Bovine cytochrome

An iterative procedure using the solid film linear driving force model has been used with a steric mass action isotherm to model displacement chromatography on ion exchange materials and the procedure applied to the separation of horse and bovine cytochrome c using neomycin sulfate as the displacer.4 The solid film linear driving force model is a set of two differential equations imposing mass transfer limitations. 

Rytdmaa, M., and Kinnunen, P.K.J., 1995, ReversibUity of the binding of cytochrome c to Uposomes. Implications for lipid-protein interactions./. B/oZ. Chem., 270 3197-3202 Salamon, Z., and ToUin, G., 1996, Surface plasmon resonance studies of complex formation between cytochrome c and bovine cytochrome c oxidase incorporated into a supported planar Upid bUayer. II. Binding of cytochrome c to oxidase-containing cardiohpin /phosphatidylcholine membranes. Biophys. J., 71 858-867 Salamon, Z., and ToUin, G., 1997, Interaction ofhorse heart cytochrome c with Upid bilayer membranes effects on redox potentials. J. Bioenerg. Biomembr. 29 211-221 Scarlett, J.L., and Murphy, M.P., 1997, Release of apoptogenic proteins from the... 

Hydrolysis of peptides or proteins with acid yields a mixture of free a-amino acids. When completely hydrolyzed, each type of protein yields a characteristic proportion or mixture of the different amino acids. The 20 common amino acids almost never occur in equal amounts in a protein. Some amino acids may occur only once or not at all in a given type of protein others may occur in large numbers. Table 3-3 shows the composition of the amino acid mixtures obtained on complete hydrolysis of bovine cytochrome c and chymotrypsinogen, the inactive precursor of the digestive enzyme chymotrypsin. These two proteins, with very different functions, also differ significantly in the relative numbers of each kind of amino acid they contain. 

Amino acid Bovine cytochrome c Bovine chymotrypsinogen... 

Figure 22-23 Electrospray quadrupole mass spectrum of acidified bovine cytochrome c showing peaks from species with different numbers of protons, MHfJ+. [From T. Wachs and J. Henion, Electrospray Device tor Coupling Microscale Separations and Other Miniaturized Devices with Electrospray Mass Spectrometry." Anal. Chem. 200T, 73, 632.]...

Usanov SA, Graham SE, Lepesheva GI, et al. Probing the interaction of bovine cytochrome P450scc (CYP11A1) with adrenodoxin evaluating site-directed mutations by molecular modeling. Biochemistry 2002 41 8310-8320. 

Fig. 8.24. Separation of a tryptic cytochrome C digest by pressure assisted gradient CEC. Column, 60 x 0.18 mm i.d. packed with 3 pm Vydac Cl8 eluents, (A) 0.07% trifluoroacetic acid in water, (B) 0.07% trifluoroacetic acid in acetonitrile gradient elution with 0-50% B in 20 min applied pressure, 9 MPa in (a), 5 MPa in (b) 7 MPa in (c) applied voltage, 0 kV in (a), 1 kV in (b), 0.6 kV in (c) Detection, nanospray ESI-MS, m/z 200-1500, 10 spectra/s sample, tryptic digest of 8 pmol bovine cytochrome C. (Reprinted with permission from ref. [45], Copyright [1997] American Chemical Society).

Cytochrome c, lysozyme, myoglobin, ribonuclease A Cytochrome c mixture (horse, tuna, chicken, and bovine) Cytochrome c mixture (horse, tuna, chicken, and bovine) Trypsinogen, a-chymotrypsinogen, ribonuclease A, cytochrome c... 

El-FFF is a technique devoted to the fractionation of proteins which is reflected in the number of papers applying this technique to protein separations. The possibilities of El-FFF were first demonstrated by Caldwell for the separation of albumin, lysozyme, hemoglobin, and y-globulin in two different buffer solutions (pH 4.5 and 8.0) [35]. Later, the performance of an El-FFF channel with flexible membranes [36], a channel with rigid membranes [256], or a circular channel [260] for the separation of proteins were described. In these studies, human and bovine serum albumin, y-globulin (bovine), cytochrome C (horse heart), lysozyme (egg white) and soluble ribonucleic acid (t-RNA), as well as denaturated proteins, were successfully separated. 

Fig. 2. Helix packing angle ( 2) distributions. Gray bars The distribution of angles seen in 3498 helix packing interactions from soluble proteins. Black bars The distribution seen in 88 helix interactions from the membrane proteins, bacteriorhodopsin, bovine cytochrome c oxidase, and photosynthetic reaction center (Bowie, 1997a).

Sakaki, T., Shibata, M., Yabusaki, Y., Murakami, H., and Ohkawa, H., 1990, Expression of bovine cytochrome P450c21 and its fused enzymes with yeast NADPH-cytochrome P450 reductase in Saccharomyces cerevisiae, DNA Cell Biol. 9 6039614. 

Akiba, T., Toyoshima, C., Matsunaga, T., Kawamoto, M., Kubota, T., Fukuyama, K., Namba, K., and Matsubara, H., 1996, Three-dimensional structure of bovine cytochrome bcl complex by electron cryomicroscopy and helical image reconstruction. Nature Struct. Biol. 3 553n561. 

Mukai, K., Miyazaki, T., Wakabayashi, S., Kuramitsu, S., and Matsubara, H., 1985, Dissociation of bovine cytochrome cl subcomplex and the status of cysteine residues in the subunits, J. Biochem. (Tokyo) 98 1417nl425. 

Figure 7 Model of the X-ray crystal structure of the bovine cytochrome c oxidase. The dimeric Cua site, c)dochromes a and a-i, and the Cub center are shown in black. Electrons enter the enzyme through Cua and oxygen is activated at the c)dochrome as/CuB active site...

Figure 3-23. RP separation of bovine cytochrome c tryptic digest at flow rates (A) l.OmL/min with 60-min gradient and (B) lO.OmL/min with 6-min gradient. (Reprinted...

Bovine cytochrome c oxidase is reasonably well understood at the structural level (Figure 1818). It consists of 13 subunits, of which 3 (called subunits I, II, and III) are encoded by the mitochondrial genome. Cytochrome c oxidase contains two heme A groups and three copper ions, arranged as two copper centers, designated A and B. One center, Cu /Cu, contains two copper ions linked by two bridging cysteine residues. This center initially accepts electrons from... 

From the primary structures bovine cytochrome c, [181], human [182], bovine [153], mouse [183], Saccharomyces [184], Aspergillus [185], and Neurospora [186] cytochrome b. Studies on the bovine [187] and Neurospora [188,189] Complex III are summarised. Complex III from rat [190] and Saccharomyces [191] are very similar but the latter may lack the smallest subunit , band VIII [192]. The complex forms dimers in Triton X-100 [189,192,193]. 

S. H. Northrup, K. A. Thomasson, C. M. Miller, P. D. Barker, L. D. Eltis, J. G. Guillemette, S. C. Inglis and A. G. Mauk, Effects of charged amino-acid mutations on the bimolecular kinetics of reduction of yeast iso-1-ferricytochrome-C by bovine cytochrome-B(5), Biochemistry, 32 (1993) 6613-6623. 

Fig. 20. The NIR MCD spectra of oxidized bovine cytochrome c oxidase with (dashed line) and without (solid line) CN binding. The spectra are recorded at 4.2 K and 5 T. Arrows indicate the wavelengths at which MCD magnetization curves were measured (see Fig. 21).

A comparative study of the metal centers in cytochrome c oxidase from several bacterial sources, including Thermus thermophilus and P. denitrificans, using EPR and MCD spectroscopy has established that in both cases cytochrome a is liganded by two histidine oxidases and the Cua center is identical to that in bovine cytochrome c oxidase (105, 106). The properties of the cytochrome Os/Cub dimer have not been established to be identical, although ferrocytochrome 03 is high-spin ferrous, as expected. Recent studies of the MCD properties of the Cua center in cytochrome c oxidase and a copper center in nitrous oxide reductase (107,108) show that the two centers are virtually identical. The evidence from the EPR hyperfine structure of the copper center in nitrous oxide reductase suggests that the center in this enzyme is a mixed-valence Cu(I)/Cu(II) dimer, which raises the interesting prospect that the Cua center in cytochrome c oxidase is also a dimeric copper species. 

Lee KB, Jun ES, Lamar GN, Rezzano IN, Pandey RK, Smith KM, Walker FA, Buttlaire DH (1991) Influence of heme vinyl-protein and carboxylate protein contacts on structure and redox properties of bovine cytochrome-B5. J Am Chem Soc 113 3576-3583... 

The crystal structure of bovine cytochrome c oxidase (Complex IV) homodimer has been determined to a resolution of 1.8 A (Shinzawa-Itoh et al., 2007). This integral membrane protein complex composed of thirteen different subunits per monomer is responsible for the reduction of molecular oxygen to water during aerobic respiration, with concomitant proton pumping across the mitochondrial inner membrane. A combination of high resolution X-ray structure analysis of the integral lipids in bovine Complex IV with mass spectroscopy analysis of their chain lengths and the positions of the unsaturated bonds of the... 

Delorme, C., A. Piffeteau, F. Sobrio, and A. Marquet(1997). Mechanism-based inactivation of bovine cytochrome P450, p by 18-unsamrated prt esterone derivatives. Eur. J. Biochem. 248, 252-260. 

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