ArticleBiochemistry2019
A Single Mutation in the Mycobacterium tuberculosis Heme-Degrading Protein, MhuD, Results in Different Products.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- A periplasmic protein complex mediates arabinofuranosyltransferase activity and intrinsic drug resistance inScience advances · 2026Article
- Differentiating the roles of Mycobacterium tuberculosis substrate binding proteins, FecB and FecB2, in iron uptake.PLoS pathogens · 2023Article
- Second-sphere tuning of analogues for the ferric-hydroperoxoheme form of Mycobacterium tuberculosis MhuD.Journal of inorganic biochemistry · 2023Article
- Ruffling is essential for Staphylococcus aureus IsdG-catalyzed degradation of heme to staphylobilin.Journal of inorganic biochemistry · 2022Article
- Biosynthesis of the Tricyclic Aromatic Type II Polyketide Rishirilide: New Potential Third Ring Oxygenation after Three Cyclization Steps.Molecular biotechnology · 2021Article
- A Dynamic Substrate is Required for MhuD-Catalyzed Degradation of Heme to Mycobilin.Biochemistry · 2021Article
- Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020Review
- Structure of aBiochemistry · 2019Article
- Spectroscopic Evidence for Electronic Control of Heme Hydroxylation by IsdG.Inorganic chemistry · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors.
Funding
Abstract
Mycobacterium tuberculosis heme-degrading protein MhuD degrades heme to mycobilin isomers and iron, while its closest homologues from Staphylococcus aureus, IsdG and IsdI, degrade heme to staphylobilin isomers, formaldehyde, and iron. Superposition of the structures of the heme-bound complexes reveals that the heme molecule in the MhuD active site is rotated ∼90° about the tetrapyrrole plane with respect to IsdG and IsdI active site heme molecules. Therefore, the variation in IsdG/IsdI and MhuD chromophore products may be attributed to the different heme orientations. In MhuD, two arginines, Arg22 and Arg26, stabilize the heme propionates and may account for the heme orientation. Herein, we demonstrate that the MhuD-R26S variant alters the resulting chromophore product from mycobilin to biliverdin IXα (α-BV), whereas the R22S variant does not. Surprisingly, unlike canonical heme oxygenase (HO) that also degrades heme to α-BV, the MhuD-R26S variant produces the C1 product formaldehyde rather than carbon monoxide as observed for HO. The MhuD-R26S variant is an important tool for further probing the mechanism of action of MhuD and for studying the fate of the MhuD product in mycobacterium.
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