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Updated: Feb 5, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
The affinity of MhuD for heme is consistent with a heme degrading function in vivo
Biswash Thakuri1, Amanda B Graves, Alex Chao
1Department of Chemistry, University of Vermont, Burlington, Vermont 05405, USA. matthew.liptak@uvm.edu.
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 Kd1 for heme dissociation from heme-bound MhuD was determined to be 7.6 ± 0.8 nM and the Kd2 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.
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