA synthesis. Essential and functional role for copper in the enzyme
-
the Ni in cluster A can be replaced by Cu yielding an inactive form of the acetyl-CoA synthase
-
high affinity copper-binding protein
-
contains 0.3 gatom per molecular weight of 75000 Da
-
contains 1 copper atom per enzyme molecule
-
BACE1 cytoplasmic domain interacts with the copper chaperone for superoxide dismutase-1 and binds copper
-
the recombinant enzyme contains 0.5 mol of zinc per mol of native enzyme. Additionally, 0.2 mol copper per mol native protein and traces of iron are detected
-
DddW has the highest affinity for binding Fe(II) at 5 nM, followed by Co(II), Ni(II), and Cu(II) at about 1-3 microM
-
paramagnetic Cu(II) is bound to the active site cysteine residues of mutant MerB D99S
-
the enzyme contains a copper ion in subunit I
-
the enzyme contains CuB
-
the enzyme has a CuB site
-
the enzyme is a four-subunit heme-copper oxidase containing CuB
-
the enzyme is a heme-copper terminal oxidase
-
the high-spin heme is magnetically coupled to a copper, CuB, forming a binuclear center which is the site of oxygen reduction to water
-
copper-containing enzyme
-
a type B heme-copper oxygen reductase. The binuclear Fea3Cu(B) center is the site of dioxygen chemistry and is involved in the proton translocation mechanism. The catalytic bimetallic Cu(B) center is probed in a number of different states using extended X-ray absorption fine structure (EXAFS) spectroscopy. The oxidized CuB center is four-coordinated with three histidine residues and one oxygen atom. No significant change in the protein structure in the vicinity of Cu(B) is observed upon reduction, apart from the release of the oxo ligand
-
binds 1 copper B ion per subunit
-
contains one copper atom
-
the active respiratory terminal oxidase segment of Sulfolobus sp. strain 7 contains one non-CO-reactive b-type cytochrome (b562) and two different a-type cytochromes (a583 and aa3), in addition to one copper and a Rieske-type FeS cluster, which, as a whole, function as an active caldariellaquinol oxidase supercomplex
-
the enzyme contains one copper atom
-
the recombinant subunit SoxH of the SoxM complex contains a correctly inserted binuclear Cu(A) cluster. In recombinant form, the metal interacts with cytochrome c as an artificial electron donor. The physiological electron donor is unknown, since Sulfolobus acidocaldarius does not contain any c-type cytochromes. The purple copper center of SoxM shows a pH dependency with a pKa at 6.4, suggesting protonation of the Cu-ligating histidines. Contains 1.3 Cu atoms per SoxH molecule
-
the enzyme contains a total of seven metal redox centers. One of it, the blue copper protein sulfocyanin, functionally links two subcomplexes. One is a bb3-type terminal oxidase moiety containing CuA and CuB, whereas the other consists of a Rieske FeS-protein and a homolog to cytochrome b in this case hosting two hemes AS. Based on a 1:1 stoichiometry, 1 mol complex contains 6 mol Fe and 4 mol Cu
-
cytochrome aa3-600 contains CuB
-
the enzyme contains a binuclear heme iron-copper site with only one copper CuB, while the Cu A center is lacking
-
Cox17p specifically binds Cu(I) at a molar copper content of 3.3 under redzuced conditions and significantly activates the mitochondrial. The Cu-Cox17p complex is maintained between pH values from 5.0 to 7.7. Cu is completely released from Cox17p at pH 8.0. The stringent selectivity of Cox17p for cipper is required for enzyme activation
-
cytochrome c oxidase assembly factor 11 binds copper. Residue Cys157 is important for copper binding, whilst Cys60 is not
-
oxidation of copper in cytochrome c oxidase of Prnp-/- mice is similar to that in Prnp+/+ mice
-
-
395996, 396003, 396036, 396073, 396077, 396001, 396050, 396109, 395999, 396000, 396002, 396006, 396038, 396049, 396092, 691038, 396074, 395992, 396008, 396012, 700992, 698494, 698272, 396029, 395991, 396081, 396069, 396071, 396035, 396088, 692575, 396083, 396026, 396075, 396085
-
0.7 copper atoms in minimal structure unit composed of the three subunits
-
0.96 mol Cu per mol of enzyme
-
2 copper ions at the CuA site
-
2 Cu atoms per enzyme molecule
-
2-3 Cu ions per complex of one subunit
-
2.8 - 3.8 nmol/mg protein
-
CuA contains a mononuclear Cu site with 2 cysteine sulfur and 2 imidazole nitrogen atoms as ligands
-
CuA located in subunit II
-
CuA located in subunit II, binding of O2 and reduction
-
CuA may be coordinated by 2 cysteine ligands, CuA-protein coordination model
-
CuB located in subunit I, electron flow from ferrocytochrome c to binuclear center
-
discussion of Cu content
-
models for metal binding
-
proposed third copper center, CuX, may result from impurities
-
recombinant Cox19 binds 1 mol eq of Cu(I) per monomer. Cu(I) binding may be a transient property
-
reduction of dioxygen to water takes place at the heme a3-CuB binuclear center
-
structural interpretations of cytochrome c oxidase metal active sites by X-ray absorption spectroscopy, XAS, studies
-
two atoms per molecule enzyme
-
X-ray absorption fine structure, EXAFS, studies
-
CopB exhibits metal-stimulated ATPase activity in response to Cu+, but not Cu2+. Cu+ is coordinated by four sulfur ligands, likely derived from conserved cysteine and methionine residues. The enzyme does bind Cu2+, the binding site is not the prototypical P1B-ATPase transmembrane site and does not involve sulfur coordination
-
enzyme binds Cu(I) witrh subfemtomolar affinity
-
the four most N-terminal metal-binding domains in ATP7B, upon stoichiometric copper addition, adopt a more compact arrangement with higher thermal stability than in the absence of copper. No stable complex was found in solution between the metal-binding domains and the nucleotide-binding domain of ATP7B
-
the enzyme contains two Cu(I)-binding sites. Copper binding within the His-Met-loop stabilizes Cu(I) and protects it from oxidation, which may further aid the transfer of copper from ATP7A to acceptor proteins
-
demonstration of facile copper transfer between domain 1 and domain 4
-
in HepG2 cells, elevated copper levels stimulates trafficking of ATP7B to pericanalicular vesicles. Mechanism of biliary copper excretion involves ATP7B-mediated vesicular sequestration of copper rather than direct copper translocation across the canalicular membrane
-
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