Functionalization of Bacterial Microcompartment Shell Proteins With Covalently Attached Heme.

ABSTRACT: Heme is a versatile redox cofactor that has considerable potential for synthetic biology and bioelectronic applications. The capacity to functionalize non-heme-binding proteins with covalently bound heme moieties in vivo could expand the variety of bioelectronic materials, particularly if hemes could be attached at defined locations so as to facilitate position-sensitive processes like electron transfer. In this study, we utilized the cytochrome maturation system I to develop a simple approach that enables incorporation of hemes into the backbone of target proteins in vivo. We tested our methodology by targeting the self-assembling bacterial microcompartment shell proteins, and inserting functional hemes at multiple locations in the protein backbone. We found substitution of three amino ac

SUBMITTER: Huang J 

PROVIDER: S-EPMC6962350 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature