Results 161 to 170 of about 135,211 (213)

Breaking aromaticity in the anaerobic degradation pathway of phenanthrene comprises only ATP-independent type III aryl-CoA reductases. [PDF]

Commun Biol
Samak NA, Häßler M, Schmitz OJ, Adjir K, Meckenstock RU.   +4 more
europepmc   +1 more source

Formate as electron carrier in the gut acetogen <i>Blautia luti</i>: a model for electron transfer in the gut microbiome. [PDF]

Gut Microbes
Trischler R, Müller V.
europepmc   +1 more source

In the Marathon toward Achieving Efficient Enzymatic Decarboxylation of Fatty Acids. [PDF]

ACS Cent Sci
Winkler CK, Kroutil W.
europepmc   +1 more source

Interaction of ferredoxin and ferredoxin-NADP reductase with thylakoids

Archives of Biochemistry and Biophysics, 1983
Ferredoxin-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., Cappelletti A., Nobili R. L., Garlaschi F. M., GEROLA, PAOLO, Jennings R. C.   +5 more
openaire   +4 more sources

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Interaction of ferredoxin-linked nitrite reductase with ferredoxin

BBA - Proteins and Proteomics, 1985
Abstract 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
exaly   +2 more sources

Ferredoxin-thioredoxin reductase: Properties of its complex with ferredoxin

Biochimica Et Biophysica Acta - Bioenergetics, 1988
Abstract Ferredoxin-thioredoxin reductase formed an electrostatically stabilized 1:1 complex with ferredoxin. Complex formation could be detected, following mixing of the two proteins, either by changes in optical absorbance and circular dichroism spectra or by co-chromatography during gel filtration.
Michel Droux, Bob B Buchanan, Masakazu Hirasawa   +2 more
exaly   +3 more sources

Involvement of lysine-88 of spinach ferredoxin-NADP+reductase in the interaction with ferredoxin [PDF]

FEBS Letters, 1994
A mutant of spinach ferredoxin-NADP+ reductase, in which Lys-88 has been changed to glutamine, has been obtained by site-directed mutagenesis. The mutant enzyme was fully active as a diaphorase, but partially impaired in ferredoxin-dependent cytochrome c
Alessandro Aliverti
exaly   +2 more sources

Ferredoxin/ferredoxin-thioredoxin reductase complex: Complete NMR mapping of the interaction site on ferredoxin by gallium substitution [PDF]

FEBS Letters, 2006
The reduction of ferredoxin–thioredoxin reductase (FTR) by plant-type ferredoxin plays an important role in redox regulation in plants and cyanobacteria.
Xingfu Xu, Sung-Kun Kim, Marcellus Ubbink   +2 more
exaly   +2 more sources

Lysine residues on ferredoxin-NADP+reductase fromAnabaenasp. PCC 7119 involved in substrate binding [PDF]

FEBS Letters, 1992
Ferredoxin-NADP+ reductase from Anabaena sp. PCC 7119 is chemically modified by pyridoxal 5′-phosphate. The incorporation of 2±0.3 mol pyridoxal 5′-phosphate/mol ferredoxin-NADP+ reductase inhibited NADPH-cytochrome c reductase activity by up to 95 ...
Milagros Medina, Carlos Gomez-Moreno
exaly   +2 more sources

Amino acid residues involved in functional interaction of vegetative cell ferredoxin from the cyanobacterium Anabaena sp. PCC 7120 with ferredoxin:NADP reductase, nitrite reductase and nitrate reductase [PDF]

Biochimica Et Biophysica Acta - Bioenergetics, 1995
During evolution, cyanobacterial [2Fe-2S]-ferredoxins have developed structural features that enable them to form 1:1 complexes with different redox partners, which are mainly stabilized by electrostatic interactions.
Herbert Böhme
exaly   +2 more sources