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Nature Chemical Biology, 2022
Ferredoxins are universal electron donors. A study focusing on the two human mitochondrial ferredoxins reveals the existence of unique cellular functions and partners for each protein.
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Ferredoxins are universal electron donors. A study focusing on the two human mitochondrial ferredoxins reveals the existence of unique cellular functions and partners for each protein.
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The interaction of ferredoxin with chloroplast ferredoxin-linked enzymes
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1986Ferredoxin, reduced by Photosystem I during oxygenic photosynthesis, then serves as the electron donor for the reduction of NADP+ [1], nitrite [2], and the reductive conversion of 2-oxoglutarate plus glutamine to glutamate [3]. Evidence exists thit two of these ferredoxin-dependent reductions, that of NADP+ (catalyzed by ferredoxin:NADP+ oxidoreductase,
M. Hirasawa +4 more
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Interaction of ferredoxin and ferredoxin-NADP reductase with thylakoids
Archives of Biochemistry and Biophysics, 1983Ferredoxin-NADP reductase accounts for about 50% of the NADPH diaphorase activity of spinach leaf homogenates. The enzyme is bound to thylakoid membranes, but can be slowly extracted by aqueous buffers. Ferredoxin-NADP reductase can be extracted from the membranes by a 1- to 2-min treatment with a low concentration of trypsin. This treatment completely
Forti G. +5 more
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Trends in Ecology & Evolution, 1988
Ferredoxins are electron carrier proteins that contain active sites consisting of nonheme iron and inorganic sulfur. They are ubiquitous in living cells and are believed to be among the earliest redox proteins having appeared in primitive organisms. The small size of Ferredoxins allows their amino acid sequences to be determined with relative ease, and
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Ferredoxins are electron carrier proteins that contain active sites consisting of nonheme iron and inorganic sulfur. They are ubiquitous in living cells and are believed to be among the earliest redox proteins having appeared in primitive organisms. The small size of Ferredoxins allows their amino acid sequences to be determined with relative ease, and
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Immobilized ferredoxins for affinity chromatography of ferredoxin-dependent enzymes
Journal of Chromatography A, 1992An immobilized ferredoxin more stable than the conventional immobilized spinach ferrodoxin was prepared by reacting CNBr-Sepharose with ferredoxins isolated from barley and Synechococcus vulcanus, a thermophilic blue-green alga. The dissociation constants of immobilized ferredoxin from spinach, barley and S.
N, Sakihama +5 more
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Photosynthesis Research, 2017
Reduction of ferredoxin by photosystem I (PSI) involves the [4Fe-4S] clusters FA and FB harbored by PsaC, with FB being the direct electron transfer partner of ferredoxin (Fd). Binding of the redox-inactive gallium ferredoxin to PSI was investigated by flash-absorption spectroscopy, studying both the P700+ decay and the reduction of the native iron Fd ...
Mignée, Clara +4 more
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Reduction of ferredoxin by photosystem I (PSI) involves the [4Fe-4S] clusters FA and FB harbored by PsaC, with FB being the direct electron transfer partner of ferredoxin (Fd). Binding of the redox-inactive gallium ferredoxin to PSI was investigated by flash-absorption spectroscopy, studying both the P700+ decay and the reduction of the native iron Fd ...
Mignée, Clara +4 more
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Interaction of ferredoxin-linked nitrite reductase with ferredoxin
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985Abstract The native, ferredoxin-linked, form ( M r = 85 000) of nitrite reductase (ferredoxin:nitrite oxidoreductase, EC 1.7.7.1) forms a complex with ferredoxin that can be detected either by enzyme binding to a ferredoxin-Sepharose 4B affinity column or by spectral changes produced when the two proteins are mixed.
Masakazu Hirasawa, David B. Knaff
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The Interaction of Ferredoxin with Ferredoxin-Dependent Enzymes
2007Summary Ferredoxin, reduced by Photosystem I (PS I) in the light, serves as the electron donor for the reduction of NADP + to NADPH, of sulfite to sulfide, of nitrite to ammonia and for the reductant-requiring of glutamate and 2-oxoglutarate to glutamate in all oxygenic photosynthetic organisms.
Toshiharu Hase +2 more
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The reconstitution of clostridial ferredoxin
Biochemical and Biophysical Research Communications, 1966Previous experiments from this laboratory (Lovenberg, et al., 1963; Malkin & Rabinowitz, 1966) indicated that when bacterial ferredoxin is treated with a mercurial, the color of the protein is bleached, and both the iron and the acidlabile sulfide of the protein are released.
R, Malkin, J C, Rabinowitz
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Ferredoxin and Photosynthetic Phosphorylation
Nature, 1967The iron-bearing protein ferredoxin is present in all photosynthetlc cells. It has now been shown that ferredoxin can catalyse, by two distinct photochemical reactions, the production of ATP in cell-free photosynthetic systems at rates comparable with the maximum rates of photosynthesis in vivo.
D I, Arnon, H Y, Tsujimoto, B D, McSwain
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