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387 related items for PubMed ID: 2990445

  • 1. Laser-flash-photolysis studies of p-cresol methylhydroxylase. Electron-transfer properties of the flavin and haem components.
    Bhattacharyya A, Tollin G, McIntire W, Singer TP.
    Biochem J; 1985 Jun 01; 228(2):337-45. PubMed ID: 2990445
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  • 2. Transient kinetics of intracomplex electron transfer in the human cytochrome b5 reductase-cytochrome b5 system: NAD+ modulates protein-protein binding and electron transfer.
    Meyer TE, Shirabe K, Yubisui T, Takeshita M, Bes MT, Cusanovich MA, Tollin G.
    Arch Biochem Biophys; 1995 Apr 20; 318(2):457-64. PubMed ID: 7733677
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  • 8. Functional interactions in cytochrome P450BM3: flavin semiquinone intermediates, role of NADP(H), and mechanism of electron transfer by the flavoprotein domain.
    Murataliev MB, Klein M, Fulco A, Feyereisen R.
    Biochemistry; 1997 Jul 08; 36(27):8401-12. PubMed ID: 9204888
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  • 9. Laser flash photolysis studies of the reduction kinetics of NADPH:cytochrome P-450 reductase.
    Bhattacharyya AK, Lipka JJ, Waskell L, Tollin G.
    Biochemistry; 1991 Jan 22; 30(3):759-65. PubMed ID: 1899033
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  • 10. Steady-state and laser flash induced photoreduction of yeast glutathione reductase by 5-deazariboflavin and by a viologen analogue: stabilization of flavin adenine dinucleotide semiquinone species by complexation.
    Navarro JA, Roncel M, Tollin G.
    Biochemistry; 1990 Jun 26; 29(25):6102-7. PubMed ID: 2383572
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  • 14. Laser flash photolysis studies of electron transfer between ferredoxin-NADP+ reductase and several high-potential redox proteins.
    Bhattacharyya AK, Meyer TE, Cusanovich MA, Tollin G.
    Biochemistry; 1987 Feb 10; 26(3):758-64. PubMed ID: 3032236
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  • 15. Chromatium vinosum cytochrome c-552. Reduction by photoreduced flavins and intramolecular electron transfer.
    Cusanovich MA, Tollin G.
    Biochemistry; 1980 Jul 08; 19(14):3343-7. PubMed ID: 6250567
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  • 16. Transient kinetics of redox reactions of flavodoxin: effects of chemical modification of the flavin mononucleotide prosthetic group on the dynamics of intermediate complex formation and electron transfer.
    Simondsen RP, Tollin G.
    Biochemistry; 1983 Jun 07; 22(12):3008-16. PubMed ID: 6307350
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  • 17. Comparison of the processes involved in reduction by the substrate for two homologous flavocytochromes b2 from different species of yeast.
    Capeillère-Blandin C, Barber MJ, Bray RC.
    Biochem J; 1986 Sep 15; 238(3):745-56. PubMed ID: 3026360
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  • 18. Ionic strength dependence of the kinetics of electron transfer from bovine mitochondrial cytochrome c to bovine cytochrome c oxidase.
    Hazzard JT, Rong SY, Tollin G.
    Biochemistry; 1991 Jan 08; 30(1):213-22. PubMed ID: 1846288
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  • 19. Flavocytochrome b2: kinetic studies by absorbance and electron-paramagnetic-resonance spectroscopy of electron distribution among prosthetic groups.
    Capeillère-Blandin C, Bray RC, Iwatsubo M, Labeyrie F.
    Eur J Biochem; 1975 Jun 08; 54(2):549-66. PubMed ID: 170093
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  • 20. p-Cresol methylhydroxylase. Assay and general properties.
    McIntire W, Hopper DJ, Singer TP.
    Biochem J; 1985 Jun 01; 228(2):325-35. PubMed ID: 2990444
    [Abstract] [Full Text] [Related]

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