Abstract

The overall goal of this research is to study the mechanism of light energy transduction in visual pigments and related pigments using resonance Raman spectroscopy. This technique is a very powerful one to probe the structure and changes in structure of the visual pigment retinal chromophore that accompany the early stages of vision. The ultimate goal is to understand from a molecular viewpoint how light energy is converted to what chemistry that is called visual transduction. Transduction processes are important problems in biology, and a molecular understanding of the visual system is an important step. Three main areas of study are envisioned. Experiments are planned to elucidate the nature of the chromophoric site. The structure of the primary photoproducts are to be measured so as to understand how light energy is converted to chemical energy. Lastly, dark intermediates and reaction pathways are to be probed to help elucidate how this chemical energy is used.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Eye Institute (NEI)
Type
Research Project (R01)
Project #
2R01EY003142-09
Application #
3257396
Study Section
Biophysics and Biophysical Chemistry A Study Section (BBCA)
Project Start
1979-07-01
Project End
1992-06-30
Budget Start
1987-07-01
Budget End
1988-06-30
Support Year
9
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
City College of New York
Department
Type
Schools of Arts and Sciences
DUNS #
603503991
City
New York
State
NY
Country
United States
Zip Code
10031

  Publications

Huang, L; Deng, H; Koutalos, Y et al. (1997) A resonance Raman study of the C=C stretch modes in bovine and octopus visual pigments with isotopically labeled retinal chromophores. Photochem Photobiol 66:747-54
Huang, L; Deng, H; Weng, G et al. (1996) A resonance Raman study of the C=N configurations of octopus rhodopsin, bathorhodopsin, and isorhodopsin. Biochemistry 35:8504-10
Deng, H; Huang, L; Callender, R et al. (1994) Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: a resonance Raman study of the Schiff base hydrogen/deuterium exchange. Biophys J 66:1129-36
Callender, R; Deng, H (1994) Nonresonance Raman difference spectroscopy: a general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules. Annu Rev Biophys Biomol Struct 23:215-45
Weng, G; Chen, C X; Balogh-Nair, V et al. (1994) Hydrogen bond interactions of G proteins with the guanine ring moiety of guanine nucleotides. Protein Sci 3:22-9
Manor, D; Callender, R; Noy, N (1993) The interactions of retinoids with retinol-binding protein. A resonance Raman spectroscopic study. Eur J Biochem 213:413-8
Deng, H; Manor, D; Weng, G et al. (1991) Resonance Raman studies of the HOOP modes in octopus bathorhodopsin with deuterium-labeled retinal chromophores. Biochemistry 30:4495-502
Deng, H; Manor, D; Weng, G et al. (1991) A resonance Raman study of octopus bathorhodopsin with deuterium labeled retinal chromophores. Photochem Photobiol 54:1001-7
Pande, J; McDermott, M J; Callender, R H et al. (1991) The calf gamma crystallins--a Raman spectroscopic study. Exp Eye Res 52:193-7
Yan, M; Manor, D; Weng, G et al. (1991) Ultrafast spectroscopy of the visual pigment rhodopsin. Proc Natl Acad Sci U S A 88:9809-12

Showing the most recent 10 out of 22 publications