Characterization of the Light-induced Transient States of the Chlorophyll Proteins 668 and 743 from Atriplex rosea
AUTOR(ES)
Hagar, William G.
RESUMO
The light-induced transient states of chlorophyll-protein 668 (Cp668) and its photoconverted from Cp743 were investigated using flash photolysis. Short lived transient species induced by a short flash were detected in both Cp668 and Cp743. The Cp668 transient had a half decay time of 2.0 milliseconds and showed a broad absorption band at 460 nanometers. The Cp743 transient had a half decay time of only 0.6 millisecond and had a major absorption peak at 410 nanometers in addition, to a broad absorption band around 530 nanometers. Both transient signals were quenched by oxygen. Cp668 had a temperature-dependent delayed fluorescence at room temperature with a half-life of 2.0 milliseconds, the same as the life-time of the absorption transient. This suggests that the transient species observed was a triplet state of chlorophyll.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=542992Documentos Relacionados
- Fractionation of Chlorophyll Forms from Euglena and Measurement of Light-Induced Absorbance Changes 12
- Chlorophyll a/b-binding proteins, pigment conversions, and early light-induced proteins in a chlorophyll b-less barley mutant.
- Early light-induced proteins protect Arabidopsis from photooxidative stress
- Ultraviolet light-induced crosslinking of mRNA to proteins.
- Light-Induced Electron-transfer Reactions between Chlorophyll a and Hydrogenated Pteridine Derivatives in Solution
