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Oxygen glutamate

Monosodium L-glutamate [142-47-2] C HgNO Na H20 (mol wt 187.13) crystallizes from aqueous solution at room temperature as rhombic prisms. Its stmcture, as deterrnined by x-ray crystallography (6), indicates that the sodium ions are coordinated octahedraHy by four (3a and ly) carboxyl oxygen atoms and two water molecules as follows ... [Pg.303]

Figure 1.9 Examples of functionally important intrinsic metal atoms in proteins, (a) The di-iron center of the enzyme ribonucleotide reductase. Two iron atoms form a redox center that produces a free radical in a nearby tyrosine side chain. The iron atoms are bridged by a glutamic acid residue and a negatively charged oxygen atom called a p-oxo bridge. The coordination of the iron atoms is completed by histidine, aspartic acid, and glutamic acid side chains as well as water molecules, (b) The catalytically active zinc atom in the enzyme alcohol dehydrogenase. The zinc atom is coordinated to the protein by one histidine and two cysteine side chains. During catalysis zinc binds an alcohol molecule in a suitable position for hydride transfer to the coenzyme moiety, a nicotinamide, [(a) Adapted from P. Nordlund et al., Nature 345 593-598, 1990.)... Figure 1.9 Examples of functionally important intrinsic metal atoms in proteins, (a) The di-iron center of the enzyme ribonucleotide reductase. Two iron atoms form a redox center that produces a free radical in a nearby tyrosine side chain. The iron atoms are bridged by a glutamic acid residue and a negatively charged oxygen atom called a p-oxo bridge. The coordination of the iron atoms is completed by histidine, aspartic acid, and glutamic acid side chains as well as water molecules, (b) The catalytically active zinc atom in the enzyme alcohol dehydrogenase. The zinc atom is coordinated to the protein by one histidine and two cysteine side chains. During catalysis zinc binds an alcohol molecule in a suitable position for hydride transfer to the coenzyme moiety, a nicotinamide, [(a) Adapted from P. Nordlund et al., Nature 345 593-598, 1990.)...
FIGURE 19.18 Sickle-shaped red blood cells form when only one amino acid (glutamic acid) in a polypeptide chain is replaced by another amino acid (valine). These cells are less able to take up oxygen than normal cells. [Pg.890]

Decreased cerebral blood flow, resulting from acute arterial occlusion, reduces oxygen and glucose delivery to brain tissue with subsequent lactic acid production, blood-brain barrier breakdown, inflammation, sodium and calcium pump dysfunction, glutamate release, intracellular calcium influx, free-radical generation, and finally membrane and nucleic acid breakdown and cell death. The degree of cerebral blood flow reduction following arterial occlusion is not uniform. Tissue at the... [Pg.39]

Fig. 13. The binding sites of calcium in (a) parvalbumin (41a), (b) annexin (41) and (c) calmodulin (42). The drawings show two bidentate carboxylates coordinated to Ca2 in the EF-hand site of parvalbumin, and one bidentate carboxylate coordinated to Ca2 in annexin and calmodulin. All the donor atoms coordinated to the calciums are oxygen donor atoms from carboxylates of asp = aspartate, or glu = glutamate, or else peptide carbonyl oxygens from gly = glycine or met = methionine. Redrawn after Refs. (41-42). Fig. 13. The binding sites of calcium in (a) parvalbumin (41a), (b) annexin (41) and (c) calmodulin (42). The drawings show two bidentate carboxylates coordinated to Ca2 in the EF-hand site of parvalbumin, and one bidentate carboxylate coordinated to Ca2 in annexin and calmodulin. All the donor atoms coordinated to the calciums are oxygen donor atoms from carboxylates of asp = aspartate, or glu = glutamate, or else peptide carbonyl oxygens from gly = glycine or met = methionine. Redrawn after Refs. (41-42).
Fig. 2. Possible structures for a diiron(III) peroxide unit in the peroxo intermediate consistent with available Raman and Mossbauer spectroscopic data. The symbols N and 0 designate nitrogen and oxygen donor atoms of histidine and glutamate residues, respectively. Some of the latter must be bidentate to fill the coordination spheres. Fig. 2. Possible structures for a diiron(III) peroxide unit in the peroxo intermediate consistent with available Raman and Mossbauer spectroscopic data. The symbols N and 0 designate nitrogen and oxygen donor atoms of histidine and glutamate residues, respectively. Some of the latter must be bidentate to fill the coordination spheres.
Once the initial event occurs, secondary events occur at the cellular level that contribute to cell death. Regardless of the specific initiating event, the cellular processes that follow may be similar. Excitatory amino acids such as glutamate accumulate within the cells, causing intracellular calcium accumulation. Inflammation occurs and oxygen free radicals are formed ending in the common pathway of cell death. [Pg.163]


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