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Metalloprotein hyperfine interaction

In any metalloprotein, be it tumbling in water or fixed in a frozen solution, not only the Zeeman interaction but also the hyperfine interaction will be anisotropic, so the resonance held in Equation 5.10 becomes a function of molecular orientation in the external held (or alternatively of the orientation of B in the molecular axes system) ... [Pg.76]

Electron nuclear double resonance (ENDOR) and electron spin-echo envelope modulation (ESEEM) are two of a variety of pulsed EPR techniques that are used to study paramagnetic metal centers in metalloenzymes. The techniques are discussed in Chapter 4 of reference la and will not be discussed in any detail here. The techniques can define electron-nuclear hyperfine interactions too small to be resolved within the natural width of the EPR line. For instance, as a paramagnetic transition metal center in a metalloprotein interacts with magnetic nuclei such as H, H, P, or these... [Pg.129]

Chapter 3 by Hiittermann and Kappl presents detailed strategies for the analysis of CW- and pulsed-ENDOR spectroscopy from Fe-S proteins. ENDOR is by now a well-known high-resolution technique ideal for resolving small interactions between unpaired electrons and metal nuclei or with nuclei in the coordination sphere that cannot be resolved using CW-EPR. It provides important information to characterize the functional, structural, and electronic properties of paramagnetic centers found in metalloproteins. It complements ESEEM and HYSCORE methods, which are more suited to determining hyperfine interactions from distant ligand nuclei. [Pg.680]

The different appearance of the S-band multiline signal can be attributed to at least two effects. First, as for many metalloprotein signals, the resolution was lower at X-band because of g-strain broadening, which is proportional to frequency. Second, spin interactions that are smaller than the dominating Zeeman interaction become more apparent at lower frequency, thereby shifting line positions slightly this is particularly true of second order hyperfine coupling, which is inversely proportional to frequency. [Pg.778]


See other pages where Metalloprotein hyperfine interaction is mentioned: [Pg.204]    [Pg.93]    [Pg.109]    [Pg.8]    [Pg.6213]    [Pg.121]    [Pg.6212]    [Pg.555]    [Pg.51]    [Pg.249]    [Pg.88]    [Pg.65]    [Pg.67]    [Pg.100]    [Pg.78]    [Pg.138]    [Pg.63]    [Pg.198]   
See also in sourсe #XX -- [ Pg.76 ]




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