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Superoxide dismutase resonance

Familial amyotrophic lateral sclerosis, superoxide dismutase and, 45 148 Fano resonance, 35 349-350 Fast atom bombardment mass spectrometry, heteronuclear gold cluster compounds, 39 340-342... [Pg.99]

Cass, A. E. G., Hill, H. A. O. Anion binding to copper(I) superoxide dismutase A high resolution H nuclear magnetic resonance spectroscopic study. In Chemical and Biochemical Aspects of Superoxide and Superoxide Dismutase (Bannister, J. V., Hill, H. A, O., eds.). New York-Amsterdam-Oxford, Elsevier/North-Holland, 1980, pp. 290-298... [Pg.29]

In the case of cobalt substituted Zn-fingers [102], the differences between the chemical shifts for corresponding resonances in the Co(II) and Zn(II) complexes allow the determination of the orientation and anisotropy of the magnetic susceptibility tensor [103]. Similar studies are available for pseudotetrahedral Co(II) in the zinc site of superoxide dismutase [104] and five coordinated carbonic anhydrase derivatives [105]. [Pg.173]

Fig. 9.10. (A) 200 MHz H NMR spectrum of copper-depleted, cobalt-substituted Cu,Zn superoxide dismutase (B) difference between the difference NOE spectra obtained by irradiating signals D and C, respectively. The spectra demonstrate that the NOE on E arises from D and not from C. The off-resonance position was placed symmetrical with respect to E in both cases [41]. Fig. 9.10. (A) 200 MHz H NMR spectrum of copper-depleted, cobalt-substituted Cu,Zn superoxide dismutase (B) difference between the difference NOE spectra obtained by irradiating signals D and C, respectively. The spectra demonstrate that the NOE on E arises from D and not from C. The off-resonance position was placed symmetrical with respect to E in both cases [41].
Copper, silver and gold - The paramagnetism of Cu11 has limited the use of NMR for the direct study of copper complexes, but information is readily obtained from studies of ligand nuclei. For example, the broadening of the NMR signal by copper in copper-zinc and copper-cobalt superoxide dismutases (SODs) has been used to determine the distance between the copper and the proton on bound formate (Sette et al., 1992). Also, broadening of the formate 13C NMR resonance reveals information about the orientation of the formate. [Pg.46]

As would be expected, several additional applications of cryoprobe technology in the area of biomacromolecular NMR were also published. Goger et al,253 described the reduction in time required for the acquisition of triple resonance NMR experiments performed on proteins. Later in the year, Craik et al.254 reported a study of the 21 amino acid bacterial peptide microcin J25 that relied on cryoprobe technology. In late 2003, Bertini and co-workers255 reported the application of cryoprobe-based 13C direct-detection NMR experiments on a paramagnetic oxidized superoxide dismutase. [Pg.84]

BH4 = Tetrahydrobiopterin CAM = Cytotoxic activated macrophage cNOS = Constitutive nitric oxide synthase CPR = Cytochrome P450 reductase EDRF = Endothelial-derived relaxation factor EPR = Electron paramagnetic resonance spectroscopy IL-1 = Interleukin-1 iNOS = Inducible nitric oxide synthase EPS = Lipopolysaccharide, or endotoxin NMMA = ISp-monomethyl-L-arginine NOS = Nitric oxide synthase ROS = Reactive oxygen species SOD = Superoxide dismutase TNF = Tumor necrosis factor. [Pg.2985]

M26. Misra, H. P., Inhibition of superoxide dismutase by nitroprusside and electron spin resonance observations on the formation of a superoxide-mediated nitroprusside nitroxyl free radical. J. [Pg.55]

Two rather unusual assays have been developed for superoxide dismutase. Both these assays do not reflect the catalytic activity of the enzyme. The first assay utilizes the unique effect of the metal centers on the relaxation rate of F nucleus of fluoride which can be monitored by nuclear magnetic resonance, whereas the second assay is based on the antigenicity of the proteins. [Pg.301]


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See also in sourсe #XX -- [ Pg.291 ]




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Superoxide dismutase nuclear magnetic resonance

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