title: Influence of conformational flexibility of their active sites on the electronic conductivity of enzymes.
abstract: The a.c. conductivity of the proteins lysozyme and subtilisin, both in their active and inactive or inhibited forms were determined theoretically. For this, quantum mechanical calculations and a random walk theory were used. The conclusions are that these enzymatic proteins can easily transport electrons which is most probably important in their role as catalysators of biochemical reactions. The electron transport is sensitive to three-dimensional changes of the active sites of these enzymes which have more flexibility than the whole molecule. Therefore, the flexibility of the active sites of enzyme catalysts is not only important for the conformational fitting with the reactants, but also strongly influences the transport in biochemical reactions.
authors.affiliation: Department of Protein Engineering, Chinese Academy of Science, Beijing.
authors.forename: U J
authors.initials: UJ
authors.lastname: Ye
authors.lastname: LadikJ
mesh_terms: D001665:Binding Sites; D004553:Electric Conductivity; D004798:Enzymes / Q000737:chemistry*; D008962:Models, Theoretical; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D013381:Subtilisins / Q000737:chemistry*
chemical_list: D004798:Enzymes; D009113:Muramidase; D013381:Subtilisins