Photooxidation of the high-potential iron—sulfur center in chloroplasts
AUTOR(ES)
Whitmarsh, John
RESUMO
The high-potential iron—sulfur center associated with the g = 1.89-1.90 electron paramagnetic resonance signal in spinach chloroplasts is fully reduced in the dark. It is photooxidized in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea and reduced after illumination with red actinic light in the absence of inhibitors. The light-induced redox changes of the high-potential iron—sulfur center are shown to correlate with those of plastocyanin detected at g = 2.05. Demonstration of light-induced redox changes in the high-potential iron—sulfur center provides support for a functional role of this component in the chloroplast electron transport chain.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=411586Documentos Relacionados
- Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: Thermostability and electron transfer
- Kinetics of photo-induced electron transfer from high-potential iron-sulfur protein to the photosynthetic reaction center of the purple phototroph Rhodoferax fermentans.
- Gene Cluster of Rhodothermus marinus High-Potential Iron-Sulfur Protein:Oxygen Oxidoreductase, a caa3-Type Oxidase Belonging to the Superfamily of Heme-Copper Oxidases
- Identification of the iron-sulfur center in trimethylamine dehydrogenase.
- Formation of the iron-sulfur cluster of ferredoxin in isolated chloroplasts