Static Normal Coordinate Deformations of the Heme Group in Mutants of FerrocytochromecfromSaccharomycescerevisiaeProbed by Resonance Raman Spectroscopy

2007 ◽  
Vol 111 (23) ◽  
pp. 6527-6533 ◽  
Author(s):  
Reinhard Schweitzer-Stenner ◽  
Qing Huang ◽  
Andrew Hagarman ◽  
Monique Laberge ◽  
Wallace
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Heme Group ◽  
Normal Coordinate

Resonance Raman Study of the Binding of the Anticancer Drug Amsacrine to DNA

1994 ◽  
Vol 48 (7) ◽  
pp. 822-826 ◽  
Author(s):  
Catherine A. Butler ◽  
Ralph P. Cooney ◽  
William A. Denny
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Binding Mode ◽  
Resonance Raman Spectrum ◽  
Normal Coordinate ◽  
Visible Absorption ◽  
Calf Thymus ◽  
Raman Study ◽  
Uv Visible

The binding of amsacrine [4′-(9-acridinylamino)methanesulfon- m-anisidide] to calf thymus DNA was studied by UV-visible and resonance Raman spectroscopy. A shift of the UV-visible absorption band of amsacrine at 434 to 442 nm together with a decrease in the intensity of this band is observed upon amsacrine-DNA binding. The resonance Raman spectrum of DNA-bound amsacrine shows a general slight decrease in intensity relative to the spectrum of the free species. The significant decrease in intensity of the bands at 1165, 1265, and 1380 cm−1 upon binding to DNA is attributed to the formation of a single amsacrine-DNA species. The assignment of these bands (1165, 1265, and 1380 cm−1), which was based upon a previous normal coordinate analysis (NCA) and molecular neglect of diatomic overlap (MNDO) calculation, and the observed lack of shift in the band positions upon binding are consistent with intercalation being the major binding mode of amsacrine, as inferred previously by other techniques.

Out-of-plane deformations of the heme group in different ferrocytochrome c proteins probed by resonance Raman spectroscopy

2008 ◽  
Vol 39 (12) ◽  
pp. 1848-1858 ◽  
Author(s):  
Andrew Hagarman ◽  
Carmichael J. Wallace ◽  
Monique M. Laberge ◽  
Reinhard Schweitzer-Stenner
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Heme Group ◽  
Ferrocytochrome C ◽  
Out Of Plane ◽  
C Proteins ◽  
Plane Deformations

Deformations of the Heme Group of Different Ferrocytochrome c Proteins Probed by Resonance Raman Spectroscopy

2008 ◽  
Author(s):  
Andrew Hagarman ◽  
Carmichael Wallace ◽  
Monique Laberge ◽  
Reinhard Schweitzer-Stenner ◽  
V. K. Vaidyan ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Heme Group ◽  
Ferrocytochrome C ◽  
C Proteins

scholarly journals Structure of the retinal chromophore in sensory rhodopsin I from resonance Raman spectroscopy

1989 ◽  
Vol 264 (31) ◽  
pp. 18280-18283
Author(s):  
S P Fodor ◽  
R Gebhard ◽  
J Lugtenburg ◽  
R A Bogomolni ◽  
R A Mathies
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Sensory Rhodopsin ◽  
Retinal Chromophore ◽  
Sensory Rhodopsin I
Sign in / Sign up

Export Citation Format

Share Document