A one-residue switch reverses the orientation of a heme b cofactor. Investigations of the ferriheme NO transporters nitrophorin 2 and 7 from the blood-feeding insect Rhodnius prolixus.

Abstract excerpt

This study represents the identification of a single amino acid residue that has the major responsibility for the isomeric orientation of a heme b cofactor in a ferriheme protein. The insertion of hemin b into the asymmetric environment of a protein pocket facilitates two cofactor orientations, A and B, which is often called "heme rotational disorder". The proteins studied herein are nitrophorins, a class of...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Circular Dichroism
• Share to Heme