Oxidase copper

FIGURE 21.18 (a) The Cn site of cytochrome oxidase. Copper ligands inclnde two histidine imidazole groups and two cysteine side chains from the protein, (b) The coordination of histidine imidazole ligands to the iron atom in the heme a center of cytochrome oxidase. 

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... 

ABP1 Amiloride binding protein 1 (amine oxidase (copper-containing)) ABP, DAO, 7q34 - 7q36 KAO, AOC1, DAOl 150,180,506 -150,189,312 8807 5 2428 751... 

AOC-2 Amine oxidase, copper-containing 2 (retina-specific) DA02, 17q21 RAO 38,250,135 -38,256,250 6116 4 2665 2584 (2 isoforms) 757 730... 

AOC-3 Amine oxidase, copper-containing 3 (vascular adhesion protein 1) HPAO, 17q21 SSAO, VAP1, VAP-1, 38,256,727 -38,263, 667 6941 4 4026 763... 

Cytochrome c model systems, 847 Cytochrome P-450 reactions, 844 Cytochrome enzymes, 772 Cytochrome c oxidase copper complexes, 772 Cytochromes, 982 Cytosine... 

In the following sections, examples of all the classes of reaction given above will be discussed, with emphasis on those that have been well studied. Many of the enzymes involved in these processes are hemoproteins, but non-heme prosthetic groups are important in oxygenases and are also present in some oxidases. Copper is an important metal in this context, and is present in the oxygen transport protein hemocyanin, and in oxidases such as cytochrome oxidase and laccase. Some flavoenzymes are important too, but will not be covered in this discussion. 

Fig. 7. Inner sphere of the galactose oxidase copper-binding site. Geometric details of the ligand arrangement in the aquo complex are indicated in the figure. (Based on protein coordinates PDB ID IGOG.)...

Copper Proteins Oxidases Copper Proteins with Dinuclear Active Sites Cytochrome Oxidase. 

Copper Enzymes in Denitrification Copper Hemo-cyanin/Tyrosinase Models Copper OrganometalUc Chemistry Copper Proteins Oxidases Copper Proteins with Dinuclear Active Sites Copper Proteins with Type 1 Sites Superconductivity. 

BACTERIAL OXIDASES, COPPER RESISTANCE, AND METALLO-OXIDATION... 

Active Sites, Copper Proteins Oxidases, Copper Proteins with Type 1 Sites, Copper Proteins with Type 2 Sites, Copper Enzymes in Denitrification, Iron-Sulfur Models of Protein Active Sites, Iron-Sulfur Proteins Nickel Enzymes Cofactors and Nickel Models of Protein Active Sites). However, since many metalloenzymes have been found or postulated to incorporate metal-sulfur bonding, it is appropriate that a very short sununary be included here. 

Chalcogenides Solid-state Chemistry Copper Enzymes in Denitrification Copper Hemocyanin/Tyrosinase Models Copper Proteins Oxidases Copper Proteins with Dinuclear Active Sites Copper Proteins with Type 1 Sites Copper Proteins with Type 2 Sites Iron Sulfitf Models of Protein Active Sites Iron-Snlfiir Proteins Nickel Enzymes Cofactors Nickel Models of Protein Active Sites Polynuclear Organometallic Cluster Complexes. 

D-Aspartate oxidase L-Amino-acid oxidase D-Amino-acid oxidase Amine oxidase (flavin-containing) Amine oxidase (copper-containing) D-Glutamate oxidase Ethanolamine oxidase Putrescine oxidase L-Glutamate oxidase L-Lysine oxidase... 

Is small organic or inorganic molecules that an apo-enzyme requires for its activity, e.g. in lysine oxidase, copper is loosety bound which act as cofactor. 

Cofactor of enzymes xantine and aldehyde oxidase copper antagonist... 

The copper-containing amine oxidases (copper amine oxidases, diamine oxidases) possess either a topaquinone or a 6-hydroxydopamine cofactor (Fig. 16.7-15), generally integrated in the oxidase primary structure. Tyrosine residues of the enzyme backbone in the active site are discussed as precursors for the prosthetic group[37]. 

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