Role of Ferredoxin 1 <i>(FDX1)</i> in cancer and its therapeutic potential. [PDF]
He F +7 more
europepmc +1 more source
Mutations in mitochondrial ferredoxin FDX2 suppress frataxin deficiency. [PDF]
Meisel JD +10 more
europepmc +1 more source
Rerouting reductant flux via protein tethering enhances biohydrogen production in Thermococcus kodakarensis. [PDF]
Williams SA +6 more
europepmc +1 more source
Impact of SliP4 deletion on the high-light acclimation in Synechocystis sp. PCC 6803. [PDF]
Alvarenga-Lucius L +5 more
europepmc +1 more source
Regulating ferredoxin electron transfer using nanobody and antigen interactions
Albert Truong, Jonathan J. Silberg
openalex +2 more sources
Engineering of Integral Membrane Metalloenzyme UndB and Designing of a Cell-Free Biocatalytic Platform Enabled Efficient 1‑Alkene Production. [PDF]
Iqbal T +4 more
europepmc +1 more source
Changes in the nitrate assimilation pathway serve as a component of maize stress response to competition cues. [PDF]
Kramer W +3 more
europepmc +1 more source
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The interaction of ferredoxin with chloroplast ferredoxin-linked enzymes
Biochimica Et Biophysica Acta - 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-linked nitrite reductase with ferredoxin
BBA - Proteins and Proteomics, 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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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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