Vibrational stark spectroscopy in proteins: A probe and calibration for electrostatic fields

Journal of Physical Chemistry B

Volumn 103, Issue 45, 1999, Pages 9813-9817

  Park, Eun Sun ^a   Andrews, Steven S ^a   Hu, Robert B ^a   Boxer, Steven G ^a  

^a STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0001257322     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp992329g     Document Type: Article

References (51)

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29. matrix. The local field correction f is in general a tensor quantity; it is treated here as a scalar and the value of f should be somewhat greater than 1 (see text). Due to uncertainty in the value of f we report the observed values of |Δ divided by /. For example, see: Böttcher, C. J. F. Theory of Electric Polarization; Elsevier: Amsterdam, 1973; Vol. 1.
30. 28
31. The Stark spectra are dominated by the second derivative contribution with a small first derivative contribution, and there is no measurable
32. contribution from the zeroth derivative. Numerical derivatives were usually obtained after smoothing the absorption spectrum. Complications arise if the absorption bands contain multiple peaks, as the line shapes of the different absorption bands need to be known accurately to get the individual values of |Δμ| and [Δα|. The separation of the peaks in the absorption spectrum was performed by fitting the peaks with a sum of Lorentzians and Gaussians and their analytical derivatives were used in the analysis of the Stark data.
33. Iron(II) α,α,α-tris(o-(2,2,-dimethylpropionamido)phenyl)-β-(o-3-
34. (3-pyridyl)-propionamidophenyl)-porphyrin. This compound was prepared by the general synthetic procedure described for the chloroacetyl-picket fence porphyrin analogue. For example, see: Collman, J. P.; Broring, M.; Fu, L.; Rapta, M.; Schwenninger, R.; Straumanis, A. J. Org. Chem. 1998, 23, 8082.
35. Wild-type horse heart cytochrome c was purchased from Sigma Chemical Co. The CO adduct was prepared as described in ref 27. The final sample contained ∼3 mM cytochrome c in 50/50 glycerol/buffer (100 mM phosphate buffer, pH 7.0).
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40. - bound to Fe(III)Mb.
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49. We have found that |Δμ| for NO bound to heme iron is similar to that for bound CO (Park and Boxer, to be published). Therefore, observed variations in VNO can also be interpreted quantitatively as electrochromic band shifts. Because the VSE spectrum is obtained as a difference between field on and field off, it can often be observed despite a large background absorbance.
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51. ext between 0.3 and 0.9 MV/cm, as expected from eq 1.