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Related Experiment Video

Updated: Jul 16, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Heme Oxygenase-Like Metalloenzymes.

Sarah R Pope¹, Molly J McBride², Mrutyunjay A Nair²

¹Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania, USA;

Annual Review of Biochemistry

|March 27, 2025

Summary

Heme oxygenase (HO)-like enzymes are a diverse bacterial protein group. They utilize unique diiron clusters for novel oxygenase and oxidase reactions, expanding enzyme catalysis possibilities.

Keywords:

N-oxygenase desaturase diiron iron oxygen peroxo

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Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

Published on: October 3, 2018

Area of Science:

Biochemistry and enzymology
Protein superfamily characterization
Bacterial metabolism

Background:

Heme oxygenase (HO)-like metalloenzymes represent an emerging protein superfamily.
These enzymes are primarily found in bacterial biosynthetic pathways and share conserved features with the heme catabolic enzyme, HO.
They possess a flexible protein scaffold and metal-binding residues, accommodating various cofactors like diiron, manganese-iron, and mononuclear iron.

Purpose of the Study:

To explore the diverse reaction outcomes and mechanisms of HO-like metalloenzymes.
To understand the role of the HO-like scaffold in cofactor assembly, disassembly, and reactivity.
To investigate the potential of these enzymes in catalyzing unprecedented fragmentation and rearrangement reactions.

Main Methods:

Analysis of conserved protein scaffolds and metal-binding residues.
Characterization of cofactor assembly, including diiron, manganese-iron, and mononuclear iron clusters.
Investigation of the reaction mechanism in canonical HO-like diiron oxygenases/oxidases (HDOs), focusing on the peroxo-Fe2(III/III) intermediate.

Main Results:

HO-like metalloenzymes exhibit diverse reaction capabilities and mechanisms.
The canonical HDOs utilize a diiron cluster that reacts with O2 to form a peroxo-Fe2(III/III) intermediate.
The HO-like scaffold provides unique metal-binding properties and reactivity, enabling dynamic cofactor management.

Conclusions:

The HO-like scaffold confers distinctive metal-binding properties and unusual reactivity to its metallocofactor.
These enzymes are capable of mediating fragmentation and rearrangement reactions, unprecedented in other dinuclear iron enzymes.
Significant unexplored sequence space within the HO-like metalloenzyme superfamily offers potential for discovering novel mechanisms and reactivities.