A Post Genomic Characterization of Arabidopsis Ferredoxins
Open Access
- 1 January 2004
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 134 (1) , 255-264
- https://doi.org/10.1104/pp.103.032755
Abstract
In higher plant plastids, ferredoxin (Fd) is the unique soluble electron carrier protein located in the stroma. Consequently, a wide variety of essential metabolic and signaling processes depend upon reduction by Fd. The currently available plant genomes of Arabidopsis and rice (Oryza sativa) contain several genes encoding putative Fds, although little is known about the proteins themselves. To establish whether this variety represents redundancy or specialized function, we have recombinantly expressed and purified the four conventional [2Fe-2S] Fd proteins encoded in the Arabidopsis genome and analyzed their physical and functional properties. Two proteins are leaf type Fds, having relatively low redox potentials and supporting a higher photosynthetic activity. One protein is a root type Fd, being more efficiently reduced under nonphotosynthetic conditions and supporting a higher activity of sulfite reduction. A further Fd has a remarkably positive redox potential and so, although redox active, is limited in redox partners to which it can donate electrons. Immunological analysis indicates that all four proteins are expressed in mature leaves. This holistic view demonstrates how varied and essential soluble electron transfer functions in higher plants are fulfilled through a diversity of Fd proteins.Keywords
This publication has 31 references indexed in Scilit:
- Characterization of BphF, a Rieske-Type Ferredoxin with a Low Reduction PotentialBiochemistry, 2000
- Complementary DNA Cloning and Characterization of Ferredoxin Localized in Bundle-Sheath Cells of Maize Leaves1Plant Physiology, 1999
- Photosynthetic and Heterotrophic Ferredoxin Isoproteins Are Colocalized in Fruit Plastids of TomatoPlant Physiology, 1998
- Structure−Function Relationships in Anabaena Ferredoxin: Correlations between X-ray Crystal Structures, Reduction Potentials, and Rate Constants of Electron Transfer to Ferredoxin:NADP+ Reductase for Site-Specific Ferredoxin Mutants,Biochemistry, 1997
- Electrochemical Study of Biological Functions of Particular Evolutionary Conserved Amino Acid Residues Using Mutated Molecules of Maize FerredoxinChemistry Letters, 1997
- Direct electrochemistry and EPR spectroscopy of spinach ferredoxin mutants with modified electron transfer propertiesFEBS Letters, 1995
- An Electron Transport System in Maize Roots for Reactions of Glutamate Synthase and Nitrite ReductasePlant Physiology, 1985
- In vitro synthesis of chloroplast ferredoxin as a high molecular weight precursor in a cell-free protein synthesizing system from wheat germsBiochemical and Biophysical Research Communications, 1978
- Cytochrome c: A Thermodynamic Study of the Relationships among Oxidation State, Ion‐Binding and Structural ParametersEuropean Journal of Biochemistry, 1973
- An electron transport factor from ClostridiumpasteurianumBiochemical and Biophysical Research Communications, 1962