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  1. Artikel ; Online: Photophysical Studies of Helicate and Mesocate Double-Stranded Dinuclear Ru(II) Complexes.

    Xu, Xinyue / Marlton, Samuel J P / Flint, Kate L / Hudson, Rohan J / Keene, F Richard / Hall, Christopher R / Smith, Trevor A

    The journal of physical chemistry. A

    2024  Band 128, Heft 18, Seite(n) 3587–3595

    Abstract: The metal-ligand charge transfer ( ...

    Abstract The metal-ligand charge transfer (
    Sprache Englisch
    Erscheinungsdatum 2024-04-19
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 1520-5215
    ISSN (online) 1520-5215
    DOI 10.1021/acs.jpca.4c01996
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: The characterisation of two members of the cytochrome P450 CYP150 family: CYP150A5 and CYP150A6 from Mycobacterium marinum.

    Child, Stella A / Flint, Kate L / Bruning, John B / Bell, Stephen G

    Biochimica et biophysica acta. General subjects

    2019  Band 1863, Heft 5, Seite(n) 925–934

    Abstract: Background: Actinobacteria, including the Mycobacteria, have a large component of cytochrome P450 family monooxygenases. This includes Mycobacterium tuberculosis, M. ulcerans and M. marinum, and M. vanbaalenii. These enzymes can abstract CH bonds and ... ...

    Abstract Background: Actinobacteria, including the Mycobacteria, have a large component of cytochrome P450 family monooxygenases. This includes Mycobacterium tuberculosis, M. ulcerans and M. marinum, and M. vanbaalenii. These enzymes can abstract CH bonds and have important roles in natural product biosynthesis.
    Methods: Two members of the bacterial CYP150 family, CYP150A5 and CYP150A6 from M. marinum, were produced, purified and characterised. The potential substrate ranges of both enzymes were analysed and the monooxygenase activity of CYP150A5 was reconstituted using a physiological electron transfer partner system. CYP150A6 was structurally characterised by X-ray crystallography.
    Results: CYP150A5 was shown to bind various norisoprenoids and terpenoids. It could regioselectively hydroxylate β-ionol. The X-ray crystal structure of substrate-free CYP150A6 was solved to 1.5 Å. This displayed an open conformation with short F and G helices, an unresolved F-G loop region and exposed active site pocket. The active site residues could be identified and important variations were found among the CYP150A enzymes. Haem-binding azole inhibitors were identified for both enzymes.
    Conclusions: The structure of CYP150A6 will facilitate the identification of physiological substrates and the design of better inhibitors for members of this P450 family. Based on the observed differences in substrate binding preference and sequence variations among the active site residues, their roles are predicted to be different.
    General significance: Multiple CYP150 family members were found in many bacteria and are prevalent in the Mycobacteria including several human pathogens. Inhibition and structural data are reported here for these enzymes for the first time.
    Mesh-Begriff(e) Crystallography, X-Ray ; Cytochrome P-450 Enzyme System/chemistry ; Cytochrome P-450 Enzyme System/isolation & purification ; Cytochrome P-450 Enzyme System/metabolism ; Models, Molecular ; Mycobacterium tuberculosis/cytology ; Mycobacterium tuberculosis/enzymology ; Phylogeny
    Chemische Substanzen Cytochrome P-450 Enzyme System (9035-51-2)
    Sprache Englisch
    Erscheinungsdatum 2019-02-28
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbagen.2019.02.016
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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