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    Probing the role of Val228 on the catalytic activity of Scytalidium catalase

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    Publication date
    2021-08
    End of Embargo
    2022-04-19
    Author
    Goc, G.
    Balci, B.A.
    Yorke, Briony A.
    Pearson, Y.
    Yuzugullu Karakus, Y.
    Keyword
    Catalase
    Lateral channel
    Heme
    Catechol
    Peer-Reviewed
    Yes
    Open Access status
    Not Open Access
    
    Metadata
    Show full item record
    Abstract
    Scytalidium catalase is a homotetramer including heme d in each subunit. Its primary function is the dismutation of H2O2 to water and oxygen, but it is also able to oxidase various small organic compounds including catechol and phenol. The crystal structure of Scytalidium catalase reveals the presence of three linked channels providing access to the exterior like other catalases reported so far. The function of these channels has been extensively studied, revealing the possible routes for substrate flow and product release. In this report, we have focussed on the semi-conserved residue Val228, located near to the vinyl groups of the heme at the opening of the lateral channel. Its replacement with Ala, Ser, Gly, Cys, Phe and Ile were tested. We observed a significant decrease in catalytic efficiency in all mutants with the exception of a remarkable increase in oxidase activity when Val228 was mutated to either Ala, Gly or Ser. The reduced catalytic efficiencies are characterized in terms of the restriction of hydrogen peroxide as electron acceptor in the active centre resulting from the opening of lateral channel inlet by introducing the smaller side chain residues. On the other hand, the increased oxidase activity is explained by allowing the suitable electron donor to approach more closely to the heme. The crystal structures of V228C and V228I were determined at 1.41 and 1.47 Å resolution, respectively. The lateral channels of the V228C and V228I presented a broadly identical chain of arranged waters to that observed for wild-type enzyme.
    URI
    http://hdl.handle.net/10454/18573
    Version
    No full-text in the repository
    Citation
    Goc G, Balci BA, Yorke BA et al (2021) Probing the role of Val228 on the catalytic activity of Scytalidium catalase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomimcs. 1869(8): 140662.
    Link to publisher’s version
    https://doi.org/10.1016/j.bbapap.2021.140662
    Type
    Article
    Notes
    The full-text of this article will be released for public view at the end of the publisher embargo on 19 Apr 2022.
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    Life Sciences Publications

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