Properties Of The High-Spin Heme Of Maug Are Altered By Binding Of Premadh At The Protein Surface 40 Å Away

Keywords

electron transfer; ferryl heme; peroxidase; protein-protein interaction; proton transfer

Abstract

The diheme enzyme MauG catalyzes oxidative post-translational modifications of a protein substrate, precursor protein of methylamine dehydrogenase (preMADH), that binds to the surface of MauG. The high-spin heme iron of MauG is located 40 Å from preMADH. The ferric heme is an equilibrium of five- and six-coordinate states. PreMADH binding increases the proportion of five-coordinate heme three-fold. On reaction of MauG with H2O2 both hemes become FeIV. In the absence of preMADH the hemes autoreduce to ferric in a multistep process involving multiple electron and proton transfers. Binding of preMADH in the absence of catalysis alters the mechanism of autoreduction of the ferryl heme. Thus, substrate binding alters the environment in the distal heme pocket of the high-spin heme over very long distance.

Publication Date

6-1-2017

Publication Title

FEBS Letters

Volume

591

Issue

11

Number of Pages

1566-1572

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1002/1873-3468.12666

Socpus ID

85019627366 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/85019627366

This document is currently not available here.

Share

COinS