First- and second-sphere contributions to Fe(II) site activation by cosubstrate binding in non-heme Fe enzymes.

ABSTRACT: Non-heme Fe(II) enzymes exhibit a general mechanistic strategy where binding all cosubstrates opens a coordination site on the Fe(II) for O2 activation. This study shows that strong-donor ligands, steric interactions with the substrate and second-sphere H-bonding to the facial triad carboxylate allow for five-coordinate site formation in this enzyme superfamily.

SUBMITTER: Light KM 

PROVIDER: S-EPMC3976902 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature