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Interactions with histidine

Interactions with Histidine. Imidazole lactic acid and imidazole acetic acid were identified as breakdown products when histidine was reacted with methyl linoleate, methyl linoleate hydroperoxide or hexanal for 3 weeks at 25°C and 51°C (33). It was postulated that these compounds were formed via free radical reactions. Two other products were also produced which yielded histidine upon acid hydrolysis. These were thought to be Schiff s base compounds arising... [Pg.98]

Formation of the A-685 was affected by the properties of the polypeptides. When the chi a was incorporated to BSA with THF a predominant formation of A-685 was observed (Fig. 2a). The proportion of this form was kept almost constant irrespective of the concentration of BSA up to 0.3 % (Fig. 5b). On the other hand, when apocatalase was used, a gradual decrease in the proportion of the A-685 was clearly observed (Fig. 5a) with increase in the apocatalase concentration. Apocatalase is known to form tetramer with binding sites for 4 heme molecules in the inner hydrophobic domain. Difference in the properties of polypeptides leads to the idea that chi a in the inner domain is kept as a monomeric form due to absence of the THF H20 THF species and/or due to an interaction with histidine residue(s), which suppresses the formation of the A-685. [Pg.1202]

Quinidine, however, would appear to exhibit a certain degree of structural specificity with respect to its action on the heart [260, 861]. This action would seem to result from a binding to the cardiac cell membranes (possibly through interaction with histidine units [862, 863]) which inhibits the active transport of calcium ions into the cells [864] and so produces the characteristic reduction... [Pg.51]

Much of the available thermodynamic data, snch as bond dissociation energies, gas-phase acidities and basicities, and heats of formation for ions and neutral target species, has been determined nsing TCID [37, 38]. These data inclnde a variety of metals (alkalis, magnesitrm, altrmintrm, and first and second row transition metals), and many types of target molectrles. For instance, Armentront [39] stndied an abso-Inte cation affinity scale, thermochemistry of alkali-metal cation interactions with histidine,and host-gnest interactions of crown ethers with alkali ions nsing TCID. [Pg.29]

Armentrout PB, Citir M, Chen Y, Rodgers MX. Thermochemistry of alkali metal cation interaction with histidine influence of the side chain. J Phys Chem A. 2012 116 11823-32. [Pg.81]

Interactions of histidine and other imidazole derivatives with transition metal ions in chemical and biological systems. R. J. Sundberg and R. B. Martin, Chem. Rev., 1974, 74, 471-517 (517). [Pg.28]

Another example of noncysteinyl coordination of a [4Fe-4S] center was provided by the resolution of the X-ray structure of D. gigas hy-drogenase, which revealed that one iron atom of the distal [4Fe-4S] center was ligated by the atom of a histidine residue (164). Unfortunately, the EPR signature of this center could not be determined because of intercenter spin—spin interactions with other iron—sulfur centers (95). [Pg.457]

Kinetic studies indicated that external H interacted with the renal brush border Na /H exchanger (resistant-type) at a single site with apparent pKa 7.3-7.5. Because the imidazolium ring of histidine is the principal group that is titratable in this... [Pg.250]

A review3 with 57 references discusses the interaction of Ptn and Pd11 with histidine and histidyl containing peptides. The coordinating behavior of histidyl containing peptides towards Pt11 and Pd11 depends on the histidyl position in the peptide sequence. [Pg.556]


See other pages where Interactions with histidine is mentioned: [Pg.29]    [Pg.89]    [Pg.209]    [Pg.96]    [Pg.45]    [Pg.281]    [Pg.138]    [Pg.348]    [Pg.341]    [Pg.256]    [Pg.124]    [Pg.251]    [Pg.66]    [Pg.111]    [Pg.29]    [Pg.89]    [Pg.209]    [Pg.96]    [Pg.45]    [Pg.281]    [Pg.138]    [Pg.348]    [Pg.341]    [Pg.256]    [Pg.124]    [Pg.251]    [Pg.66]    [Pg.111]    [Pg.200]    [Pg.162]    [Pg.482]    [Pg.1225]    [Pg.877]    [Pg.366]    [Pg.34]    [Pg.102]    [Pg.112]    [Pg.363]    [Pg.58]    [Pg.16]    [Pg.40]    [Pg.147]    [Pg.29]    [Pg.96]    [Pg.104]    [Pg.107]    [Pg.757]    [Pg.33]    [Pg.98]    [Pg.148]    [Pg.102]    [Pg.187]    [Pg.61]    [Pg.120]    [Pg.239]   
See also in sourсe #XX -- [ Pg.98 ]




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