The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Unusual Diheme Conformation of the Heme-Degrading Protein from Mycobacterium tuberculosis
Open accessAbstract
Heme degradation plays a pivotal role in the availability of the essential nutrient, iron, in pathogenic bacteria. A previously unannotated protein from Mycobacterium tuberculosis, Rv3592, which shares homology to heme-degrading enzymes, has been identified. Biochemical analyses confirm that Rv3592, which we have termed MhuD (mycobacterial heme utilization, degrader), is able to bind and degrade heme. Interestingly, contrary to previously reported stoichiometry for the Staphylococcus aureus heme degraders, iron-regulated surface determinant (Isd)G and IsdI, MhuD has the ability to bind heme in a 1:2 protein-to-heme ratio, although the MhuD-diheme complex is inactive. Furthermore, the 1.75-A crystal structure of the MhuD-diheme complex reveals two stacked hemes forming extensive contacts with residues in the active site. In particular, the solvent-exposed heme is axially liganded by His75 and is stacked planar upon the solvent-protected heme. The solvent-protected heme is coordinated by a chloride ion, which is, in turn, stabilized by Asn7. Structural comparison between MhuD-diheme and inactive IsdG and IsdI bound to only one highly distorted metalloporphyrin ring reveals that several residues located in alpha-helix 2 and the subsequent loop appear to be responsible for heme stoichiometric differences and suggest open and closed conformations for substrate entry and product exit.
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“This unusual diheme conformation does not affect the heme degrading capabilities of MhuD, however, as the product of MhuD heme degradation has not been determined; it is unclear if the diheme active site degrades heme to staphylobilin.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [56]
In the citing paper
“IsdG-family heme oxygenases have been characterized in S. lugdunensis, Bacillus anthracis, Bradyrhizobium japonicum, Brucella melitensis, and Mycobacterium tuberculosis [46, 50, 56–58].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [56]
In the citing paper
“Each MhuD monomer binds two heme molecules with the porphyrin rings stacked 3.45 Å apart [56].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [56]
In the citing paper
“While IsdG orthologs from each of these bacteria have been shown to bind and degrade heme, differences do exist.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [56]
In the citing paper
“This unusual diheme conformation does not affect the heme degrading capabilities of MhuD, however, as the product of MhuD heme degradation has not been determined; it is unclear if the diheme active site degrades heme to staphylobilin.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [56]
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- Fontan, 2009, Mycobacterium tuberculosis sigma factor E protects against environmental stress, immune responses, Microbe, 4, 119
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Mycobacterium tuberculosis Rv2074 is a coenzyme F420-dependent mycobilin reductase
de Miranda, R., Martinez, J., Cuthbert, B. J., Mendoza, J., Jackson, C. J., & Goulding, C. W. (2026) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2026.113467
Capture of long‐missing heme oxygenases that degrade both heme b and heme c
Hou, J., Dong, W., Yang, H., Liang, Y., & Gao, H. (2026) · mLife · doi:10.1002/mlf2.70118
Metadata
- Authors
- Chim, N., Iniguez, A., Nguyen, T. Q., & Goulding, C. W.
- Affiliations
- University of California, Irvine (US)
- Corresponding author
- Goulding, Celia W.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2010-01
- Volume
- 395
- Issue
- 3
- Pages
- 595-608
- ISSN
- 0022-2836 (ISSN-L)
- PMC
- PMC2859679
- OpenAlex
- W2048048044
- Cited by
- 102
- References
- 54
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 2 · 2023: 4 · 2022: 5 · 2021: 9 · 2020: 2 · 2019: 7 · 2018: 7 · 2017: 5 · 2016: 9 · 2015: 6 · 2014: 7 · 2013: 9 · 2012: 6
- FWCI
- 3.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Colorado State University
- National Institutes of Health (n01ai075320-008)
- U.S. Public Health Service (P01A1068135)
- National Institute of Allergy and Infectious Diseases (AI081161, P01AI068135, R01AI081161, N01AI75320)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- Mycobacterium tuberculosis, heme degradation, heme utilization, iron acquisition, crystal structure, chloride coordination, Staphylococcus aureus, metalloporphyrins, protein conformation
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, Binding Sites, Heme, Models, Molecular, Molecular Sequence Data, Mycobacterium tuberculosis, Oxygenases, Protein Binding, Protein Conformation, Recombinant Proteins, Sequence Homology, Amino Acid, Crystallography, X-Ray, Protein Structure, Quaternary, Macromolecular Substances, Protein Multimerization
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