Relevant bibliographies by topics / Flavin hydroquinone dependent Enzymes

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  2. Dissertations / Theses
  3. Books
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Academic literature on the topic 'Flavin hydroquinone dependent Enzymes'

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Published: 25 May 2024

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Journal articles on the topic "Flavin hydroquinone dependent Enzymes"

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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 (August 24, 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 maleylacetate reductase gene, npdC. In an in vitro assay containing NpdA2, an E. coli lysate transforms p-nitrophenol stoichiometrically to hydroquinone and hydroxyquinol. It was concluded that the p-nitrophenol catabolic pathway in JS443 most likely begins with a two-step transformation of p-nitrophenol to hydroxy-1,4-benzoquinone, catalyzed by NpdA2. Hydroxy-1,4-benzoquinone is reduced to hydroxyquinol, which is degraded through the hydroxyquinol ortho cleavage pathway. The hydroquinone detected in vitro is a dead-end product most likely resulting from chemical or enzymatic reduction of the hypothetical intermediate 1,4-benzoquinone. NpdA2 hydroxylates a broad range of chloro- and nitro-substituted phenols, resorcinols, and catechols. Only p-nitro- or p-chloro-substituted phenols are hydroxylated twice. Other substrates are hydroxylated once, always at a position para to a hydroxyl group.
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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 (February 9, 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 nicotine blue, several other quinones were reduced by the enzyme. The NAD(P)H-nicotine blue oxidoreductase may prevent intracellular one-electron reductions of nicotine blue which may lead to semiquinone radicals and potentially toxic reactive oxygen species.
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Hyster, Todd K. "Radical Biocatalysis: Using Non-Natural Single Electron Transfer Mechanisms to Access New Enzymatic Functions." Synlett 31, no. 03 (May 7, 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 for catalyzing non-natural radical reactions within enzyme active sites are, however, undeveloped. In this account, we highlight three distinct strategies developed in our group that exploit non-natural single electron transfer mechanisms to unveil previously unknown radical biocatalytic functions. These strategies allow common oxidoreductases to be used to address the enduring synthetic challenge of asymmetric hydrogen atom transfer.1 Introduction2 Photoinduced Electron Transfer from NADPH3 Ground State Electron Transfer from Flavin Hydroquinone4 Enzymatic Redox Activation in NADPH-Dependent Oxidoreductases5 Conclusion
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Wojcieszyńska, Danuta, Katarzyna Hupert-Kocurek, and Urszula Guzik. "Flavin-Dependent Enzymes in Cancer Prevention." International Journal of Molecular Sciences 13, no. 12 (December 7, 2012): 16751–68. http://dx.doi.org/10.3390/ijms131216751.

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

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Menon, Binuraj R. K., Jonathan Latham, Mark S. Dunstan, Eileen Brandenburger, Ulrike Klemstein, David Leys, Chinnan Karthikeyan, Michael F. Greaney, Sarah A. Shepherd, and Jason Micklefield. "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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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 (June 5, 2020): 6481–99. http://dx.doi.org/10.1007/s00253-020-10705-w.

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Moon, Shin, and Choe. "Crystal Structures of Putative Flavin Dependent Monooxygenase from Alicyclobacillus Acidocaldarius." Crystals 9, no. 11 (October 23, 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 binding pocket and phylogenetic analysis showed that this protein is more closely related to other bacterial group D flavin dependent monooxygenases, such as DszC (sulfoxidase) and DnmZ and Kijd3 (nitrososynthases).
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Shepherd, Sarah A., Chinnan Karthikeyan, Jonathan Latham, Anna-Winona Struck, Mark L. Thompson, Binuraj R. K. Menon, Matthew Q. Styles, Colin Levy, David Leys, and Jason Micklefield. "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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Saleem-Batcha, Raspudin, Frederick Stull, Jacob N. Sanders, Bradley S. Moore, Bruce A. Palfey, K. N. Houk, and Robin Teufel. "Enzymatic control of dioxygen binding and functionalization of the flavin cofactor." Proceedings of the National Academy of Sciences 115, no. 19 (April 23, 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 regiospecific formation of a covalent flavin–oxygen adduct and oxygenating species (i.e., the flavin-N5-oxide) by mimicking a critical transition state. This study unambiguously demonstrates how enzymes may control the O2 functionalization of an organic cofactor as prerequisite for oxidative catalysis. Our work thus illustrates how O2 reactivity can be harnessed in an enzymatic environment and provides crucial knowledge for future rational design of O2-reactive enzymes.
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Dissertations / Theses on the topic "Flavin hydroquinone dependent Enzymes"

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Röllig, Robert. "Chemical hydride transfer for flavin dependent monooxygenases of two-component systems." Electronic Thesis or Diss., Aix-Marseille, 2021. http://www.theses.fr/2021AIXM0436.

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Le terme monooxygénases flavoprotéiques (flavoprotein monooxygenases FPMO) recouvre aussi bien des flavoenzymes formées d’une seule composante que de deux. L'indépendance fonctionnelle de la partie oxygénase de la 2,5-dicétocamphane 1,2-monooxygénase I (2,5-DKCMO), une Baeyer-Villiger monooxygénase de type II, FMN dépendante, de sa contrepartie réductase, ainsi que le mécanisme de transfert de la flavine par libre diffusion, ont été étudiés dans des réactions sans réductase mais où des analogues biomimétiques synthétiques de nicotinamide (NCB) ont été utilisés pour réduire le FMN. L'équilibre entre la réduction de la flavine et la (ré)oxydation enzymatique a été identifié comme le goulot d'étranglement du système. Dans le but de trouver des donneurs d'hydrure potentiellement rentables pour les réactions d'oxydoréduction enzymatique, des stratégies de réduction de la flavine, indépendantes des cofacteurs nicotinamide naturels et biomimétiques, ont été étudiées. La capacité d’un complexe d’iridium III à transférer des hydrures afin de réduire la flavine a été exploitée. [Cp*Ir(bpy-OMe)H]+ (Ir* (H+)), résistant au pH et à l'oxygène, a permis la réaction enzymatique de monooxygénases respectivement FMNH2 et FADH2 dépendantes, 2,5-DKCMO et la styrène monooxygénase de sphingopyxis fribergensis Kp.5.2 (SfStyA). L’utilisation du système Ir* (H+)/SfStyA a conduit à une augmentation de six fois de l’état de l’art en terme de turn over number (TON) d’un catalyseur métallique. Cependant des améliorations sont encore nécessaires pour confirmer cette approche comme un accès prometteur à une plate-forme technologique efficace et versatile, pour l’utilisation de flavoenzymes
The term flavoprotein monooxygenases (FPMO) covers two different types of flavoenzymes: single and two component oxygenases. Two component FPMOs consist of a reductase and an oxygenating enzyme. The functional independence of the oxygenase part of 2,5-diketocamphane 1,2-monooxygenase I (2,5 DKCMO), an FMN dependent type II Baeyer-Villiger monooxygenase, from the reductase counterpart, as well as the mechanism of flavin transfer by free diffusion, was investigated in a reductase-free reaction, using synthetic nicotinamide biomimetics (NCBs) for the reduction of FMN. The balance of flavin reduction and enzymatic (re)oxidation was identified as the bottleneck of the system. Aiming for potentially cost efficient hydride donors for enzymatic redox reactions, nicotinamide coenzyme and nicotinamide biomimetic independent flavin reduction strategies were investigated. The capability of the pH and oxygen robust iridium III complex [Cp*Ir(bpy-OMe)H]+ (Ir* (H+)) to transfer hydrides for flavin reduction for the enzymatic reaction of respectively FMNH2 and FADH2 dependent monooxygenases, 2,5 DKCMO and styrene monooxygenase from Sphingopyxis fribergensis Kp.5.2 (SfStyA) was exploited. The Ir* (H+)/SfStyA approach outperformed the state of the art system by six-fold in terms of turn over number of the metal catalyst. Nevertheless, the robustness of the system remains challenging, and improvements are required to establish the approach as an efficient and versatile platform technology for flavoenzymes
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Karunaratne, Kalani Udara. "Probing the methylene and hydride transfers in flavin- dependent thymidylate synthase." Diss., University of Iowa, 2018. https://ir.uiowa.edu/etd/6443.

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All organisms must maintain an adequate level of thymidylate, which gets phosphorylated twice and then utilized by DNA polymerases for DNA replication that must precede cell division. Most organisms rely on classical thymidylate synthase (TSase) for this function. However, a subset of microorganisms – including a number of notable, widespread human pathogens – relies on an enzyme with a distinct structure and catalytic strategy. This enzyme is termed flavin-dependent thymidylate synthase (FDTS), as the flavin is required for thymidylate production. Because of this considerable orthogonality between FDTS and classical TSase, FDTS serves as a promising target for new therapeutics – one that could have only mild adverse effects on the host organism. FDTS catalyzes the reductive methylation of uridylate (2′-deoxyuridine-5′-monophosphate; dUMP) to yield thymidylate (2′-deoxythymidine-5′-monophosphate; dTMP). The methylene originally resides on CH2H4folate and is eventually transferred to the nucleotide. This methylene’s route to dUMP is unique in enzymology, and our experiments described herein strive to gain an understanding of the molecular details of its transfer. Compounds that mimic intermediates and transition states along this path are likely to bind FDTS tightly and could be leads for drugs, and our new insights could facilitate this. After methylene transfer is complete, a hydride transfer from flavin to the nucleotide occurs. We utilized rapid quench flow techniques in heavy water to follow the hydrogen transfers in FDTS; solvent isotope effects were measured and analyzed, furnishing evidence that the hydride transfer contributes to rate limitation. Reconstitution of the enzyme with unnatural flavins both reinforced these conclusions and suggested new hypotheses and experiments.
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Yuan, Hongling. "Mechanistic Studies of Two Selected Flavin-Dependent Enzymes: Choline Oxidase and D-Arginine Dehydrogenase." Digital Archive @ GSU, 2011. http://digitalarchive.gsu.edu/chemistry_diss/56.

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Choline oxidase catalyzes the flavin-dependent, two-step oxidation of choline to glycine betaine via the formation of an aldehyde intermediate. The oxidation of choline includes two reductive half-reactions followed by oxidative half-reactions. In the first oxidation reaction, the alcohol substrate is activated to its alkoxide via proton abstraction and oxidized via transfer of a hydride from the alkoxide α-carbon to the N(5) atom of the enzyme-bound flavin. In the wild-type enzyme, proton and hydride transfers are mechanistically and kinetically uncoupled. The role of Ser101 was investigated in this dissertation. Replacement of Ser101 with threonine, alanine, cysteine, or valine demonstrated the importance of the hydroxyl group of Ser101 in proton abstraction and in hydride transfer. Moreover, the kinetic studies on the Ser101Ala variant have revealed the importance of a specific residue for the optimization of the overall turnover of choline oxidase. The UV-visbible absorbance of Ser101Cys suggests Cys101 can form an adduct with the C4a atom of the flavin. The mechanism of formation of the C4a-cysteinyl adduct has been elucidated. D-arginine dehydrogenase (DADH) catalyzes the oxidation of D-amino acids to the corresponding imino acids, which are non-enzymatically hydrolyzed to α-keto acids and ammonia. The enzyme is strick dehrogenase and deoesnot react with molecular oxygen. Steady state kinetic studies wirh D-arginine and D-histidine as a substrate and PMS as the electron acceptor has been investigated. The enzyme has broad substrate specificity for D-amino acids except aspartate, glutamate and glycine, with preference for arginine and lysine. Leucine is the slowest substrate in which steady state kinetic parameters can be obtained. The chemical mechanism of leucine dehydrogenation catalyzed by DADH was explored with a combination of pH, substrate and solvent kinetic isotope effects (KIE) and proton inventories by using rapid kinetics in a stopped-flow spectrophotometer. The data are discussed in the context of the crystallographic structures at high resolutions (<1.3 Å) of the enzyme in complex with iminoarginine or iminohistidine.
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Wehelie, Rahma. "Mycoplasma pyrimidine deoxynucleotide biosynthesis : molecular characterization of a new family flavin-dependent thymidylate synthase /." Uppsala : Dept. of Molecular Biosciences, Swedish University of Agricultural Sciences, 2006. http://epsilon.slu.se/200676.pdf.

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Lee, Brendon. "The Role of F420-dependent Enzymes in Mycobacteria." Phd thesis, Canberra, ACT : The Australian National University, 2017. http://hdl.handle.net/1885/148416.

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Tuberculosis (TB) is the leading cause of death by an infectious disease, recently surpassing HIV/AIDS. The causative agent, Mycobacterium tuberculosis, is difficult to treat as it can survive harsh conditions and can switch between an active infection, which causes ~1.5 million deaths a year, and a latent state, which infects up to one third of the world’s population. M. tuberculosis is also becoming more resistant to frontline drugs, making it a dangerous world epidemic. It is therefore essential that new treatments are developed to help combat TB. A new enzyme superfamily has recently been discovered that utilises the rare co-factor F420, which is not produced or utilized by humans, allowing for specific drug targeting of the mostly uncharacterized enzymes that utilise it. The aim of this thesis is to better understand the roles of these enzymes in Mycobacteria and to investigate the mechanism by which M. tuberculosis might evolve resistance to a new class of prodrugs that are activated by the F420-dependent enzyme deazaflavin-dependent nitroreductase (Ddn). Prodrugs that are activated by Ddn include pretomanid and delamanid, which are effective against both an active and latent TB infection. Ddn is natively a quinone reductase, but also reacts with these drugs to reduce them, thereby releasing nitrous oxide and other breakdown products that are thought to inhibit hydroxymycolic acid dehydrogenase. Resistance against pretomanid in vitro has been documented in laboratory studies to occur via mutations to the F420 biosynthetic pathway, the enzyme F420-dependent glucose-6-phosphate dehydrogenase that reduces F420, and Ddn. However, the fitness cost of such mutations, i.e. whether they would still be virulent and transmissible, has not been studied. This important question will determine whether such genetic changes could lead to clinically relevant resistance. I explored this question with a detailed study of Ddn to establish (i) whether its activity is essential for the fitness of M. tuberculosis and (ii) whether any mutations could knock out the prodrug-activating activity without substantially affecting the native quinone reductase activity. I investigated this by better defining the physiological role of Ddn, showing that it can reduce menaquinone, and that this activity can enhance respiration of the cell by coupling with cytochrome bd. I also demonstrated that Ddn orthologues have similar quinone reductase activity as Ddn, but have no activity with pretomanid, except for the M. marinum orthologue that has activity with both. Through site directed mutagenesis I have identified a number of mutations to Ddn’s active site that eliminate activity with pretomanid while retaining some quinone reductase activity. A clinical strain that had acquired one of the tested mutations v through neutral genetic drift/variation showed resistance to pretomanid, despite never having been exposed to the compound. Interestingly, the other nitroimidazole prodrug, delamanid, was still effective Computational modelling suggets this to be due to the way that each nitroimidazole binds Ddn. The first step to developing a new drug to target an F420-dependent enzyme, we first need to identify genes/proteins that are essential for some aspect of the life cycle of M. tuberculsosis. Collaborators have shown that the F420-dependent enzyme Rv0121c (homologous to MSMEG_6526 in Mycobacterium smegmatis) from the flavin/deazaflavin oxidoreductase (FDOR) protein superfamily is essential for escape from dormancy. As a model for M. tuberculosis we made a MSMEG_6526 knockout in M. smegmatis and confirmed that it is conditionally essential. This was demonstrated by the slower growth rate of Δ6526 compared to wildtype in minimal media with several different carbon sources, and the lack of growth on acetate and pyruvate. Proteomics showed the upregulation of the methylcitrate cycle, glyoxylate cycle, and several F420-dependent enzymes, including the Ddn orthologue MSMEG_2027. Proteins that were downregulated were part of the Kerbs cycle, late stage glycolysis, and several amino acid metabolomic pathways. This was complemented with metabolomics, revealing several metabolites that were affected by the MSMEG_6526 knockout. The pathway that these metabolites were involved in included the Krebs cycle and several related amino acid metabolic pathways. This suggests that MSMEG_6526 is somehow involved in amino acid metabolism. The crystal structures of Rv0121c and MSMEG_6526 in complex with F420 were solved, revealing homodimers of the split β-barrel fold that defines the FDOR super family. The structures revealed three extended loops, two of which made a more defined active site compared to other FDORs. The third loop was not involved with the active site and is not conserved between the two enzymes, while the active site and F420 binding are highly conserved. The structure was also used to identify the type of substrates that can bind these enzymes. The other chapters presented in this thesis are collaborative projects that I had contributed towards. These include detailed characterization of the FDOR superfamily in which a number of specific sub-groups of the FDOR superfamily based on sequence similarity and structural motifs. We also identified novel F420-dependent biliverdin reductases in M. tuberculosis that reduce bilirubin, a known antioxidant. Finally, we expand the list of chemicals that FDORs has promiscuous activity with, including antimicrobials that we show are more vi potent with F420 knocked out. The final chapter is a comprehensive review of F420, it precursor Fo, and related enzymes in Mycobacteria, methanogens, and other bacteria that utilise it.
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Goldman, Peter John. "The roles of redox active cofactors in catalysis : structural studies of iron sulfur cluster and flavin dependent enzymes." Thesis, Massachusetts Institute of Technology, 2013. http://hdl.handle.net/1721.1/82313.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2013.
Cataloged from PDF version of thesis.
Includes bibliographical references.
Cofactors are highly prevalent in biological systems and have evolved to take on many functions in enzyme catalysis. Two cofactors, flavin adenine dinucleotide (FAD) and [4Fe-4S] clusters, were originally determined to aid in electron transfer and redox chemistry. However, additional activities for these cofactors continue to be discovered. The study of FAD in the context of rebeccamycin and staurosporine biosynthesis has yielded another role for this cofactor in the enzyme StaC. A homolog of this enzyme, RebC, uses its FAD cofactor in the oxidation of 7-carboxy-K252c. StaC also uses 7-carboxy-K252 as a substrate, but its reaction does not result in a redox transformation. Biochemical and X-ray crystallographic methods were employed to determine that, indeed, the role of FAD in the StaC system is not to catalyze redox chemistry. Instead, FAD sterically drives an initial decarboxylation event. Subtle differences in the active sites of RebC and StaC promote this redox neutral decarboxylation, by activating water for a final protonation step. In another system, the characterization of the S-adenosyl-L-methionine (AdoMet) radical superfamily showed the versatility of these cofactors. In this superfamily, which includes over 40,000 unique sequences, [4Fe-4S] clusters are responsible for the initiation of radical chemistry. A recently described subclass of this superfamily, the dehydrogenases, require additional [4Fe-4S] cluster for activity. This requirement led to the hypothesis that these enzymes are catalyzing redox chemistry by directly ligating substrates to auxiliary (Aux) clusters. X-ray structures of 2-deoxy-scyllo-inosamine dehydrogenase (BtrN), required for the biosynthesis of 2-deoxystreptamine, and an anaerobic sulfatase maturating enzyme, anSMEcpe, which installs a required formylglycine posttranslational modification, refute this hypothesis. In these structures, substrate binding is distal from each enzymes' Aux clusters. However, the Aux cluster binding architecture shared between BtrN, anSMEcpe, and another AdoMet radical enzyme, MoaA, involved in molybdenum cofactor biosynthesis, suggests that the structural features will be a staple in the AdoMet radical superfamily, common to - 30% of the AdoMet radical reactions.
by Peter John Goldman.
Ph.D.
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Kubitza, Christian [Verfasser], Axel [Akademischer Betreuer] Scheidig, and Bernd [Gutachter] Clement. "Structural Characterization of Flavin-dependent Monooxygenases from Zonocerus variegatus and the Human Mitochondrial Amidoxime Reducing Component (mARC) – Enzymes involved in Biotransformation / Christian Kubitza ; Gutachter: Bernd Clement ; Betreuer: Axel Scheidig." Kiel : Universitätsbibliothek Kiel, 2018. http://d-nb.info/1237685664/34.

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Books on the topic "Flavin hydroquinone dependent Enzymes"

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Tamanoi, Fuyuhiko, and Pimchai Chaiyen. Flavin-Dependent Enzymes. Elsevier Science & Technology, 2020.

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Tamanoi, Fuyuhiko, and Pimchai Chaiyen. Flavin-Dependent Enzymes. Elsevier Science & Technology Books, 2020.

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Flavin-Dependent Enzymes: Mechanisms, Structures and Applications. Elsevier, 2020. http://dx.doi.org/10.1016/s1874-6047(20)x0002-3.

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Book chapters on the topic "Flavin hydroquinone dependent Enzymes"

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Fagan, Rebecca L., and Bruce A. Palfey. "Flavin-Dependent Enzymes." In Comprehensive Natural Products II, 37–113. Elsevier, 2010. http://dx.doi.org/10.1016/b978-008045382-8.00135-0.

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Pimviriyakul, Panu, and Pimchai Chaiyen. "Flavin-dependent dehalogenases." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications, 365–97. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.05.010.

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Pimviriyakul, Panu, and Pimchai Chaiyen. "Overview of flavin-dependent enzymes." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications, 1–36. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.06.006.

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Saaret, Annica, Arune Balaikaite, and David Leys. "Biochemistry of prenylated-FMN enzymes." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications, 517–49. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.05.013.

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Phintha, Aisaraphon, Kridsadakorn Prakinee, and Pimchai Chaiyen. "Structures, mechanisms and applications of flavin-dependent halogenases." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications, 327–64. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.05.009.

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"Copyright." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications, iv. Elsevier, 2020. http://dx.doi.org/10.1016/s1874-6047(20)30035-4.

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"Contributors." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications, xi—xiv. Elsevier, 2020. http://dx.doi.org/10.1016/s1874-6047(20)30037-8.

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Chaiyen, Pimchai, and Fuyuhiko Tamanoi. "Preface." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications, xv—xvi. Elsevier, 2020. http://dx.doi.org/10.1016/s1874-6047(20)30038-x.

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Hall, Mélanie. "Flavoenzymes for biocatalysis." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications, 37–62. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.05.001.

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Martin, Caterina, Claudia Binda, Marco W. Fraaije, and Andrea Mattevi. "The multipurpose family of flavoprotein oxidases." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications, 63–86. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.05.002.

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You might also be interested in the extended bibliographies on the topic 'Flavin hydroquinone dependent Enzymes' for particular source types:
Journal articles
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