Basic cucumber

Food. Food-grade calcium chloride is used in cheese making to aid in rennet coagulation and to replace calcium lost in pasteurization. In the canning iadustry it is used to firm the skin of fmit such as tomatoes, cucumbers, and jalapenos. It acts as a control in many flocculation, coagulation systems (37). Food-grade calcium chloride is used in the brewing iadustry both to control the mineral salt characteristics of the water and as a basic component of certain beers (see Beer). 

The molecular structure of another blue protein, the phytocyanin (phytocyanins are electron carriers found in the non-photosynthetic part of plants) cucumber basic protein (FW=10 100), also known as plantacyanin, is shown in Figure 33.60... 

Guss, J. M., et al. (1988). Phase determination by multiple-wavelength x-ray diffraction crystal structure of a basic blue copper protein from cucumbers. Science 241, 806-811. 

Cucumber basic > Electron transfer Cucumber Guss etal. (1988)... 

There are a number of excellent sources of information on copper proteins notable among them is the three-volume series Copper Proteins and Copper Enzymes (Lontie, 1984). A review of the state of structural knowledge in 1985 (Adman, 1985) included only the small blue copper proteins. A brief review of extended X-ray absorption fine structure (EXAFS) work on some of these proteins appeared in 1987 (Hasnain and Garner, 1987). A number of new structures have been solved by X-ray diffraction, and the structures of azurin and plastocyanin have been extended to higher resolution. The new structures include two additional type I proteins (pseudoazurin and cucumber basic blue protein), the type III copper protein hemocyanin, and the multi-copper blue oxidase ascorbate oxidase. Results are now available on a copper-containing nitrite reductase and galactose oxidase. 

Cucumber basic blue protein has been put in a class of its own in view of having a disulfide, unUke plastocyanin, although its fold is generally like that of plastocyanin. 

Cucumber basic blue protein (Cbp) is a protein without known function, also known as cusacyanin or plantacyanin. Its structure (Guss et al., 1988) completes the repertoire of cupredoxins with known structures. The topology of its folding is similar (Fig. 5) to those of plastocyanin and azurin, as might have been expected from sequence similarities and... 

Fig. 5. (a) Copper site in cucumber basic blue protein (Cbp). (b) Ribbon drawing of the Cbp backbone, (c and d) Schematic of Cbp topology. 

Blue copper proteins, 36 323, 377-378, see also Azurin Plastocyanin active site protonations, 36 396-398 charge, 36 398-401 classification, 36 378-379 comparison with rubredoxin, 36 404 coordinated amino acid spacing, 36 399 cucumber basic protein, 36 390 electron transfer routes, 36 403-404 electron transport, 36 378 EXAFS studies, 36 390-391 functional role, 36 382-383 occurrence, 36 379-382 properties, 36 380 pseudoazurin, 36 389-390 reduction potentials, 36 393-396 self-exchange rate constants, 36 401-403 UV-VIS spectra, 36 391-393 Blue species... 

We have studied the blue copper proteins plastocyanin, azurin, cucumber basic protein ( ) and nitrite reductase (NiR) (159,160). We shah focus on these four in the remainder of this section. 

Fig. 8. Simulated (160) and experimental (165,166) MCD spectra of (a) azurin, (b) plastocyanin, (c) cucumber basic protein, and (d) nitrite reductase.

The same tests also were employed with a somewhat different collection of plants, such as radish, cucumber, soybean, and ryegrass. These approaches seem simple and basic to weed scientists today, but they were revolutionary in the early 1950s and essential to discovering the biological properties and effectiveness of the triazine herbicides. 

Basic blue proteins have been isolated from a number of plant sources and have previously been referred to as plantacyanin (Aikazyan and Nalbandyan, 1975,1979 Sakurai et al, 1982). The protein from cucumber has been the most extensively studied of the basic blue proteins and the crystal structure is now available (Guss et al., 1988). The function of this basic blue protein is unknown, however, it is probably not involved in photosynthetic electron transport as it will not replace plastocyanin in that electron transport chain (Adman, 1985). 

The cucumber basic blue protein is made up of a single polypeptide chain of 96 amino acids containing a single copper ion with a molecular weight of 10000 (Adman, 1985). The amino acid sequence (Bergman et al., 1977) is very similar to those of stellacyanin and umecyanin. The copper in cucumber blue protein displays the characteristic spectroscopic properties of a typical blue copper site (Table 5-5). 

The crystal structure of cucumber basic blue protein has now been refined to 3.0 A resolution (Adman, 1985). The protein consists of eight strands, only five of which form a P-sandwich and the protein has less P-sheet character than plastocyanin or azurin. The ligands to copper are provided by the side chains of His-39, Cys-79, His-84 and Met-89. The copper site has the N2SS coordination seen in plastocyanin. The imidazole rings of the His-39 and His-94 residues are exposed to the solvent providing a likely entry site for electon transfer to the copper centre. 

Unknown stellacyanin, umecyanin, cucumber basic blue copper protein... 

Bond Cu(SCPh3)L Azurin Populus plastocyanin Enteromorpha prolifera plastocyanin Pseudoazurin Cucumber basic blue copper protein"... 

Solvent is usually excluded from the blue copper site, which is buried 6 A inside the protein, having only the His ligand from the copperbinding loop exposed to the surface. The phytocyanins, stellacyanin and plantacyanin (cucumber basic protein), are exceptions, in which both His ligands are solvent exposed and the copper ion is only 3 A beneath the protein surface. This situation makes the copper center in this family of blue copper proteins more accessible to low-molecular-weight solutes (see Section V). 

Plantacyanins are strongly basic proteins with an isoelectric point close to 11. First isolated from cucumber in 1974, plantacyanins have since been characterized from various other plant species (Markossian et al., 1974 Aikazyan and Nalbandyan, 1981). They exhibit relatively high sequence identity to stellacyanin and spectroscopic properties similar... 

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