Structural assignment of spectra by characterization of conformational substates in bound MbCO.

ABSTRACT: Residue motions of the distal heme pocket and bound CO ligand of carbonmonoxy Myoglobin are studied using a combination of molecular dynamics simulations and quantum chemical methods. Using mixed quantum mechanics/molecular mechanics calculations together with sampling from molecular dynamics simulations (QM/MM(MD)), the experimentally observed spectroscopic A(0) and A(1) substates of the bound CO ligand are assigned to the open and closed conformation of His(64) and the His(epsilon)(64) tautomer, respectively. Several previously proposed origins of the A(3) substate, including rotamers of the doubly protonated His(64)H(+) side chain, His(64)H(+) inside the distal pocket, and cooperative motions with Arg(45), are investigated with QM/MM(MD). However, the signatures of the calculated infrar

SUBMITTER: Devereux M 

PROVIDER: S-EPMC2711460 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature