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L with such water molecules will not contribute since such bonding is not commensurate with the vibrational data on wt RCs or the G(M201)D mutant (at least when P is neutral).
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0011250502
-
-
note
-
Because the data extend to only 3.8 ns and this at best is about four 1/e times of the slower component, the error in the associated time constant for the longer-lived component in the anion region and P-bleaching decay is much larger than indicated by simple best fits (1.0 ± 0.4 ns and 1.2 ± 0.4 ns, respectively). For example, in the anion region, holding the slow component fixed at 1.5, 2.0, 2.5, or 3.0 ns gives visually good fits to the gion data in Figure 6, with the value of the faster time constant only marginally changed. The use of time constants longer than about 4 ns for the slow component gives poorer fits and unreasonable spectra at the asymptote of the decay. These considerations suggest that the time constant of the slower component is likely in the 1-4 ns range. This behavior parallels that previously observed for the DH and KDH mutants.
-
-
-
-
52
-
-
0011198741
-
-
note
-
- formation (Figure 2B).
-
-
-
-
53
-
-
0011214760
-
-
note
-
(a) The amplitude spectra in Figure 7 were generated from fits in which the value of the longer component was held fixed at 2.5 ns. Varying this time constant between 1.0 and 3.5 ns does not appreciably affect the derived spectra.
-
-
-
-
54
-
-
0011227950
-
-
note
-
+.
-
-
-
-
55
-
-
0011237168
-
-
note
-
-1; not shown).
-
-
-
-
56
-
-
0011175408
-
-
note
-
Y excited states of the chromophores (via origin shifts and/or dephasing times of certain modes). These particular excited-state properties are outside the scope of this paper. Inspection of the RR data shown in Figures 8 and 9 clearly shows that the RR intensities of the V(M131)D versus wild-type RCs are different at a given excitation wavelength. This observation is similar to that made in previous RR studies of genetically modified RCs. These studies have shown that the RR intensities of the cofactors can be significantly affected by altering protein residues in the vicinity of a particular cofactor, even in cases when the genetic modification does not affect the ground-state absorption features or vibrational frequencies of the cofactor to any appreciable extent.
-
-
-
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57
-
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0025004006
-
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Peloquin, J.M.; Bylina, E.J.; Youvan, D.C.; Bocian, D.F. Biochemistry 1990, 29, 8417-8424.
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-
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0011211375
-
-
note
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- occurs in the Rb. sphaeroides DH mutant but with a yield of only ∼7%, half that found in the Rb. capsulatus DH mutant.
-
-
-
-
59
-
-
0011228114
-
-
note
-
M has been replaced by a BPh, an Rb. capsulatus mutant involving alterations/ swapping of large sections of the L and M polypeptides, and Rb. capsulatus wild-type RCs at low temperature at high excitation intensities.
-
-
-
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60
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0001583619
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0011250504
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Calculations on hydrogen bonding to the ring V keto group of a BPh and experimental results on manipulation of hydrogen bonds to P indicate that these hydrogen bonds generally shift the redox properties of the cofactors by 50-80 mV.
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