The affinity of MhuD for heme is consistent with a heme degrading function in vivo

Biswash Thakuri; Amanda B. Graves; Alex Chao; Sommer L. Johansen; Celia W. Goulding; Matthew D. Liptak

doi:10.1039/C8MT00238J

The affinity of MhuD for heme is consistent with a heme degrading function in vivo†

Biswash Thakuri,^a Amanda B. Graves,^a Alex Chao,

^b Sommer L. Johansen,^a Celia W. Goulding

^bc and Matthew D. Liptak

*^a

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* Corresponding authors

^a Department of Chemistry, University of Vermont, Burlington, Vermont 05405, USA
E-mail: matthew.liptak@uvm.edu

^b Department of Molecular Biology and Biochemistry, University of California-Irvine, Irvine, California 92627, USA

^c Department of Pharmaceutical Sciences, University of California-Irvine, Irvine, California 92627, USA

Abstract

MhuD is a protein found in mycobacteria that can bind up to two heme molecules per protein monomer and catalyze the degradation of heme to mycobilin in vitro. Here the K_d1 for heme dissociation from heme-bound MhuD was determined to be 7.6 ± 0.8 nM and the K_d2 for heme dissocation from diheme-bound MhuD was determined to be 3.3 ± 1.1 μM. These data strongly suggest that MhuD is a competent heme oxygenase in vivo.

This article is part of the themed collection: Metallomics Recent HOT articles

Metallomics

The affinity of MhuD for heme is consistent with a heme degrading function in vivo†

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