Blue copper electron transfer

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... 

Several copper enzymes will be discussed in detail in subsequent sections of this chapter. Information about major classes of copper enzymes, most of which will not be discussed, is collected in Table 5.1 as adapted from Chapter 14 of reference 49. Table 1 of reference 4 describes additional copper proteins such as the blue copper electron transfer proteins stellacyanin, amicyanin, auracyanin, rusticyanin, and so on. Nitrite reductase contains both normal and blue copper enzymes and facilitates the important biological reaction NO) — NO. Solomon s Chemical Reviews article4 contains extensive information on ligand field theory in relation to ground-state electronic properties of copper complexes and the application of... 

Ceruloplasmin is involved in copper storage and transport as well as in iron mobilisation and oxidation. Among the blue oxidases it is unique since it contains, in addition to the usual motif of a type 1 combined with the trinuclear cluster, two other type 1 coppers. Electron transfer occurs, however, only between five of the six copper ions since one of the type 1 centres is not catalytically relevant due to its too high redox potential. The redox potentials of the centres were determined and possible electron transfer pathways among the copper sites were discussed.101... 

Some progress has been made in the characterization of the redox centres. The presence of a potential type 1 blue copper site in subunit I is in accord with EXAFS data that have demonstrated Cu—S interactions, in particular the possibility of two sulfur atoms bound to CuA.1309 It seems possible therefore that CuA is a type 1 copper, typical of copper electron-transfer proteins. The nature of CuB is less certain ESR parameters indicate that CuB is similar to type 3 copper, which occurs pairwise in copper oxidases as the 02-binding site. 

Blue copper proteins transfer electrons between various biological systems, e.g., between the two photosystems in photosynthesis (plastocyanin). They are characterized by a number of unusual properties, viz., a bright blue color, an unusually high reduction potential, and distinctive... 

In this reaction, copper metal plates out on the surface of the zinc. The blue color of the aqueous Cu2+ ion fades as it is replaced by the colorless aqueous Zn2+ ion (Figure 18.1). Clearly, this redox reaction is spontaneous it involves electron transfer from a Zn atom to a Cu2+ ion. 

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

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. 

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+ ... 

Copper, Cu+(d10), Cu2+ (d9) 4, tetrahedral N-Thiolate, thioether, AMmidazole Electron transfer in Type I blue copper proteins... 

C. Electron-Transfer Kinetics of Blue Copper Proteins... 

Electronic spectra of metalloproteins find their origins in (i) internal ligand absorption bands, such as n->n electronic transitions in porphyrins (ii) transitions associated entirely with metal orbitals (d-d transitions) (iii) charge-transfer bands between the ligand and the metal, such as the S ->Fe(II) and S ->Cu(II) charge-transfer bands seen in the optical spectra of Fe-S proteins and blue copper proteins, respectively. Figure 6.3a presents the characteristic spectrum of cytochrome c, one of the electron-transport haemoproteins of the mitochondrial... 

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