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MCD magnetization plots

Figure 4. MCD magnetization plots for (a) oxidized and (b) partially reduced Thermus thermophilus ferredoxin. Data collected at 1.55 K (x), 4.22 K (A), and 9-100 K ( ), with magnetic fields between 0 and 4.5 T. Figure 4. MCD magnetization plots for (a) oxidized and (b) partially reduced Thermus thermophilus ferredoxin. Data collected at 1.55 K (x), 4.22 K (A), and 9-100 K ( ), with magnetic fields between 0 and 4.5 T.
Figure 7. MCD magnetization plots for thionine-oxidized Av at 800 nm (a) and thionine oxidized AvV at 760 nm (b). Magnetic fields between 0 and 4.S T. Modified from Ref. 8. Figure 7. MCD magnetization plots for thionine-oxidized Av at 800 nm (a) and thionine oxidized AvV at 760 nm (b). Magnetic fields between 0 and 4.S T. Modified from Ref. 8.
Fig. 6.15 MCD spectrum of [Co2(C02EtH2Ll)(CH3COO)2](PF6) as solid mull at 1.5 K and 7.0 T. Gaussian deconvolved spectrum is identical with the recorded spectrum except for noise. On the right magnetization plots fiom VTVH analysis of the bands at 506 and 530 nm... Fig. 6.15 MCD spectrum of [Co2(C02EtH2Ll)(CH3COO)2](PF6) as solid mull at 1.5 K and 7.0 T. Gaussian deconvolved spectrum is identical with the recorded spectrum except for noise. On the right magnetization plots fiom VTVH analysis of the bands at 506 and 530 nm...
Fig. 6.32 Gaussian deconvoluted ethanol MCD spectium of [Co2(C02EtH2Ll)(CH3COO)2]" in the presence of one equivalent penicillin. The spectrum was recorded 1 h after mixing and subsequent incubation at 40 °C. On the right magnetization plots obtained after VTVH analysis at 1.5,3,6, 12,25 and 50 K of two selected transitions (499 and 517 nm). For clarity the plots for 12, 25 and 50 K have been omitted... Fig. 6.32 Gaussian deconvoluted ethanol MCD spectium of [Co2(C02EtH2Ll)(CH3COO)2]" in the presence of one equivalent penicillin. The spectrum was recorded 1 h after mixing and subsequent incubation at 40 °C. On the right magnetization plots obtained after VTVH analysis at 1.5,3,6, 12,25 and 50 K of two selected transitions (499 and 517 nm). For clarity the plots for 12, 25 and 50 K have been omitted...
Mathematically, the magnetic g values for the state involved in the electronic transitions are directly related to the ratios Aj/Dq and Cq/Dq. Plotting As vs H/2kT (this graph is called an MCD magnetization curve) permits the determination of the magnetic properties (g values) of the ground and excited states, Cq and Aj. Although the values determined in this manner are not as precise as those obtained... [Pg.60]

Inspection of the temperature dependence of the MCD bands of the oxidized and reduced [3Fe-4S] center in T. thermophilus ferredoxin, see Figure 3, reveals that the reduced cluster magnetizes more rapidly with decreasing temperature. This is shown more clearly in the magnetization data, which are shown as plots of MCD intensity, in the form of a percentage of that estimated... [Pg.333]

FIGURE 1.10 Panel (a) shows the effect of ZFS (left side) and application of a magnetic field in three molecular directions on the spin states giving rise to the observed saturation magnetization behavior (VTVH MCD) plotted in panel (b) for a S = 5/2, D> 0, and EID = 1/3 Kramers ion. [Pg.15]

FIGURE 1.12 VTVH MCD for a non-Kramers 5 = 2 system with rhombic distortion. Panel (a) plots the data as a function of f)H/2kT and panel (b) as a function of HkT. The inset shows the effect of ZFS and a magnetic field on the Ms = 2 ground-state wavefunction.30... [Pg.17]

Fig. 12. Magnetization behavior for resting metapyrocatechase. (A) MCD amplitude at 890 nm for a range of applied magnetic field strengths (0-5.9 T) at a series of fixed temperatures plotted as a function of pHI2kT. (B) Replot of saturation data shown in (A) as a function of temperature at fixed fields. Solid curves represent the fit to the data for an isolated non-Kramers doublet with rhombic zero field splitting [Eq. (20)]. Fig. 12. Magnetization behavior for resting metapyrocatechase. (A) MCD amplitude at 890 nm for a range of applied magnetic field strengths (0-5.9 T) at a series of fixed temperatures plotted as a function of pHI2kT. (B) Replot of saturation data shown in (A) as a function of temperature at fixed fields. Solid curves represent the fit to the data for an isolated non-Kramers doublet with rhombic zero field splitting [Eq. (20)].
Fig. 17. Saturation-magnetization behavior for (A) native metapyrocatechase at 890 nm, (B) anaerobic metapyrocatechase-catechol complex at 750 nm, and (C) anaerobic metapyro-catechase-catechol-azide complex at 680 nm. The MCD intensity amplitude for a range of magnetic fields (0-5.9 T) at a series of fixed temperatures is plotted as a function of fiHI IkT. The insets show MCD spectra at 4.2 K and 5.9 T of resting metapyrocatechase, its substrate complex, and the enzyme-substrate-azide complex. Fig. 17. Saturation-magnetization behavior for (A) native metapyrocatechase at 890 nm, (B) anaerobic metapyrocatechase-catechol complex at 750 nm, and (C) anaerobic metapyro-catechase-catechol-azide complex at 680 nm. The MCD intensity amplitude for a range of magnetic fields (0-5.9 T) at a series of fixed temperatures is plotted as a function of fiHI IkT. The insets show MCD spectra at 4.2 K and 5.9 T of resting metapyrocatechase, its substrate complex, and the enzyme-substrate-azide complex.

See other pages where MCD magnetization plots is mentioned: [Pg.328]    [Pg.328]    [Pg.328]    [Pg.335]    [Pg.339]    [Pg.213]    [Pg.174]    [Pg.477]    [Pg.106]    [Pg.14]    [Pg.17]    [Pg.357]    [Pg.154]    [Pg.90]    [Pg.48]    [Pg.98]    [Pg.132]    [Pg.299]    [Pg.154]    [Pg.1548]   
See also in sourсe #XX -- [ Pg.335 , Pg.336 , Pg.339 , Pg.340 , Pg.341 ]




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