Articles with "flavin" as a keyword



Flavin‐N5 Covalent Intermediate in a Nonredox Dehalogenation Reaction Catalyzed by an Atypical Flavoenzyme

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Published in 2018 at "ChemBioChem"

DOI: 10.1002/cbic.201700594

Abstract: The flavin‐dependent enzyme 2‐haloacrylate hydratase (2‐HAH) catalyzes the conversion of 2‐chloroacrylate, a major component in the manufacture of acrylic polymers, to pyruvate. The enzyme was expressed in Escherichia coli, purified, and characterized. 2‐HAH was shown… read more here.

Keywords: flavoenzyme; flavin covalent; covalent; flavin ... See more keywords

Broadening the Scope of the Flavin‐Tag Method by Improving Flavin Incorporation and Incorporating Flavin Analogs

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Published in 2022 at "Chembiochem"

DOI: 10.1002/cbic.202200144

Abstract: Methods for facile site‐selective modifications of proteins are in high demand. We have recently shown that a flavin transferase can be used for site‐specific covalent attachment of a chromo‐ and fluorogenic flavin (FMN) to any… read more here.

Keywords: flavin tag; flavin incorporation; tag method; flavin ... See more keywords

Asymmetric catalysis by flavin-dependent halogenases.

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Published in 2023 at "Chirality"

DOI: 10.1002/chir.23550

Abstract: In nature, flavin-dependent halogenases (FDHs) catalyze site-selective chlorination and bromination of aromatic natural products. This ability has led to extensive efforts to engineer FDHs for selective chlorination, bromination, and iodination of electron rich aromatic compounds.… read more here.

Keywords: flavin dependent; catalysis; asymmetric catalysis; dependent halogenases ... See more keywords

Mechanism of Nitrone Formation by a Flavin-Dependent Monooxygenase

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Published in 2024 at "Biochemistry"

DOI: 10.1021/acs.biochem.3c00656

Abstract: OxaD is a flavin-dependent monooxygenase (FMO) responsible for catalyzing the oxidation of an indole nitrogen atom, resulting in the formation of a nitrone. Nitrones serve as versatile intermediates in complex syntheses, including challenging reactions like… read more here.

Keywords: flavin; flavin dependent; dependent monooxygenase; mechanism ... See more keywords

Oxidation of Flavin by Molecular Oxygen: Computational Insights into a Possible Radical Mechanism

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Published in 2024 at "ACS Omega"

DOI: 10.1021/acsomega.4c00307

Abstract: As a highly electrophilic moiety capable of oxidizing a variety of small organic molecules and biomolecules, flavin is an important prosthetic group in many enzymes. Upon oxidation of the substrate, flavin is converted into its… read more here.

Keywords: flavin; oxidation; molecular oxygen; radical mechanism ... See more keywords

Advanced flavin catalysts elaborated with polymers

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Published in 2018 at "Polymer Journal"

DOI: 10.1038/s41428-018-0089-8

Abstract: AbstractA variety of biological redox reactions are mediated by flavoenzymes due to the unique redox activity of isoalloxazine ring systems, which are found in flavin cofactors. In the field of synthetic organic chemistry, the term… read more here.

Keywords: flavin catalysts; polymer; flavin; catalytic activity ... See more keywords

pH modulates efficiency of singlet oxygen production by flavin cofactors

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Published in 2024 at "RSC Advances"

DOI: 10.1039/d4ra05540c

Abstract: Flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) are frequently used interchangeably in the catalysis of various reactions as part of flavoenzymes because they have the same functional component, the isoalloxazine ring. However, they differ… read more here.

Keywords: flavin; oxygen; singlet oxygen; fmn ... See more keywords

A single hydrogen bond that tunes flavin redox reactivity and activates it for modification

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Published in 2024 at "Chemical Science"

DOI: 10.1039/d4sc01642d

Abstract: Electron bifurcation produces high-energy products based on less energetic reagents. This feat enables biological systems to exploit abundant mediocre fuel to drive vital but demanding reactions, including nitrogen fixation and CO2 capture. Thus, there is… read more here.

Keywords: flavin; chemistry; hydrogen bond; bond ... See more keywords

Evolutionary and molecular foundations of multiple contemporary functions of the nitroreductase superfamily

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Published in 2017 at "Proceedings of the National Academy of Sciences of the United States of America"

DOI: 10.1073/pnas.1706849114

Abstract: Significance Functionally diverse enzyme superfamilies are sets of homologs that conserve a structural fold and mechanistic details but perform various distinct chemical reactions. What are the evolutionary routes by which ancestral proteins diverge to produce… read more here.

Keywords: molecular foundations; flavin; enzyme superfamilies; foundations multiple ... See more keywords

An uncharacteristically low-potential flavin governs the energy landscape of electron bifurcation

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Published in 2022 at "Proceedings of the National Academy of Sciences of the United States of America"

DOI: 10.1073/pnas.2117882119

Abstract: Significance Nature has long been an inspiration for materials design, as it exemplifies exquisite control of both matter and energy. Electron bifurcation, a mechanism employed in biological systems to drive thermodynamically unfavorable and energetically challenging… read more here.

Keywords: energy landscape; energy; electron bifurcation; electron ... See more keywords

Ultrafast photooxidation of protein-bound anionic flavin radicals

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Published in 2022 at "Proceedings of the National Academy of Sciences of the United States of America"

DOI: 10.1073/pnas.2118924119

Abstract: Significance Flavoproteins are colored proteins involved in a large variety of biochemical reactions. They can perform photochemical reactions, which are increasingly exploited for bioengineering new protein-derived photocatalysts. In particular, light-induced reduction of the resting oxidized… read more here.

Keywords: protein bound; anionic flavin; flavin radicals; bound anionic ... See more keywords