Structural Changes of the Trinuclear Copper Center in Bilirubin Oxidase upon Reduction.

ABSTRACT: Geometric and electronic structure changes in the copper (Cu) centers in bilirubin oxidase (BOD) upon a four-electron reduction were investigated by quantum mechanics/molecular mechanics (QM/MM) calculations. For the QM region, the unrestricted density functional theory (UDFT) method was adopted for the open-shell system. We found new candidates of the native intermediate (NI, intermediate II) and the resting oxidized (RO) states, i.e., NI^H+ and RO₀. Elongations of the Cu-Cu atomic distances for the trinuclear Cu center (TNC) and very small structural changes around the type I Cu (T1Cu) were calculated as the results of a four-electron reduction. The QM/MM optimized structures are in good agreement with recent high-resolution X-ray structures. As the structural change in the TNC

SUBMITTER: Tokiwa T 

PROVIDER: S-EPMC6337666 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature