Results 21 to 30 of about 23,312 (291)

Comparative Analysis of NADPH-Cytochrome P450 Reductases From Legumes for Heterologous Production of Triterpenoids in Transgenic Saccharomyces cerevisiae

open access: yesFrontiers in Plant Science, 2021
Triterpenoids are plant specialized metabolites with various pharmacological activities. They are widely distributed in higher plants, such as legumes.
Pramesti Istiandari   +13 more
doaj   +1 more source

Tamoxifen-like metallocifens target thioredoxin system determining mitochondrial impairment leading to apoptosis in Jurkat cells [PDF]

open access: yes, 2017
Tamoxifen-like metallocifens (TLMs) of the group-8 metals (Fe, Ru, and Os) show strong anti-proliferative activity on cancer cell lines resistant to apoptosis, owing to their unique redox properties. In contrast, the thioredoxin system, which is involved
Alberto Bindoli   +9 more
core   +3 more sources

Nitrite Reductase Activity of Cytochrome c [PDF]

open access: yesJournal of Biological Chemistry, 2008
Small increases in physiological nitrite concentrations have now been shown to mediate a number of biological responses, including hypoxic vasodilation, cytoprotection after ischemia/reperfusion, and regulation of gene and protein expression. Thus, while nitrite was until recently believed to be biologically inert, it is now recognized as a potentially
Swati, Basu   +7 more
openaire   +2 more sources

Identification of a Novel Self-Sufficient Styrene Monooxygenase from Rhodococcus opacus 1CP. [PDF]

open access: yes, 2009
Sequence analysis of a 9-kb genomic fragment of the actinobacterium Rhodococcus opacus 1CP led to identification of an open reading frame encoding a novel fusion protein, StyA2B, with a putative function in styrene metabolism via styrene oxide and ...
Berkel, W.J.H., van   +5 more
core   +4 more sources

Homologous bd oxidases share the same architecture but differ in mechanism

open access: yesNature Communications, 2019
Cytochrome bd oxidases couple quinol oxidation and the release of protons to the periplasmic side with proton uptake from the cytoplasmic side to reduce dioxygen to water and they are the terminal reductases in bacterial and archaeal respiratory chains ...
Alexander Theßeling   +7 more
doaj   +1 more source

How Thermophilic Gram-Positive Organisms Perform Extracellular Electron Transfer: Characterization of the Cell Surface Terminal Reductase OcwA

open access: yesmBio, 2019
Extracellular electron transfer is the key process underpinning the development of bioelectrochemical systems for the production of energy or added-value compounds.
N. L. Costa   +7 more
doaj   +1 more source

Structural Features of Cytochrome b5–Cytochrome b5 Reductase Complex Formation and Implications for the Intramolecular Dynamics of Cytochrome b5 Reductase [PDF]

open access: yesInternational Journal of Molecular Sciences, 2021
Membrane cytochrome b5 reductase is a pleiotropic oxidoreductase that uses primarily soluble reduced nicotinamide adenine dinucleotide (NADH) as an electron donor to reduce multiple biological acceptors localized in cellular membranes. Some of the biological acceptors of the reductase and coupled redox proteins might eventually transfer electrons to ...
Carlos Gutiérrez-Merino   +3 more
openaire   +3 more sources

Metabolism of BYZX in human liver microsomes and cytosol: identification of the metabolites and metabolic pathways of BYZX. [PDF]

open access: yesPLoS ONE, 2013
BYZX, [(E)-2-(4-((diethylamino)methyl)benzylidene)-5,6-dimethoxy-2,3-dihydroinden-one], belongs to a series of novel acetylcholinesterase inhibitors and has been synthesized as a new chemical entity for the treatment of Alzheimer's disease symptoms. When
Lushan Yu   +5 more
doaj   +1 more source

Cloning, sequencing, and characterization of the hexahydro-1,3,5-trinitro-1,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous [PDF]

open access: yes, 2002
Hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) is a high explosive which presents an environmental hazard as a major land and groundwater contaminant.
Basran, A   +6 more
core   +2 more sources

A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases

open access: yesNature Communications, 2023
Quinol-dependent nitric oxide reductases (qNORs) are considered members of the respiratory heme-copper oxidase superfamily, are unique to bacteria, and are commonly found in pathogenic bacteria where they play a role in combating the host immune response.
Alex J. Flynn   +4 more
doaj   +1 more source

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