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Tracking the function of the cytochrome c6-like protein in higher plants
Authors:Weigel Martin  Pesaresi Paolo  Leister Dario
Institution:1. Molecular Neurogenomics Group, Department of Molecular Genetics, VIB, University of Antwerp, Antwerp 2610, Belgium;2. Neurogenetics Laboratory, Institute Born-Bunge, University of Antwerp, Antwerp 2610, Belgium;3. Neurogenetics Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA;4. Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA;5. Centralized Service Facility, Department of Molecular Genetics, VIB, University of Antwerp, Antwerp 2610, Belgium;6. Department of Biological Sciences, Florida Atlantic University, Jupiter, FL 33458, USA;7. Applied Molecular Genomics Unit, Department of Molecular Genetics, VIB, University of Antwerp, Antwerp 2610, Belgium;8. Neurodegenerative Brain Diseases Group, Department of Molecular Genetics, VIB, University of Antwerp, Antwerp 2610, Belgium;9. Peripheral Neuropathy Group, Department of Molecular Genetics, VIB, University of Antwerp, Antwerp 2610, Belgium;1. Group of Antioxidants, Free Radicals and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry, Cell and Molecular Biology of Plants, Estación Experimental del Zaidín, CSIC, C/ Profesor Albareda, 1, 18008 Granada, Spain
Abstract:The contention that plastocyanin is the only mobile electron donor to photosystem I in higher plants was recently shaken by the discovery of a cytochrome c(6)-like protein in Arabidopsis and other flowering plants. However, the genetic and biochemical data presented in support of the idea that the cytochrome c(6) homologue can replace plastocyanin have now been challenged by two complementary studies. This re-opens the debate on the real function(s) of cytochrome c in the chloroplasts of higher plants.
Keywords:
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