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Journal Abstract Search

508 related items for PubMed ID: 20193654

  • 1. The FMN-dependent two-component monooxygenase systems.
    Ellis HR.
    Arch Biochem Biophys; 2010 May; 497(1-2):1-12. PubMed ID: 20193654
    [Abstract] [Full Text] [Related]

  • 2. Vibrio harveyi flavin reductase--luciferase fusion protein mimics a single-component bifunctional monooxygenase.
    Jawanda N, Ahmed K, Tu SC.
    Biochemistry; 2008 Jan 08; 47(1):368-77. PubMed ID: 18067321
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  • 5. Investigations of two-component flavin-dependent monooxygenase systems.
    Robbins JM, Ellis HR.
    Methods Enzymol; 2019 Jan 08; 620():399-422. PubMed ID: 31072495
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  • 6. Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: Structural basis for the flavin affinity.
    Kim SH, Hisano T, Iwasaki W, Ebihara A, Miki K.
    Proteins; 2008 Feb 15; 70(3):718-30. PubMed ID: 17729270
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  • 9. Transformation of a Flavin-Free FMN Reductase to a Canonical Flavoprotein through Modification of the π-Helix.
    Musila JM, Ellis HR.
    Biochemistry; 2016 Nov 22; 55(46):6389-6394. PubMed ID: 27806563
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  • 10. Equilibrium and transient state spectrophotometric studies of the mechanism of reduction of the flavoprotein domain of P450BM-3.
    Sevrioukova I, Shaffer C, Ballou DP, Peterson JA.
    Biochemistry; 1996 Jun 04; 35(22):7058-68. PubMed ID: 8679531
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  • 11. Potentiometric and further kinetic characterization of the flavin-binding domain of Saccharomyces cerevisiae flavocytochrome b2. Inhibition by anions binding in the active site.
    Cénas N, Lê KH, Terrier M, Lederer F.
    Biochemistry; 2007 Apr 17; 46(15):4661-70. PubMed ID: 17373777
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  • 12. Two-Component Flavin-Dependent Riboflavin Monooxygenase Degrades Riboflavin in Devosia riboflavina.
    Kanazawa H, Shigemoto R, Kawasaki Y, Oinuma KI, Nakamura A, Masuo S, Takaya N.
    J Bacteriol; 2018 Jun 15; 200(12):. PubMed ID: 29610214
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  • 13. Mechanism for sulfur acquisition by the alkanesulfonate monooxygenase system.
    Ellis HR.
    Bioorg Chem; 2011 Dec 15; 39(5-6):178-84. PubMed ID: 21880344
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  • 14. Mechanism of flavin reduction in the alkanesulfonate monooxygenase system.
    Gao B, Ellis HR.
    Biochim Biophys Acta; 2007 Mar 15; 1774(3):359-67. PubMed ID: 17289450
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  • 16. Quantitation of FAD-dependent cytochrome P450 reductase activity by photoreduction.
    Hodgson AV, Strobel HW.
    Anal Biochem; 1996 Dec 01; 243(1):154-7. PubMed ID: 8954538
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  • 17. The reduced flavin-dependent monooxygenase SfnG converts dimethylsulfone to methanesulfinate.
    Wicht DK.
    Arch Biochem Biophys; 2016 Aug 15; 604():159-66. PubMed ID: 27392454
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  • 18. Electron transfer in flavocytochrome P450 BM3: kinetics of flavin reduction and oxidation, the role of cysteine 999, and relationships with mammalian cytochrome P450 reductase.
    Roitel O, Scrutton NS, Munro AW.
    Biochemistry; 2003 Sep 16; 42(36):10809-21. PubMed ID: 12962506
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  • 19. Deletional studies to investigate the functional role of a dynamic loop region of alkanesulfonate monooxygenase.
    Xiong J, Ellis HR.
    Biochim Biophys Acta; 2012 Jul 16; 1824(7):898-906. PubMed ID: 22564769
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  • 20. Resonance Raman study on the oxidized and anionic semiquinone forms of flavocytochrome b2 and L-lactate monooxygenase. Influence of the structure and environment of the isoalloxazine ring on the flavin function.
    Tegoni M, Gervais M, Desbois A.
    Biochemistry; 1997 Jul 22; 36(29):8932-46. PubMed ID: 9220981
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