Results 81 to 90 of about 6,613 (229)
Unraveling the Role of P450 Reductase in Herbicide Metabolic Resistance Mechanism
ABSTRACT Plants require cytochrome P450 reductase (CPR) to supply two electrons for cytochrome P450 monooxygenase enzymes (P450) to react with an organic substrate. The transfer of electrons to the P450 active site in the P450 catalytic site relies on a robust and intricate CPR:P450 complex in the endoplasmic reticulum membrane.
Carlos Alberto Gonsiorkiewicz Rigon +3 more
wiley +1 more source
Flavodoxins are small flavin mononucleotide (FMN)‐containing proteins that mediate a variety of electron transfer processes. The primary sequence of flavodoxin from Fusobacterium nucleatum, a pathogenic oral bacterium, is marked with a number of distinct
Robert G Mothersole +4 more
semanticscholar +1 more source
Mapping the interactions between flavodoxin and its physiological partners flavodoxin reductase and cobalamin-dependent methionine synthase [PDF]
Flavodoxins are electron-transfer proteins that contain the prosthetic group flavin mononucleotide. In Escherichia coli , flavodoxin is reduced by the FAD-containing protein NADPH:ferredoxin (flavodoxin) oxidoreductase; flavodoxins serve as electron donors in the reductive activation of ...
D A, Hall +5 more
openaire +2 more sources
We brought evidence that glacier ice alga Ancylonema alaskanum (Zygnematophceae) sequesters iron and forms organic metal complexes. We found that phenols were already present in the green Ancylonema alaskanum laboratory strain. Our study showed that their vacuole turned brownish due to enhanced iron‐phenol complexation under nutrient limitation with ...
Lenka Procházková +4 more
wiley +1 more source
Summary Flavodoxin (Fld) plays a pivotal role in photosynthetic microorganisms as an alternative electron carrier flavoprotein under adverse environmental conditions.
Zhigang Li +9 more
semanticscholar +1 more source
Two soluble flavoproteins, purified from Escherichia coli cytosol and identified as flavodoxin and NADPH-flavodoxin (ferredoxin) reductase (flavodoxin reductase), have been found in combination to support the 17 alpha-hydroxylase activities of heterologously expressed bovine 17 alpha-hydroxylase cytochrome P450 (P450c17).
C M, Jenkins, M R, Waterman
openaire +2 more sources
SUMMARY In recent years, accurate and low‐cost variant calling has enabled the genotyping of large diversity panels for genome‐wide association studies. As a result, phenotyping rather than genotyping is now the rate‐limiting step, especially in field experiments.
Rens Dijkhuizen +10 more
wiley +1 more source
Electron-transferring flavoprotein (Etf) and butyryl-CoA dehydrogenase (Bcd) from Acidaminococcus fermentans catalyze the endergonic reduction of ferredoxin by NADH, which is also driven by the concomitant reduction of crotonyl-CoA by NADH, a process ...
Nilanjan Chowdhury +3 more
semanticscholar +1 more source
Two Key Ferredoxins for Nitrogen Fixation Have Different Specificities and Biophysical Properties
Two ferredoxins, FdC and FdN, are collectively essential for the process of nitrogen fixation by the iron nitrogenase in R. capsulatus. We explore the biophysical factors, through spectroscopic and structural characterizations, which determine ferredoxin functionality and pathway specificity. The structure of FdC (PDB: 9I2A) and model of FdN (AF‐D5ARY6)
Holly Addison +5 more
wiley +1 more source
Flavodoxins (Flds) are small, bacterial proteins that transfer electrons to various redox enzymes. Flavodoxins are reduced by ferredoxin/flavodoxin NADP+ oxidoreductases (FNRs), but little is known of the FNR-Fld interaction.
I. Gudim +3 more
semanticscholar +1 more source

