Diversity of structures and functions of oxo-bridged non-heme diiron proteins.

ABSTRACT: Oxo-bridged diiron proteins are a distinct class of non-heme iron proteins. Their active sites are composed of two irons that are coordinated by amino acid side chains, and a bridging oxygen that interacts with each iron. These proteins are members of the ferritin superfamily and share the structural feature of a four α-helix bundle that provides the residues that coordinate the irons. The different proteins also display a wide range of structures and functions. A prototype of this family is hemerythrin, which functions as an oxygen transporter. Several other hemerythrin-like proteins have been described with a diversity of functions including oxygen and iron sensing, and catalytic activities. Rubrerythrins react with hydrogen peroxide and rubrerythrin-like proteins possess a rubredoxin do

SUBMITTER: Caldas Nogueira ML 

PROVIDER: S-EPMC8165033 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature