1887
banner image
No data available.
Please log in to see this content.
You have no subscription access to this content.
No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.
Calculation of the circular dichroism spectra of carbon monoxy- and deoxy myoglobin: Interpretation of a time-resolved circular dichroism experiment
Rent:
Rent this article for
USD
10.1063/1.2041467
/content/aip/journal/jcp/123/18/10.1063/1.2041467
http://aip.metastore.ingenta.com/content/aip/journal/jcp/123/18/10.1063/1.2041467

Figures

Image of FIG. 1.
FIG. 1.

Circular dichroism for nm (close to the MbCO peak) and nm (close to the Mb peak) as a function of the pump-probe delay. The CD curves are fitted by two exponential functions (7 and 43 psec). The inset shows the corresponding normalized transmission curves.

Image of FIG. 2.
FIG. 2.

(a) Sketch of the main aminoacids involved in the CD signal. The residues yielding a positive (resp. negative) rotational strength are drawn in blue (resp. red). The proximal histidine (His93) is singled out due to its particular role: it induces the lifting of the degeneracy of the heme transitions but contributes very little to the rotational strength. His36, His97, Phe46, and Trp7 which are considered in the calculation are not represented because of their weak contribution to the rotational strength. (b) Sketch of the residues with their coordinate axes.

Image of FIG. 3.
FIG. 3.

Absorption spectra for (a) MbCO and (b) Mb; CD spectra for (c) MbCO and (d) Mb. The red solid lines are experimental spectra and the black dashed lines are calculated ones.

Image of FIG. 4.
FIG. 4.

Calculated spectra for MbCO and Mb and for two intermediate configurations (see text).

Image of FIG. 5.
FIG. 5.

Sketch of the electronic levels for the heme and His93 and the normal modes resulting from their coupling. The two low-lying normal modes have rotational strengths of opposite signs.

Image of FIG. 6.
FIG. 6.

Calculated CD spectra for a mixing of 80% MbCO and 20% for an isotropic distribution (blue dashed line) and a pump-induced anisotropy (red solid line).

Image of FIG. 7.
FIG. 7.

Histogram of the calculated variation of the contribution of the residues to the rotational strength of the high-energy band when passing from (red) and from (blue). See text for the definition of the intermediate structures.

Tables

Generic image for table
Table I.

Energy, oscillator strength, and polarization of the electronic transitions of the aromatic pending groups. The polarization is expressed as the angle (in degrees) between the transition moment and the axis (see Fig. 2).

Generic image for table
Table II.

Calculation of the contributions of the transitions of individual residues to the rotational strength of the heme in the Soret band for MbCO and Mb.

Generic image for table
Table III.

Calculation of the contributions of the transitions of individual residues to the rotational strength (in DBM) of the heme in the high-energy band of Mb, , and (see text).

Loading

Article metrics loading...

/content/aip/journal/jcp/123/18/10.1063/1.2041467
2005-11-04
2014-04-25
Loading

Full text loading...

This is a required field
Please enter a valid email address
752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
Scitation: Calculation of the circular dichroism spectra of carbon monoxy- and deoxy myoglobin: Interpretation of a time-resolved circular dichroism experiment
http://aip.metastore.ingenta.com/content/aip/journal/jcp/123/18/10.1063/1.2041467
10.1063/1.2041467
SEARCH_EXPAND_ITEM