In:
The Journal of Chemical Physics, AIP Publishing, Vol. 86, No. 4 ( 1987-02-15), p. 2439-2441
Abstract:
Nonphotochemical holeburning spectroscopy has been used to study a chlorophyllide chromophore substituted for heme in apomyoglobin. The observed holewidths were compared with those found for the same chromophore embedded in the polymeric glass polystyrene. Hole formation occurs with comparable efficiency in the protein and in the polymeric matrix. A T(1.26±0.07) temperature dependence was measured for the pure-dephasing contribution to the homogeneous linewidth for the chromophore in the protein between 1.35 and 2.5 K. This temperature dependence is very similar to that observed for many chromophores is amorphous host matrices. This suggests that the characteristic properties of the matrix responsible for pure dephasing in glasses and in the protein are very similar.
Type of Medium:
Online Resource
ISSN:
0021-9606
,
1089-7690
Language:
English
Publisher:
AIP Publishing
Publication Date:
1987
detail.hit.zdb_id:
3113-6
detail.hit.zdb_id:
1473050-9
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