Aspartic acid cytochrome

Fig. 3. Cation-exchange chromatography of protein standards. Column poly(aspartic acid) Vydac (10 pm), 20 x 0.46 cm. Sample 25 pi containing 12.5 pg of ovalbumin and 25 pg each of the other proteins in the weak buffer. Flow rate 1 ml/min. Weak buffer 0.05 mol/1 potassium phosphate, pH 6.0. Strong buffer same +0.6 mol/1 sodium chloride Elution 80-min linear gradient, 0-100% strong buffer. Peaks a = ovalbumin, b = bacitracin, c = myoglobin, d = chymotrypsinogen A, e = cytochrom C (reduced), / = ribonuclease A, g = cytochrome C (oxidised), h = lysozyme. The cytochrome C peaks were identified by oxidation with potassium ferricyanide and reduction with sodium dithionite [47]...

Ellis, S. W., Hayhurst, G. P., Smith, G., et al. (1995) Evidence that aspartic acid 301 is a critical substrate-contact residue in the active site of cytochrome P450 2D6. J. Biol. Chem. 270, 29,055-29,058. 

ARH-R, aryl hydrocarbon receptor AROM, cytochrome P450-linked aromatase Asn, asparagine ASNS, asparagine synthetase Asp, aspartate, aspartic acid... 

As already discussed, the model proposed by Tsukihara et alP depends on the so-scalled H-pathway of proton transfer and on the function of an aspartic acid that is not conserved in the bacterial oxidases. This model also depends crucially on the formyl group and on the hydroxyethyl farnesyl side chain of heme a. Many proton-pumping bacterial oxidases, such as cytochrome boj, from E. coll, have replaced heme a with a protoheme (heme B) that lacks both the formyl and the farnesyl side chain. Therefore, this model is restricted to heme a - containing oxidases, and implies different mechanisms of proton translocation in different members of the heme-copper oxidase superfamily. 

Cytochrome c Gold nanoparticle/aspartic acid Conventional aggregates ot core-shell nanoparticles [122]... 

The amino acid analyses in the purest preparations with 0.43% iron gave the results shown in Table II. Cystine, lysine, tyrosine, glutamic and aspartic acids, and leucine were isolated in a pure state from cytochrome c. 

Thiosulfate cyanide sulfurtransferase symmetry in 78 TTiiouridine 234 Three-dimensional structures of aconitase 689 adenylate kinase 655 aldehyde oxido-reductase 891 D-amino acid oxidase 791 a-amylase, pancreatic 607 aspartate aminotransferase 57,135 catalytic intermediates 752 aspartate carbamyltransferase 348 aspartate chemoreceptor 562 bacteriophage P22 66 cadherin 408 calmodulin 317 carbonic acid anhydrase I 679 carboxypeptidase A 64 catalase 853 cholera toxin 333, 546 chymotrypsin 611 citrate synthase 702, 703 cutinase 134 cyclosporin 488 cytochrome c 847 cytochrome c peroxidase 849 dihydrofolate reductase 807 DNA 214, 223,228,229, 241 DNA complex... 

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