Results 81 to 90 of about 33,968 (291)

Amino acid residues associated with cluster N3 in the NuoF subunit of the proton‐translocating NADH‐quinone oxidoreductase from Escherichia coli

open access: yesFEBS Letters, 2005
The NuoF subunit, which harbors NADH‐binding site, of Escherichia coli NADH‐quinone oxidoreductase (NDH‐1) contains five conserved cysteine residues, four of which are predicted to ligate cluster N3. To determine this coordination, we overexpressed and purified the NuoF subunit and NuoF + E subcomplex in E. coli.
Velazquez, Isabel   +4 more
openaire   +2 more sources

Hole hopping through tyrosine/tryptophan chains protects proteins from oxidative damage [PDF]

open access: yes, 2015
Living organisms have adapted to atmospheric dioxygen by exploiting its oxidizing power while protecting themselves against toxic side effects. Reactive oxygen and nitrogen species formed during oxidative stress, as well as high-potential reactive ...
Gray, Harry B., Winkler, Jay R.
core   +1 more source

Mechanisms of Aristolochic Acid Resistance in Specialist Butterflies and Evolutionary Insights for Potential Protective Pathways

open access: yesAdvanced Science, EarlyView.
The study provides an extreme example of insect adaptation to highly toxic defenses of host plants, and investigates the complex strategies to resist carcinogenic aristolochic acids, including physical isolation, metabolic detoxification, and DNA repair.
Yang Luan   +20 more
wiley   +1 more source

A GMC Oxidoreductase GmcA Is Required for Symbiotic Nitrogen Fixation in Rhizobium leguminosarum bv. viciae

open access: yesFrontiers in Microbiology, 2020
GmcA is a FAD-containing enzyme belonging to the GMC (glucose-methanol-choline oxidase) family of oxidoreductases. A mutation in the Rhizobium leguminosarum gmcA gene was generated by homologous recombination.
Qian Zou   +5 more
doaj   +1 more source

Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli [PDF]

open access: yes, 2017
Disulfide bond formation is part of the folding pathway for many periplasmic and outer membrane proteins that contain structural disulfide bonds. In Escherichia coli, a broad variety of periplasmic protein thiol:disulfide oxidoreductases have been ...
Fabianek, Renata A.   +2 more
core  

Zinc accumulation and utilisation by wine yeasts [PDF]

open access: yes, 2009
The present study has focused on the accumulation of zinc by wine yeast strains of Saccharomyces cerevisiae during fermentation of both grape juice and chemically defined medium with different carbohydrates and at varying levels of zinc. The results have
Bollag, Tatiana   +4 more
core   +2 more sources

Ce‐Doped Lignin‐Based Nanozyme with Heat‐Activated Hydrolase Activity

open access: yesAdvanced Science, EarlyView.
A novel Ce‐doped lignin‐based hydrolase nanozyme (Ce‐AL) is synthesized using Ce ions coordinated with aminated industrial lignin. The Ce‐AL effectively hydrolyzes phosphate ester bonds and protein amide bonds, maintain high activity at 100°C, and successfully fights bacteria biofilms.
Xin Liu   +7 more
wiley   +1 more source

A structural phylogeny for understanding 2-oxoacid oxidoreductase function [PDF]

open access: yes, 2018
2-Oxoacid:ferredoxin oxidoreductases (OFORs) are essential enzymes in microbial one-carbon metabolism. They use thiamine pyrophosphate to reversibly cleave carbon-carbon bonds, generating low potential (~-500 mV) electrons. Crystallographic analysis of a
Chen, Yang-Ting   +2 more
core   +1 more source

Nanozymes for Energy and Environmental Sustainability

open access: yesAdvanced Science, EarlyView.
At present, the widely used nanozymes are oxidoreductase and hydrolase, which have proved to have great application prospects in energy and environment. ABSTRACT Nanozymes have shown remarkable promise in addressing pressing challenges in energy and environmental sustainability.
Xiaoqi Li, Jinxing Chen, Shaojun Dong
wiley   +1 more source

Identification of crucial amino acids in mouse aldehyde oxidase 3 that determine substrate specificity.

open access: yesPLoS ONE, 2013
In order to elucidate factors that determine substrate specificity and activity of mammalian molybdo-flavoproteins we performed site directed mutagenesis of mouse aldehyde oxidase 3 (mAOX3).
Martin Mahro   +6 more
doaj   +1 more source

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