Results 71 to 80 of about 29,105 (237)

Myocardial inflammation is associated with impaired mitochondrial oxidative capacity in ischaemic cardiomyopathy

open access: yesESC Heart Failure, Volume 12, Issue 2, Page 1246-1255, April 2025.
Abstract Aims Myocardial inflammation and impaired mitochondrial oxidative capacity are hallmarks of heart failure (HF) pathophysiology. The extent of myocardial inflammation in patients suffering from ischaemic cardiomyopathy (ICM) or dilated cardiomyopathy (DCM) and its association with mitochondrial energy metabolism are unknown.
Julius Borger   +15 more
wiley   +1 more source

Determination of Flavin Potential in Proteins by Xanthine/Xanthine Oxidase Method

open access: yesBio-Protocol, 2020
This protocol describes a simple xanthine/xanthine oxidase enzymatic equilibration method for determination of the redox potential of a flavin. As an example of the use of this method, we determine the reduction potential of the covalently bound FAD ...
Elena Maklashina, Gary Cecchini
doaj   +1 more source

Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor

open access: yesNature Communications, 2021
An important type of post-translational protein modification is the conversion of peptidyl amino acid into enzyme cofactor. Here, the authors report functional and structural characterization of a flavoprotein monooxygenase essential for biosynthesis of ...
Toshinori Oozeki   +7 more
doaj   +1 more source

Protochlorophyllide reductase: A flavoprotein?

open access: yes, 1988
Protochlorophyllide reductase (EC 1.6.99.1) catalyses the light-dependent reduction of protochlorophyllide to chlorophyllide. Evidence has been obtained for the possible involvement of FAD in this reaction: (i) protochlorophyllide reductase is inhibited ...
Caroline J. Walker   +3 more
core   +1 more source

Light‐Driven Butyrate Production by a Probiotic Clostridium tyrobutyricum Enabled by a Cell‐Semiconductor Hybrid Interface

open access: yesFood Chemistry International, EarlyView.
This schematic illustrates a light‐driven biohybrid system where CdS nanoparticles, mineralized on the probiotic Clostridium tyrobutyricum, inject photoelectrons to elevate intracellular NADH. This boosts the flux through key NADH‐dependent enzymes (GapA, Hbd, and Bcd), reprogramming metabolism to enhance butyrate yield by 33.2% and selectivity to 95.7%
Qianru Zhao   +3 more
wiley   +1 more source

Synthesis and Antibacterial Activity of Metal(loid) Nanostructures by Environmental Multi-Metal(loid) Resistant Bacteria and Metal(loid)-Reducing Flavoproteins

open access: yesFrontiers in Microbiology, 2018
Microbes are suitable candidates to recover and decontaminate different environments from soluble metal ions, either via reduction or precipitation to generate insoluble, non-toxic derivatives.
Maximiliano Figueroa   +14 more
doaj   +1 more source

A luminal flavoprotein in endoplasmic reticulum-associated degradation [PDF]

open access: yes, 2009
The quality control system of the endoplasmic reticulum (ER) discriminates between native and nonnative proteins. The latter are degraded by the ER-associated degradation (ERAD) pathway.
Bodenmiller, Bernd   +5 more
core   +1 more source

From identification of fluorescent flavoproteins to mitochondrial redox indicators in intact tissues [PDF]

open access: yesJournal of Innovative Optical Health Sciences, 2014
Development of the use of flavin and nicotinamide-adenine nucleotide fluorescence in monitoring the redox state of the free mitochondrial NADH/NAD+ couple in cells, tissues and organs is reviewed.
Ilmo E. Hassinen
doaj   +1 more source

Discovery of flavoprotein oxidases:New insights and potential for applications [PDF]

open access: yes
Flavoprotein oxidases are redox enzymes that utilize a flavin cofactor to oxidize their substrates, using molecular oxygenas an electron acceptor and producing hydrogen peroxide as by-product.
Santema, Lars
core   +1 more source

The X‐Ray Crystal Structure of BorF, the Flavin Reductase Subunit of a Two‐Component Flavin‐Dependent Tryptophan Halogenase

open access: yesProteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT BorF is a short‐chain flavin reductase from a desert soil bacterium that uses NADH to reduce FAD to FADH2, which is used by the tryptophan‐6‐halogenase BorH to chlorinate tryptophan in the biosynthetic pathway of borregomycin A. The X‐ray crystal structure of BorF bound to FAD was solved to 2.37 Å by molecular replacement.
Zheng Ma   +3 more
wiley   +1 more source

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