Quantum cluster size and solvent polarity effects on the geometries and Mossbauer properties of the active site model for ribonucleotide reductase intermediate X: a density functional theory study.

ABSTRACT: In studying the properties of metalloproteins using ab initio quantum mechanical methods, one has to focus on the calculations on the active site. The bulk protein and solvent environment is often neglected, or is treated as a continuum dielectric medium with a certain dielectric constant. The size of the quantum cluster of the active site chosen for calculations can vary by including only the first-shell ligands which are directly bound to the metal centers, or including also the second-shell residues which are adjacent to and normally have H-bonding interactions with the first-shell ligands, or by including also further hydrogen bonding residues. It is not well understood how the size of the quantum cluster and the value of the dielectric constant chosen for the calculations will influen

SUBMITTER: Han WG 

PROVIDER: S-EPMC2863024 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature