[Fe-Fe]-hydrogenase Reactivated by Residue Mutations as Bridging Carbonyl Rearranges: A QM/MM Study.

ABSTRACT: In the current work, we found aqueous enzyme phase reaction pathways for the reactivation of the exogenously inhibited [Fe-Fe]-hydrogenases by O₂, or OH^-, which metabolizes to H₂O^1,2. We used the hybrid quantum mechanics/molecular mechanics (QM/MM) method to study the reactivation pathways of the exogenously inhibited enzyme matrix. The ONIOM calculations performed on the enzyme agree with experimental results³, i.e., wild-type [Fe-Fe]-hydrogenase H-cluster is inhibited by oxygen metabolites. An enzyme spherical region with a radius of 8 Å (from the distal iron, Fe_d) has been screened for residues that prevent H₂O from leaving the catalytic site and reactivate the [Fe-Fe]-hydrogenase H-cluster. In the screening pr

SUBMITTER: Motiu S 

PROVIDER: S-EPMC4452136 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature