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Blue copper

Form deep blue copper salts usually sparingly soluble in water. [Pg.381]

MHM Olsson, U Ryde, BO Roos, K Pierloot. On the relative stability of tetragonal and trigonal Cu(II) complexes with relevance to the blue copper proteins. J Biol Inorg Chem 3 109-125, 1998. [Pg.412]

Molecular liquids. The bottom layer, carbon tetrachloride (CCI4), and the top layer, octane (CbHis), are nonpolar molecular liquids that are not soliirle in water. The middle layer is a water solution of blue copper sulfate. [Pg.235]

On the relationship between protein-forced ligand fields and the properties of blue copper centres. H. B. Gray and B. G. Malmstrom, Comments Inorg. Chem., 1983, 2, 203-209 (14). [Pg.41]

Copper proteins. Systems containing the blue copper centre. J. A. Fee, Struct. Bonding (Berlin),... [Pg.42]

Structure and electron transfer reactivity of the blue copper protein, plastocyanin. A. G. Sykes, Chem. Soc. Rev., 1985,14, 283 (117). [Pg.68]

Blue copper electron transfer proteins, 6,712-717 Blue copper oxidases, 6,699 Blue copper proteins, 2, 557 6, 649 Blue electron transfer proteins, 6,649,652 spectroscopy, 6, 651 Blue oxidases copper, 6,654,655 Blueprint process, 6,124 Blue proteins model studies, 6,653 Boleite... [Pg.92]

M.7 Copper (II) nitrate reacts with sodium hydroxide to produce a precipitate of light blue copper(II) hydroxide. [Pg.123]

Messerschmidt A (1988) Metal Sites in Small Blue Copper Proteins, Blue Copper Oxidases and Vanadium-Containing Enzymes. 90 37-68 Michel H, see Hemmerich P (1982) 48 93-124... [Pg.251]

The many redox reactions that take place within a cell make use of metalloproteins with a wide range of electron transfer potentials. To name just a few of their functions, these proteins play key roles in respiration, photosynthesis, and nitrogen fixation. Some of them simply shuttle electrons to or from enzymes that require electron transfer as part of their catalytic activity. In many other cases, a complex enzyme may incorporate its own electron transfer centers. There are three general categories of transition metal redox centers cytochromes, blue copper proteins, and iron-sulfur proteins. [Pg.1486]

Blue copper proteins. A typical blue copper redox protein contains a single copper atom in a distorted tetrahedral environment. Copper performs the redox function of the protein by cycling between Cu and Cu. Usually the metal binds to two N atoms and two S atoms through a methionine, a cysteine, and two histidines. An example is plastocyanin, shown in Figure 20-29Z>. As their name implies, these molecules have a beautiful deep blue color that is attributed to photon-induced charge transfer from the sulfur atom of cysteine to the copper cation center. [Pg.1487]

C20-0102. Blue copper proteins are blue when they contain Cu but colorless as Cu compounds. The color comes from an interaction in which a photon causes an electron to transfer from a sulfur lone pair on a cysteine iigand to the copper center. Why does this charge transfer interaction occur for Cu but not Cu+ ... [Pg.1495]

Blanford CF, Heath RS, Armstrong FA. 2007. A stable electrode for high-potential, electrocatalytic O2 reduction based on rational attachment of a blue copper oxidase to a graphite surface. Chem Commun 1710-1712. [Pg.630]

Fee, J.A. Copper Proteins - Systems Containing the Blue Copper Center. Vol. 23,... [Pg.128]

Blue copper in azutin Trigonal distorted toward tetrahedral... [Pg.163]


See other pages where Blue copper is mentioned: [Pg.118]    [Pg.403]    [Pg.435]    [Pg.1090]    [Pg.393]    [Pg.396]    [Pg.396]    [Pg.398]    [Pg.48]    [Pg.180]    [Pg.245]    [Pg.256]    [Pg.355]    [Pg.356]    [Pg.512]    [Pg.58]    [Pg.191]    [Pg.196]    [Pg.435]    [Pg.1090]    [Pg.598]    [Pg.107]    [Pg.114]    [Pg.764]    [Pg.585]    [Pg.146]    [Pg.497]    [Pg.323]    [Pg.329]    [Pg.211]    [Pg.93]    [Pg.93]    [Pg.133]   
See also in sourсe #XX -- [ Pg.117 ]




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Active site protonations, blue copper

Active site protonations, blue copper proteins

Ascorbate oxidase Blue copper oxidases

Blue Copper Oxidases

Blue Copper Oxidases A. Messerschmidt

Blue and White Copper Sulfate

Blue copper digestion

Blue copper electron transfer

Blue copper enzymes

Blue copper evolution

Blue copper fragmentation

Blue copper oxidases Ascorbate oxidase Ceruloplasmin

Blue copper oxidases Laccase

Blue copper oxidases dioxygen binding

Blue copper oxidases evolution

Blue copper proteins Tetragonal structures

Blue copper proteins Trigonal structures

Blue copper proteins activation

Blue copper proteins amicyanin

Blue copper proteins ascorbate

Blue copper proteins auracyanin

Blue copper proteins axial ligand

Blue copper proteins azurin

Blue copper proteins binding sites

Blue copper proteins bonding

Blue copper proteins characterization

Blue copper proteins charge transfer excitation

Blue copper proteins classification

Blue copper proteins conservation

Blue copper proteins crystal structures

Blue copper proteins electron self-exchange rates

Blue copper proteins electron transfer

Blue copper proteins family members

Blue copper proteins function

Blue copper proteins halocyanin

Blue copper proteins identification

Blue copper proteins isolation

Blue copper proteins laccases

Blue copper proteins ligands, amino acid sequence

Blue copper proteins metal coordination

Blue copper proteins metal coordination geometry

Blue copper proteins metal substitution

Blue copper proteins multicopper oxidases

Blue copper proteins nitrosocyanin

Blue copper proteins optical absorption

Blue copper proteins oxidation site

Blue copper proteins oxygen activation

Blue copper proteins phytocyanins

Blue copper proteins plantacyanin

Blue copper proteins protein strain

Blue copper proteins pseudoazurin

Blue copper proteins resonance Raman spectroscopy

Blue copper proteins rusticyanin

Blue copper proteins sequences

Blue copper proteins solution structures

Blue copper proteins spectroscopic properties

Blue copper proteins stellacyanin

Blue copper proteins structural properties

Blue copper proteins sulfocyanin

Blue copper proteins uclacyanin

Blue copper structural analysis

Copper blue staining, caused

Copper phthalocyanine (Monastral Blue)

Copper phthalocyanine blue

Copper phthalocyanine blue metal-free pigment

Copper proteins, blue plastocyanin

Copper proteins, blue spectroscopy

Cucumber basic blue protein copper site

Electrochemistry of Blue Copper Proteins

Electron blue copper proteins

Electron paramagnetic resonance blue copper protein

Electron transfer in blue copper proteins

Electron transport, blue copper proteins

Electronic spectra, blue copper proteins

Greens and blues with a copper basis

Metal-free copper phthalocyanine blue

Metalloproteins blue copper proteins

Mononuclear blue copper proteins

Non-blue copper oxidases

Optical spectra, blue copper

Optical spectra, blue copper protein

Phase- and Flocculation-Stabilized Copper Phthalocyanine Blue Pigments

Plastocyanin, blue copper center

Protein blue-copper

Redox potentials blue copper oxidases

Reduction potentials blue copper proteins

Self-exchange rate constants, blue copper

Self-exchange rate constants, blue copper proteins

Spectral properties, blue copper

Spectral properties, blue copper plastocyanin

Spectroscopic studies, blue copper

Structural Relationships among the Blue Copper Oxidases

Structure of blue copper proteins

The Blue Copper Oxidases

Type 1 Blue Copper Proteins — Electron Transport

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