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Journal articles on the topic 'Flavin hydroquinone dependent Enzymes'

Author: Grafiati

Published: 25 May 2024

Last updated: 31 July 2025

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1

Perry, Lynda L., and Gerben J. Zylstra. "Cloning of a Gene Cluster Involved in the Catabolism of p-Nitrophenol by Arthrobacter sp. Strain JS443 and Characterization of the p-Nitrophenol Monooxygenase." Journal of Bacteriology 189, no. 21 (2007): 7563–72. http://dx.doi.org/10.1128/jb.01849-06.

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ABSTRACT The npd gene cluster, which encodes the enzymes of a p-nitrophenol catabolic pathway from Arthrobacter sp. strain JS443, was cloned and sequenced. Three genes, npdB, npdA1, and npdA2, were independently expressed in Escherichia coli in order to confirm the identities of their gene products. NpdA2 is a p-nitrophenol monooxygenase belonging to the two-component flavin-diffusible monooxygenase family of reduced flavin-dependent monooxygenases. NpdA1 is an NADH-dependent flavin reductase, and NpdB is a hydroxyquinol 1,2-dioxygenase. The npd gene cluster also includes a putative maleylacet

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2

Mihasan, Marius, Calin-Bogdan Chiribau, Thorsten Friedrich, Vlad Artenie, and Roderich Brandsch. "An NAD(P)H-Nicotine Blue Oxidoreductase Is Part of the Nicotine Regulon and May Protect Arthrobacter nicotinovorans from Oxidative Stress during Nicotine Catabolism." Applied and Environmental Microbiology 73, no. 8 (2007): 2479–85. http://dx.doi.org/10.1128/aem.02668-06.

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ABSTRACT An NAD(P)H-nicotine blue (quinone) oxidoreductase was discovered as a member of the nicotine catabolic pathway of Arthrobacter nicotinovorans. Transcriptional analysis and electromobility shift assays showed that the enzyme gene was expressed in a nicotine-dependent manner under the control of the transcriptional activator PmfR and thus was part of the nicotine regulon of A. nicotinovorans. The flavin mononucleotide-containing enzyme uses NADH and, with lower efficiency, NADPH to reduce, by a two-electron transfer, nicotine blue to the nicotine blue leuco form (hydroquinone). Besides

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3

Hyster, Todd K. "Radical Biocatalysis: Using Non-Natural Single Electron Transfer Mechanisms to Access New Enzymatic Functions." Synlett 31, no. 03 (2019): 248–54. http://dx.doi.org/10.1055/s-0037-1611818.

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Exploiting non-natural reaction mechanisms within native enzymes is an emerging strategy for expanding the synthetic capabilities of biocatalysts. When coupled with modern protein engineering techniques, this approach holds great promise for biocatalysis to address long-standing selectivity and reactivity challenges in chemical synthesis. Controlling the stereochemical outcome of reactions involving radical intermediates, for instance, could benefit from biocatalytic solutions because these reactions are often difficult to control by using existing small molecule catalysts. General strategies

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4

Wojcieszyńska, Danuta, Katarzyna Hupert-Kocurek, and Urszula Guzik. "Flavin-Dependent Enzymes in Cancer Prevention." International Journal of Molecular Sciences 13, no. 12 (2012): 16751–68. http://dx.doi.org/10.3390/ijms131216751.

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5

Hilvert, Donald, and E. T. Kaisert. "Semisynthetic Enzymes: Design of Flavin-Dependent Oxidoreductases." Biotechnology and Genetic Engineering Reviews 5, no. 1 (1987): 297–318. http://dx.doi.org/10.1080/02648725.1987.10647841.

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6

Menon, Binuraj R. K., Jonathan Latham, Mark S. Dunstan, et al. "Structure and biocatalytic scope of thermophilic flavin-dependent halogenase and flavin reductase enzymes." Organic & Biomolecular Chemistry 14, no. 39 (2016): 9354–61. http://dx.doi.org/10.1039/c6ob01861k.

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7

Moon, Shin, and Choe. "Crystal Structures of Putative Flavin Dependent Monooxygenase from Alicyclobacillus Acidocaldarius." Crystals 9, no. 11 (2019): 548. http://dx.doi.org/10.3390/cryst9110548.

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Flavin dependent monooxygenases catalyze various reactions to play a key role in biological processes, such as catabolism, detoxification, and biosynthesis. Group D flavin dependent monooxygenases are enzymes with an Acyl-CoA dehydrogenase (ACAD) fold and use Flavin adenine dinucleotide (FAD) or Flavin mononucleotide (FMN) as a cofactor. In this research, crystal structures of Alicyclobacillus acidocaldarius protein formerly annotated as an ACAD were determined in Apo and FAD bound state. Although our structure showed high structural similarity to other ACADs, close comparison of substrate bin

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8

Mügge, Carolin, Thomas Heine, Alvaro Gomez Baraibar, Willem J. H. van Berkel, Caroline E. Paul, and Dirk Tischler. "Flavin-dependent N-hydroxylating enzymes: distribution and application." Applied Microbiology and Biotechnology 104, no. 15 (2020): 6481–99. http://dx.doi.org/10.1007/s00253-020-10705-w.

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9

Shepherd, Sarah A., Chinnan Karthikeyan, Jonathan Latham, et al. "Extending the biocatalytic scope of regiocomplementary flavin-dependent halogenase enzymes." Chemical Science 6, no. 6 (2015): 3454–60. http://dx.doi.org/10.1039/c5sc00913h.

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10

Saleem-Batcha, Raspudin, Frederick Stull, Jacob N. Sanders, et al. "Enzymatic control of dioxygen binding and functionalization of the flavin cofactor." Proceedings of the National Academy of Sciences 115, no. 19 (2018): 4909–14. http://dx.doi.org/10.1073/pnas.1801189115.

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The reactions of enzymes and cofactors with gaseous molecules such as dioxygen (O2) are challenging to study and remain among the most contentious subjects in biochemistry. To date, it is largely enigmatic how enzymes control and fine-tune their reactions with O2, as exemplified by the ubiquitous flavin-dependent enzymes that commonly facilitate redox chemistry such as the oxygenation of organic substrates. Here we employ O2-pressurized X-ray crystallography and quantum mechanical calculations to reveal how the precise positioning of O2 within a flavoenzyme’s active site enables the regiospeci

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11

de Gonzalo, Gonzalo, and Andrés R. Alcántara. "Multienzymatic Processes Involving Baeyer–Villiger Monooxygenases." Catalysts 11, no. 5 (2021): 605. http://dx.doi.org/10.3390/catal11050605.

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Baeyer–Villiger monooxygenases (BVMOs) are flavin-dependent oxidative enzymes capable of catalyzing the insertion of an oxygen atom between a carbonylic Csp2 and the Csp3 at the alpha position, therefore transforming linear and cyclic ketones into esters and lactones. These enzymes are dependent on nicotinamides (NAD(P)H) for the flavin reduction and subsequent reaction with molecular oxygen. BVMOs can be included in cascade reactions, coupled to other redox enzymes, such as alcohol dehydrogenases (ADHs) or ene-reductases (EREDs), so that the direct conversion of alcohols or α,β-unsaturated ca

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12

Pié Porta, Ariadna, Elif Erdem, and John M. Woodley. "Tools to investigate oxygen-related challenges with flavin-dependent enzymes." Archives of Biochemistry and Biophysics 764 (February 2025): 110246. https://doi.org/10.1016/j.abb.2024.110246.

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13

Zhang, Jun-Jie, Hong Liu, Yi Xiao, Xian-En Zhang, and Ning-Yi Zhou. "Identification and Characterization of Catabolic para-Nitrophenol 4-Monooxygenase and para-Benzoquinone Reductase from Pseudomonas sp. Strain WBC-3." Journal of Bacteriology 191, no. 8 (2009): 2703–10. http://dx.doi.org/10.1128/jb.01566-08.

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ABSTRACT Pseudomonas sp. strain WBC-3 utilizes para-nitrophenol (PNP) as a sole source of carbon, nitrogen, and energy. In order to identify the genes involved in this utilization, we cloned and sequenced a 12.7-kb fragment containing a conserved region of NAD(P)H:quinone oxidoreductase genes. Of the products of the 13 open reading frames deduced from this fragment, PnpA shares 24% identity to the large component of a 3-hydroxyphenylacetate hydroxylase from Pseudomonas putida U and PnpB is 58% identical to an NAD(P)H:quinone oxidoreductase from Escherichia coli. Both PnpA and PnpB were purifie

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14

Huang, Yan, Randy Xun, Guanjun Chen, and Luying Xun. "Maintenance Role of a Glutathionyl-Hydroquinone Lyase (PcpF) in Pentachlorophenol Degradation by Sphingobium chlorophenolicum ATCC 39723." Journal of Bacteriology 190, no. 23 (2008): 7595–600. http://dx.doi.org/10.1128/jb.00489-08.

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ABSTRACT Pentachlorophenol (PCP) is a toxic pollutant. Its biodegradation has been extensively studied in Sphingobium chlorophenolicum ATCC 39723. All enzymes required to convert PCP to a common metabolic intermediate before entering the tricarboxylic acid cycle have been characterized. One of the enzymes is tetrachloro-p-hydroquinone (TeCH) reductive dehalogenase (PcpC), which is a glutathione (GSH) S-transferase (GST). PcpC catalyzes the GSH-dependent conversion of TeCH to trichloro-p-hydroquinone (TriCH) and then to dichloro-p-hydroquinone (DiCH) in the PCP degradation pathway. PcpC is susc

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15

Wang, Jinyu, and Yajun Liu. "Systematic Theoretical Study on the pH-Dependent Absorption and Fluorescence Spectra of Flavins." Molecules 28, no. 8 (2023): 3315. http://dx.doi.org/10.3390/molecules28083315.

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Flavins are a class of organic compounds with the basic structure of 7,8-dimethy-10-alkyl isoalloxazine. They are ubiquitous in nature and participate in many biochemical reactions. Due to various existing forms, there is a lack of systematic research on the absorption and fluorescence spectra of flavins. In this study, employing the density functional theory (DFT) and time-dependent (TD) DFT, we calculated the pH-dependent absorption and fluorescence spectra of flavin of three redox states (quinone, semiquinone, and hydroquinone) in solvents. The chemical equilibrium of three redox states of

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16

McLEAN, Kirsty J., Nigel S. SCRUTTON, and Andrew W. MUNRO. "Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin reductase homologue FprA." Biochemical Journal 372, no. 2 (2003): 317–27. http://dx.doi.org/10.1042/bj20021692.

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The genome sequence of the pathogenic bacterium Mycobacterium tuberculosis revealed numerous cytochrome P450 enzymes, which require accessory redox enzymes for catalytic function (ferredoxin reductase and ferredoxin). The most likely ferredoxin reductase is encoded by fprA, and its structure resembles eukaryotic adrenodoxin reductases. We have cloned, expressed and purified the flavoenzyme product of the fprA gene in Escherichia coli. FprA reduces various electron acceptors using either NADPH or NADH as the electron donor, but discriminates in favour of NADPH (apparent Km for NADH=50.6±3.1 μM;

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17

Zverinsky, I. V., H. G. Zverinskaya, I. P. Sutsko, P. G. Telegin, and A. G. Shlyahtun. "Effects of berberine on the recovery of rat liver xenobiotic-metabolizing enzymes after partial hepatectomy." Biomeditsinskaya Khimiya 61, no. 3 (2015): 381–83. http://dx.doi.org/10.18097/pbmc20156103381.

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We have studied the effect of berberine on the recovery processes of liver xenobiotic-metabolizing function during its compensatory growth after 70% partial hepatectomy. It was found the hepatic ability to metabolize foreign substances are not restored up to day 8. Administration of berberine (10 mg/kg intraperitoneally) for 6 days led to normalization of both cytochrome P450-dependent and flavin-containing monooxygenases. It is suggested that in the biotransformation of berberine involved not only cytochrome P450, but also flavin-containing monooxygenases.

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18

Dick, Scott, Laura Marrone, Abraham M. Thariath, Miguel A. Valvano, and Thammaiah Viswanatha. "Cofactor- and substrate-binding domains in flavin-dependent N-hydroxylating enzymes." Trends in Biochemical Sciences 23, no. 11 (1998): 414. http://dx.doi.org/10.1016/s0968-0004(98)01271-7.

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19

Neubauer, Pia R., Olga Blifernez-Klassen, Lara Pfaff, Mohamed Ismail, Olaf Kruse, and Norbert Sewald. "Two Novel, Flavin-Dependent Halogenases from the Bacterial Consortia of Botryococcus braunii Catalyze Mono- and Dibromination." Catalysts 11, no. 4 (2021): 485. http://dx.doi.org/10.3390/catal11040485.

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Halogen substituents often lead to a profound effect on the biological activity of organic compounds. Flavin-dependent halogenases offer the possibility of regioselective halogenation at non-activated carbon atoms, while employing only halide salts and molecular oxygen. However, low enzyme activity, instability, and narrow substrate scope compromise the use of enzymatic halogenation as an economical and environmentally friendly process. To overcome these drawbacks, it is of tremendous interest to identify novel halogenases with high enzymatic activity and novel substrate scopes. Previously, Ne

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20

Wick, Jonas, Daniel Heine, Gerald Lackner, et al. "A Fivefold Parallelized Biosynthetic Process Secures Chlorination of Armillaria mellea (Honey Mushroom) Toxins." Applied and Environmental Microbiology 82, no. 4 (2015): 1196–204. http://dx.doi.org/10.1128/aem.03168-15.

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ABSTRACTThe basidiomycetous tree pathogenArmillaria mellea(honey mushroom) produces a large variety of structurally related antibiotically active and phytotoxic natural products, referred to as the melleolides. During their biosynthesis, some members of the melleolide family of compounds undergo monochlorination of the aromatic moiety, whose biochemical and genetic basis was not known previously. This first study on basidiomycete halogenases presents the biochemicalin vitrocharacterization of five flavin-dependentA. melleaenzymes (ArmH1 to ArmH5) that were heterologously produced inEscherichia

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21

Heine, Thomas, Willem van Berkel, George Gassner, Karl-Heinz van Pée, and Dirk Tischler. "Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities." Biology 7, no. 3 (2018): 42. http://dx.doi.org/10.3390/biology7030042.

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Flavoprotein monooxygenases create valuable compounds that are of high interest for the chemical, pharmaceutical, and agrochemical industries, among others. Monooxygenases that use flavin as cofactor are either single- or two-component systems. Here we summarize the current knowledge about two-component flavin adenine dinucleotide (FAD)-dependent monooxygenases and describe their biotechnological relevance. Two-component FAD-dependent monooxygenases catalyze hydroxylation, epoxidation, and halogenation reactions and are physiologically involved in amino acid metabolism, mineralization of aroma

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22

Andorfer, Mary C., and Jared C. Lewis. "Understanding and Improving the Activity of Flavin-Dependent Halogenases via Random and Targeted Mutagenesis." Annual Review of Biochemistry 87, no. 1 (2018): 159–85. http://dx.doi.org/10.1146/annurev-biochem-062917-012042.

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Flavin-dependent halogenases (FDHs) catalyze the halogenation of organic substrates by coordinating reactions of reduced flavin, molecular oxygen, and chloride. Targeted and random mutagenesis of these enzymes have been used to both understand and alter their reactivity. These studies have led to insights into residues essential for catalysis and FDH variants with improved stability, expanded substrate scope, and altered site selectivity. Mutations throughout FDH structures have contributed to all of these advances. More recent studies have sought to rationalize the impact of these mutations o

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23

Pozzi, Cecilia, Ludovica Lopresti, Giusy Tassone, and Stefano Mangani. "Targeting Methyltransferases in Human Pathogenic Bacteria: Insights into Thymidylate Synthase (TS) and Flavin-Dependent TS (FDTS)." Molecules 24, no. 8 (2019): 1638. http://dx.doi.org/10.3390/molecules24081638.

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In cells, thymidylate synthases provide the only de novo source of 2′-deoxythymidine-5′-monophosphate (dTMP), required for DNA synthesis. The activity of these enzymes is pivotal for cell survival and proliferation. Two main families of thymidylate synthases have been identified in bacteria, folate-dependent thymidylate synthase (TS) and flavin-dependent TS (FDTS). TS and FDTS are highly divergent enzymes, characterized by exclusive catalytic mechanisms, involving different sets of cofactors. TS and FDTS mechanisms of action have been recently revised, providing new perspectives for the develo

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24

Lim, Guiyeoul, Donato Calabrese, Allison Elizabeth Wolder, et al. "H2-driven biocatalysis for flavin-dependent ene-reduction in a continuous closed-loop flow system utilizing H2 from water electrolysis." Communications chemistry 7 (September 27, 2024): 200. https://doi.org/10.1038/s42004-024-01288-y.

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ABSTRACT Despite the increasing demand for efficient and sustainable chemical processes, the development of scalable systems using biocatalysis for fine chemical production remains a significant challenge. We have developed a scalable flow system using immobilized enzymes to facilitate flavin-dependent biocatalysis, targeting as a proof-of-concept asymmetric alkene reduction. The system integrates a flavin-dependent Old Yellow Enzyme (OYE) and a soluble hydrogenase to enable H<sub>2</sub>-driven regeneration of the OYE cofactor FMNH<sub>2</sub>. Molecular hydrogen was produced by water electro

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Biegasiewicz, Kyle F., Simon J. Cooper, Xin Gao, et al. "Photoexcitation of flavoenzymes enables a stereoselective radical cyclization." Science 364, no. 6446 (2019): 1166–69. http://dx.doi.org/10.1126/science.aaw1143.

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Photoexcitation is a common strategy for initiating radical reactions in chemical synthesis. We found that photoexcitation of flavin-dependent “ene”-reductases changes their catalytic function, enabling these enzymes to promote an asymmetric radical cyclization. This reactivity enables the construction of five-, six-, seven-, and eight-membered lactams with stereochemical preference conferred by the enzyme active site. After formation of a prochiral radical, the enzyme guides the delivery of a hydrogen atom from flavin—a challenging feat for small-molecule chemical reagents. The initial electr

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Fejzagić, Alexander Veljko, Jan Gebauer, Nikolai Huwa, and Thomas Classen. "Halogenating Enzymes for Active Agent Synthesis: First Steps Are Done and Many Have to Follow." Molecules 24, no. 21 (2019): 4008. http://dx.doi.org/10.3390/molecules24214008.

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Halogens can be very important for active agents as vital parts of their binding mode, on the one hand, but are on the other hand instrumental in the synthesis of most active agents. However, the primary halogenating compound is molecular chlorine which has two major drawbacks, high energy consumption and hazardous handling. Nature bypassed molecular halogens and evolved at least six halogenating enzymes: Three kind of haloperoxidases, flavin-dependent halogenases as well as α-ketoglutarate and S-adenosylmethionine (SAM)-dependent halogenases. This review shows what is known today on these enz

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27

Willetts, Andrew. "The Isoenzymic Diketocamphane Monooxygenases of Pseudomonas putida ATCC 17453—An Episodic History and Still Mysterious after 60 Years." Microorganisms 9, no. 12 (2021): 2593. http://dx.doi.org/10.3390/microorganisms9122593.

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Researching the involvement of molecular oxygen in the degradation of the naturally occurring bicyclic terpene camphor has generated a six-decade history of fascinating monooxygenase biochemistry. While an extensive bibliography exists reporting the many varied studies on camphor 5-monooxygenase, the initiating enzyme of the relevant catabolic pathway in Pseudomonas putida ATCC 17453, the equivalent recorded history of the isoenzymic diketocamphane monooxygenases, the enzymes that facilitate the initial ring cleavage of the bicyclic terpene, is both less extensive and more enigmatic. First ref

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Ung, Kien Lam, Chloé Poussineau, Julie Couston, Husam M. A. B. Alsarraf, and Mickaël Blaise. "Crystal structure of MAB_4123, a putative flavin-dependent monooxygenase from Mycobacterium abscessus." Acta Crystallographica Section F Structural Biology Communications 79, no. 5 (2023): 128–36. http://dx.doi.org/10.1107/s2053230x2300345x.

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Numerous bacteria from different phylae can perform desulfurization reactions of organosulfur compounds. In these degradation or detoxification pathways, two-component flavin-dependent monooxygenases that use flavins (FMN or FAD) as a cofactor play important roles as they catalyse the first steps of these metabolic routes. The TdsC or DszC and MsuC proteins belong to this class of enzymes as they process dibenzothiophene (DBT) and methanesulfinate. Elucidation of their X-ray structures in apo, ligand-bound and cofactor-bound forms has provided important molecular insights into their catalytic

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Shah, Mihir V., James Antoney, Suk Woo Kang, et al. "Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis." Catalysts 9, no. 10 (2019): 868. http://dx.doi.org/10.3390/catal9100868.

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The asymmetric reduction of enoates, imines and ketones are among the most important reactions in biocatalysis. These reactions are routinely conducted using enzymes that use nicotinamide cofactors as reductants. The deazaflavin cofactor F420 also has electrochemical properties that make it suitable as an alternative to nicotinamide cofactors for use in asymmetric reduction reactions. However, cofactor F420-dependent enzymes remain under-explored as a resource for biocatalysis. This review considers the cofactor F420-dependent enzyme families with the greatest potential for the discovery of ne

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Pimviriyakul, Panu, Panida Surawatanawong, and Pimchai Chaiyen. "Oxidative dehalogenation and denitration by a flavin-dependent monooxygenase is controlled by substrate deprotonation." Chemical Science 9, no. 38 (2018): 7468–82. http://dx.doi.org/10.1039/c8sc01482e.

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Hughes, Kristin, Riley Osadchey Brown, Sydney Brender, et al. "Using structure and informatics to probe the mechanism of enzymes in the flavin amine oxidase superfamily." Structural Dynamics 12, no. 2_Supplement (2025): A411. https://doi.org/10.1063/4.0000717.

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Flavoenzymes, which use a flavin adenine dinucleotide (FAD) cofactor, feature a wide range of activities and substrate specificities. This includes the ability to act as oxidases, relying on molecular oxygen (O2) as a co-substrate, or as dehydrogenases wherein the FAD is redox-cycled not by O2, but by other redox-active proteins or small-molecule substrates. Nicotine oxidoreductase (NicA2) is a flavin-dependent enzyme that provides a useful model system for interrogating structure-function relationships: first characterized as an oxidase, NicA2 has been proven to be a true dehydrogenase, with

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Capeillère-Blandin, C., M. J. Barber, and R. C. Bray. "Comparison of the processes involved in reduction by the substrate for two homologous flavocytochromes b2 from different species of yeast." Biochemical Journal 238, no. 3 (1986): 745–56. http://dx.doi.org/10.1042/bj2380745.

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A detailed study of the electron exchanges involved between FMN and haem b2 groups within flavocytochrome b2 of yeast Hansenula anomala (H-enzyme) was performed. The results were compared with those for the homologous enzyme of yeast Saccharomyces cerevisiae (Sx-enzyme) re-investigated at 5 degrees C. The mid-point reduction potentials of FMN and haem were determined by two complementary methods: potentiometric titration with substrate, L-lactate, in the presence of dye mediators with quantification of the reduced species performed by spectrophotometry at suitable wavelengths; anaerobic titrat

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Ferreira, Maria Isabel M., Toshiya Iida, Syed A. Hasan, et al. "Analysis of Two Gene Clusters Involved in the Degradation of 4-Fluorophenol by Arthrobacter sp. Strain IF1." Applied and Environmental Microbiology 75, no. 24 (2009): 7767–73. http://dx.doi.org/10.1128/aem.00171-09.

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ABSTRACT Arthrobacter sp. strain IF1 is able to grow on 4-fluorophenol (4-FP) as a sole source of carbon and energy. To clone the 4-FP degradation genes, DNA libraries were constructed and screened with a probe obtained by PCR using primers designed on the basis of conserved regions of aromatic two-component monooxygenases. Sequencing of positive clones yielded two gene clusters, each harboring a gene encoding a monooxygenase with high sequence similarity to the oxygenase component of 4-nitrophenol and 4-chlorophenol monooxygenase systems. Both these monooxygenase genes were differentially exp

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Pimviriyakul, Panu, and Pimchai Chaiyen. "A complete bioconversion cascade for dehalogenation and denitration by bacterial flavin–dependent enzymes." Journal of Biological Chemistry 293, no. 48 (2018): 18525–39. http://dx.doi.org/10.1074/jbc.ra118.005538.

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Chanda, Kakoli, Atifa Begum Mozumder, Ringhoilal Chorei, Ridip Kumar Gogoi, and Himanshu Kishore Prasad. "A Lignocellulolytic Colletotrichum sp. OH with Broad-Spectrum Tolerance to Lignocellulosic Pretreatment Compounds and Derivatives and the Efficiency to Produce Hydrogen Peroxide and 5-Hydroxymethylfurfural Tolerant Cellulases." Journal of Fungi 7, no. 10 (2021): 785. http://dx.doi.org/10.3390/jof7100785.

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Fungal endophytes are an emerging source of novel traits and biomolecules suitable for lignocellulosic biomass treatment. This work documents the toxicity tolerance of Colletotrichum sp. OH toward various lignocellulosic pretreatment-derived inhibitors. The effects of aldehydes (vanillin, p-hydroxybenzaldehyde, furfural, 5-hydroxymethylfurfural; HMF), acids (gallic, formic, levulinic, and p-hydroxybenzoic acid), phenolics (hydroquinone, p-coumaric acid), and two pretreatment chemicals (hydrogen peroxide and ionic liquid), on the mycelium growth, biomass accumulation, and lignocellulolytic enzy

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Manenda, Mahder S., Marie-Ève Picard, Liping Zhang, et al. "Structural analyses of the Group A flavin-dependent monooxygenase PieE reveal a sliding FAD cofactor conformation bridging OUT and IN conformations." Journal of Biological Chemistry 295, no. 14 (2020): 4709–22. http://dx.doi.org/10.1074/jbc.ra119.011212.

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Group A flavin-dependent monooxygenases catalyze the cleavage of the oxygen–oxygen bond of dioxygen, followed by the incorporation of one oxygen atom into the substrate molecule with the aid of NADPH and FAD. These flavoenzymes play an important role in many biological processes, and their most distinct structural feature is the choreographed motions of flavin, which typically adopts two distinct conformations (OUT and IN) to fulfill its function. Notably, these enzymes seem to have evolved a delicate control system to avoid the futile cycle of NADPH oxidation and FAD reduction in the absence

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Deng, Yaming, Quan Zhou, Yuzhou Wu, Xi Chen, and Fangrui Zhong. "Properties and Mechanisms of Flavin-Dependent Monooxygenases and Their Applications in Natural Product Synthesis." International Journal of Molecular Sciences 23, no. 5 (2022): 2622. http://dx.doi.org/10.3390/ijms23052622.

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Natural products are usually highly complicated organic molecules with special scaffolds, and they are an important resource in medicine. Natural products with complicated structures are produced by enzymes, and this is still a challenging research field, its mechanisms requiring detailed methods for elucidation. Flavin adenine dinucleotide (FAD)-dependent monooxygenases (FMOs) catalyze many oxidation reactions with chemo-, regio-, and stereo-selectivity, and they are involved in the synthesis of many natural products. In this review, we introduce the mechanisms for different FMOs, with the cl

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Ogawa, Aoba, Gen-ichi Sampei, and Gota Kawai. "Crystal structure of the flavin-dependent thymidylate synthase Thy1 from Thermus thermophilus with an extra C-terminal domain." Acta Crystallographica Section F Structural Biology Communications 75, no. 6 (2019): 450–54. http://dx.doi.org/10.1107/s2053230x19007192.

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The thymidylate synthases ThyA and Thy1 are enzymes that catalyse the formation of thymidine monophosphate from 2′-deoxyuridine monophosphate. Thy1 (or ThyX) requires flavin for catalytic reactions, while ThyA does not. In the present study, the crystal structure of the flavin-dependent thymidylate synthase Thy1 from Thermus thermophilus HB8 (TtThy1, TTHA1096) was determined in complex with FAD and phosphate at 2.5 Å resolution. TtThy1 is a tetrameric molecule like other Thy1 proteins, to which four FAD molecules are bound. In the crystal of TtThy1, two phosphate ions were bound to each dUMP-b

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Mączka, Wanda, Katarzyna Wińska, and Małgorzata Grabarczyk. "Biotechnological Methods of Sulfoxidation: Yesterday, Today, Tomorrow." Catalysts 8, no. 12 (2018): 624. http://dx.doi.org/10.3390/catal8120624.

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The production of chiral sulphoxides is an important part of the chemical industry since they have been used not only as pharmaceuticals and pesticides, but also as catalysts or functional materials. The main purpose of this review is to present biotechnological methods for the oxidation of sulfides. The work consists of two parts. In the first part, examples of biosyntransformation of prochiral sulfides using whole cells of bacteria and fungi are discussed. They have more historical significance due to the low predictability of positive results in relation to the workload. In the second part,

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Buss, Maren, Christina Geerds, Thomas Patschkowski, Karsten Niehaus, and Hartmut H. Niemann. "Perfect merohedral twinning combined with noncrystallographic symmetry potentially causes the failure of molecular replacement with low-homology search models for the flavin-dependent halogenase HalX from Xanthomonas campestris." Acta Crystallographica Section F Structural Biology Communications 74, no. 6 (2018): 345–50. http://dx.doi.org/10.1107/s2053230x18006933.

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Flavin-dependent halogenases can be used as biocatalysts because they regioselectively halogenate their substrates under mild reaction conditions. New halogenases with novel substrate specificities will add to the toolbox of enzymes available to organic chemists. HalX, the product of the xcc-b100_4193 gene, is a putative flavin-dependent halogenase from Xanthomonas campestris. The enzyme was recombinantly expressed and crystallized in order to aid in identifying its hitherto unknown substrate. Native data collected to a resolution of 2.5 Å showed indications of merohedral twinning in a hexagon

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Matsubara, Toshiyuki, Takashi Ohshiro, Yoshihiro Nishina, and Yoshikazu Izumi. "Purification, Characterization, and Overexpression of Flavin Reductase Involved in Dibenzothiophene Desulfurization byRhodococcus erythropolis D-1." Applied and Environmental Microbiology 67, no. 3 (2001): 1179–84. http://dx.doi.org/10.1128/aem.67.3.1179-1184.

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ABSTRACT The dibenzothiophene (DBT)-desulfurizing bacterium,Rhodococcus erythropolis D-1, removes sulfur from DBT to form 2-hydroxybiphenyl using four enzymes, DszC, DszA, DszB, and flavin reductase. In this study, we purified and characterized the flavin reductase from R. erythropolis D-1 grown in a medium containing DBT as the sole source of sulfur. It is conceivable that the enzyme is essential for two monooxygenase (DszC and DszA) reactions in vivo. The purified flavin reductase contains no chromogenic cofactors and was found to have a molecular mass of 86 kDa and four identical 22-kDa sub

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Williams, Richard E., Deborah A. Rathbone, Nigel S. Scrutton, and Neil C. Bruce. "Biotransformation of Explosives by the Old Yellow Enzyme Family of Flavoproteins." Applied and Environmental Microbiology 70, no. 6 (2004): 3566–74. http://dx.doi.org/10.1128/aem.70.6.3566-3574.2004.

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ABSTRACT Several independent studies of bacterial degradation of nitrate ester explosives have demonstrated the involvement of flavin-dependent oxidoreductases related to the old yellow enzyme (OYE) of yeast. Some of these enzymes also transform the nitroaromatic explosive 2,4,6-trinitrotoluene (TNT). In this work, catalytic capabilities of five members of the OYE family were compared, with a view to correlating structure and function. The activity profiles of the five enzymes differed substantially; no one compound proved to be a good substrate for all five enzymes. TNT is reduced, albeit slo

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Messiha, Hanan L., Thanyaporn Wongnate, Pimchai Chaiyen, Alex R. Jones, and Nigel S. Scrutton. "Magnetic field effects as a result of the radical pair mechanism are unlikely in redox enzymes." Journal of The Royal Society Interface 12, no. 103 (2015): 20141155. http://dx.doi.org/10.1098/rsif.2014.1155.

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Environmental exposure to electromagnetic fields is potentially carcinogenic. The radical pair mechanism is considered the most feasible mechanism of interaction between weak magnetic fields encountered in our environment and biochemical systems. Radicals are abundant in biology, both as free radicals and reaction intermediates in enzyme mechanisms. The catalytic cycles of some flavin-dependent enzymes are either known or potentially involve radical pairs. Here, we have investigated the magnetic field sensitivity of a number of flavoenzymes with important cellular roles. We also investigated t

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Kassay, Norbert, Vanda Toldi, József Tőzsér, and András Szabó. "Cigarette smoke toxin hydroquinone and misfolding pancreatic lipase variant cooperatively promote endoplasmic reticulum stress and cell death." PLOS ONE 17, no. 6 (2022): e0269936. http://dx.doi.org/10.1371/journal.pone.0269936.

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Mutation-induced protein misfolding of pancreatic secretory enzymes and consequent endoplasmic reticulum stress can cause chronic pancreatitis. A recent study revealed that cigarette smoke also increases the risk of the disease through endoplasmic reticulum stress. Here, we investigated the cumulative cellular effect of the G233E misfolding human pancreatic lipase variant and hydroquinone; a main toxic constituent of cigarette smoke, using mammalian cell lines. We found that hydroquinone reduces cell viability on a dose-dependent manner through programmed cell death, and diminishes lipase secr

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Spohn, Gabriele, Andre Kleinridders, F. Thomas Wunderlich, et al. "VKORC1 deficiency in mice causes early postnatal lethality due to severe bleeding." Thrombosis and Haemostasis 101, no. 06 (2009): 1044–50. http://dx.doi.org/10.1160/th09-03-0204.

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SummaryVitamin K hydroquinone is oxidised to the epoxide form (K>O) during vitamin K-dependent posttranslational γ-glutamyl carboxylation resulting in biological active so called vitamin K-dependent proteins. In turn, K>O is reduced by the enzyme VKORC1 (vitamin K epoxide reductase complex component 1) to complete the vitamin K cycle. To investigate the biological role of VKORC1 in vivo, we generated VKORC1 knockout mice. Homozygous VKORC1-deficient mice developed normally until birth. Within 2–20 days after birth, the knockout mice died due to extensive, predominantly intracerebral haem

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Zografos, Alexandros, and Marina Petsi. "Advances in Catalytic Aerobic Oxidations by Activation of Dioxygen-Monooxygenase Enzymes and Biomimetics." Synthesis 50, no. 24 (2018): 4715–45. http://dx.doi.org/10.1055/s-0037-1610297.

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Monooxygenases are not only some of the most versatile machineries in our lives, but also some of the most explored enzymes in modern organic synthesis. They provide knowledge and inspiration on how the most abandoned oxidant, dioxygen, can be activated and utilized to deliver selective oxidations. This review presents an outline in the mechanisms that Nature uses to succeed in these processes and recent indicative examples on how chemists use this knowledge to develop selective oxidation protocols based on dioxygen as the terminal oxidant.1 Introduction2 Monooxygenases2.1 Metal-Based Monooxyg

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Gao, Jinmin, Liyuan Li, Shijie Shen, et al. "Cofactor-independent C–C bond cleavage reactions catalyzed by the AlpJ family of oxygenases in atypical angucycline biosynthesis." Beilstein Journal of Organic Chemistry 20 (May 23, 2024): 1198–206. http://dx.doi.org/10.3762/bjoc.20.102.

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Biosynthesis of atypical angucyclines involves unique oxidative B-ring cleavage and rearrangement reactions, which are catalyzed by AlpJ-family oxygenases, including AlpJ, JadG, and GilOII. Prior investigations established the essential requirement for FADH2/FMNH2 as cofactors when utilizing the quinone intermediate dehydrorabelomycin as a substrate. In this study, we unveil a previously unrecognized facet of these enzymes as cofactor-independent oxygenases when employing the hydroquinone intermediate CR1 as a substrate. The enzymes autonomously drive oxidative ring cleavage and rearrangement

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Dzeja, Petras P., Peter Bast, Cevher Ozcan, et al. "Targeting nucleotide-requiring enzymes: implications for diazoxide-induced cardioprotection." American Journal of Physiology-Heart and Circulatory Physiology 284, no. 4 (2003): H1048—H1056. http://dx.doi.org/10.1152/ajpheart.00847.2002.

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Modulation of mitochondrial respiratory chain, dehydrogenase, and nucleotide-metabolizing enzyme activities is fundamental to cellular protection. Here, we demonstrate that the potassium channel opener diazoxide, within its cardioprotective concentration range, modulated the activity of flavin adenine dinucleotide-dependent succinate dehydrogenase with an IC50 of 32 μM and reduced the rate of succinate-supported generation of reactive oxygen species (ROS) in heart mitochondria. 5-Hydroxydecanoic fatty acid circumvented diazoxide-inhibited succinate dehydrogenase-driven electron flow, indicatin

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Gorlatova, Natalia, Marek Tchorzewski, Tatsuo Kurihara, Kenji Soda, and Nobuyoshi Esaki. "Purification, Characterization, and Mechanism of a Flavin Mononucleotide-Dependent 2-Nitropropane Dioxygenase fromNeurospora crassa." Applied and Environmental Microbiology 64, no. 3 (1998): 1029–33. http://dx.doi.org/10.1128/aem.64.3.1029-1033.1998.

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ABSTRACT A nitroalkane-oxidizing enzyme was purified to homogeneity fromNeurospora crassa. The enzyme is composed of two subunits; the molecular weight of each subunit is approximately 40,000. The enzyme catalyzes the oxidation of nitroalkanes to produce the corresponding carbonyl compounds. It acts on 2-nitropropane better than on nitroethane and 1-nitropropane, and anionic forms of nitroalkanes are much better substrates than are neutral forms. The enzyme does not act on aromatic compounds. When the enzyme reaction was conducted in an18O2 atmosphere with the anionic form of 2-nitropropane as

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Roberts, Kenneth M., José R. Tormos, and Paul F. Fitzpatrick. "Characterization of Unstable Products of Flavin- and Pterin-Dependent Enzymes by Continuous-Flow Mass Spectrometry." Biochemistry 53, no. 16 (2014): 2672–79. http://dx.doi.org/10.1021/bi500267c.

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