The flavin reductase ActVB from Streptomyces coelicolor: characterization of the electron transferase activity of the flavoprotein form [PDF]
FEBS Letters, Elsevier, 2005, 579, pp.2817-20, 2015 The flavin reductase ActVB is involved in the last step of actinorhodin biosynthesis in Streptomyces coelicolor. Although ActVB can be isolated with some FMN bound, this form was not involved in the flavin reductase activity. By studying the ferric reductase activity of ActVB, we show that its FMN-bound form exhibits a proper enzymatic activity of ...
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The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotides [PDF]
The journal of biological chemistry, American Society for
Biochemistry and Molecular Biology, 1999, 274, pp.18252-60, 2015 The NAD(P)H:flavin oxidoreductase from Escherichia coli, named Fre, is a monomer of 26.2 kDa that catalyzes the reduction of free flavins using NADPH or NADH as electron donor. The enzyme does not contain any prosthetic group but accommodates both the reduced pyridine nucleotide and the flavin in a ternary complex prior to oxidoreduction.
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Pulse radiolysis studies on superoxide reductase from Treponema pallidum [PDF]
FEBS Letters, Elsevier, 2001, 497, pp.171-3, 2015 Superoxide reductases (SORs) are small metalloenzymes, which catalyze reduction of O2*- to H2O2. The reaction of the enzyme from Treponema pallidum with superoxide was studied by pulse radiolysis methods. The first step is an extremely fast bi-molecular reaction of the ferrous center with O2, with a rate constant of 6 x 10 (8) M(-1) s(-1).
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The stability of 3 transmembrane and 4 transmembrane human vitamin K epoxide reductase models [PDF]
, 2016 3 transmembrane and 4 transmembrane helices models are suggested for the human vitamin K epoxide reductase (VKOR). In this study, we investigate the stability of the human 3 transmembrane/4 transmembrane VKOR models employing a coarse-grained normal mode analysis and molecular dynamics simulation.
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Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction [PDF]
Structure, 2004, 12, pp.1729-40, 2015 Some sulfate-reducing and microaerophilic bacteria rely on the enzyme superoxide reductase (SOR) to eliminate the toxic superoxide anion radical (O2*-). SOR catalyses the one-electron reduction of O2*- to hydrogen peroxide at a nonheme ferrous iron center. The structures of Desulfoarculus baarsii SOR (mutant E47A) alone and in complex with ferrocyanide
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Sampling of conformational ensemble for virtual screening using molecular dynamics simulations and normal mode analysis [PDF]
Future Medicinal Chemistry, 2015, 7 (17), pp.2317-2331, 2016 Aim: Molecular dynamics simulations and normal mode analysis are well-established approaches to generate receptor conformational ensembles (RCEs) for ligand docking and virtual screening. Here, we report new fast molecular dynamics-based and normal mode analysis-based protocols combined with conformational pocket classifications to efficiently generate
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Discovery of superoxide reductase: an historical perspective [PDF]
Journal of Biological Inorganic Chemistry, 2004, 9, pp.119-23, 2014 For more than 30 years, the only enzymatic system known to catalyze the elimination of superoxide was superoxide dismutase, SOD. SOD has been found in almost all organisms living in the presence of oxygen, including some anaerobic bacteria, supporting the notion that superoxide is a key and general component of oxidative stress. Recently, a new concept
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Detoxification of superoxide without production of H2O2: antioxidant activity of superoxide reductase complexed with ferrocyanide [PDF]
proceedings of the national Academy of Sciences of the United
States of America, PNAS, 2006, pp.14750-5, 2015 The superoxide radical O(2)(-.) is a toxic by-product of oxygen metabolism. Two O(2)(-.) detoxifying enzymes have been described so far, superoxide dismutase and superoxide reductase (SOR), both forming H2O2 as a reaction product. Recently, the SOR active site, a ferrous iron in a [Fe(2+) (N-His)(4) (S-Cys)] pentacoordination, was shown to have the ...
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A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor [PDF]
The journal of biological chemistry, American Society for
Biochemistry and Molecular Biology, 2004, 279, pp.44362-9, 2015 The two-component flavin-dependent monooxygenases belong to an emerging class of enzymes involved in oxidation reactions in a number of metabolic and biosynthetic pathways in microorganisms. One component is a NAD(P)H:flavin oxidoreductase, which provides a reduced flavin to the second component, the proper monooxygenase.
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How native state topology affects the folding of Dihydrofolate Reductase and Interleukin-1beta [PDF]
, 2000 The overall structure of the transition state and intermediate ensembles experimentally observed for Dihydrofolate Reductase and Interleukin-1beta can be obtained utilizing simplified models which have almost no energetic frustration. The predictive power of these models suggest that, even for these very large proteins with completely different folding
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