Table 1.
Parameters | ARF | SDX | Rhodobacter sphaeroides Rieske protein fragment | |||
---|---|---|---|---|---|---|
(+−) quadrant | Nδ1a (His44)b | Nδ2a (His64)b | Nδ1a (His44)b | Nδ2a (His64)b | Nδ1a (His131)b | Nδ2a (His152)b |
Q | 2.44 | 2.07 | 2.64 | 2.11 | 2.40 | 2.13 |
G, MHz2 | 13.7 | 16.2 | 13.3 | 16.3 | 13.8 | 15.8 |
a, MHz | 6.5 | 7.9 | 6.0 | 7.8 | 6.6 | 7.6 |
T, MHz | 1.5 | 1.6 | 1.2 | 1.3 | 1.6 | 1.5 |
(++) quadrantc,d | ||||||
gz, MHz | 0.43; 1.03e | 0.3; 1.03e | 0.36; 1.13e | |||
gx, MHz | 0.49; 1.1 | 0.42; 1.04 | 0.43; 1.22 | |||
gy, MHzd | 0.25; 1.22 | 0.31; n.r.f | n.r.f; 1.01 | |||
references | this work | [18] | [21] |
The terminology for 15Nδ1,2 is based on Ref. [18].
In R. sphaeroides cytochrome bc1 complex, the isotropic HF constant of one of two histidine 14Nδ ligands (14aiso ~5MHz; equivalent to 15Nδ2 in Table 1) in the presence of the Qo-site occupant, stigmatellin, is different from the configurations in the presence of myxothiazol, suggesting that the Nδ2, at which the changes identified occur, likely belongs to His152 involved in the interaction with the Qo-site occupants [28]. Tentative assignments of Nδ1,2 in Table 1 are made based on this previous observation in conjunction with the amino acid sequence homology, and should not be taken as definitive.
The positions of the peak maxima in this quadrant were determined with the accuracy ~0.03 MHz.
HYSCORE spectra recorded at the low- and high-field edges near the maximal and minimal g values give “single-crystal-like” patterns from the reduced cluster, whose gz and gx axes are directed along the external magnetic field. In contrast, the resonance condition at the intermediate gy value is fulfilled by many different, yet well-defined orientations.
The relative ESEEM intensity of the largest coupling ~1.03 MHz in 15N-ARF is only ~70% of that of the equivalent couplings in the high-potential protein homologs including SDX (see Fig. 2B).
Not resolved.