The roles of Asn7 and Trp67 in tuning the ferryl haem form of Staphylococcus aureus IsdG
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Abstract
The ferryl haem form of W67F IsdG contains an organic radical. This variant yields a biliverdin product, distinct from the staphylobilin product of wild-type enzyme.
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Cites
Iron in infection and immunity
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Passage of Heme-Iron Across the Envelope of <i>Staphylococcus aureus</i>
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Iron-Source Preference of <i>Staphylococcus aureus</i> Infections
Skaar, E. P., Humayun, M., Bae, T., DeBord, K. L., & Schneewind, O. (2004) · Science · doi:10.1126/science.1099930 · Cited by 440 · see citing works
Heme Synthesis and Acquisition in Bacterial Pathogens
Choby, J. E., & Skaar, E. P. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.018 · Cited by 343 · see citing works
IsdG and IsdI, Heme-degrading Enzymes in the Cytoplasm of Staphylococcus aureus
Skaar, E. P., Gaspar, A. H., & Schneewind, O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307952200 · Cited by 282 · see citing works
Structural biology of heme binding in the Staphylococcus aureus Isd system
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Flagged first, then by citations
- Authors
- Grover, A., Nabi, A., Conger, M. A., & Liptak, M. D.
- Affiliations
- University of Vermont (US)
- Corresponding author
- Liptak, M. D.
- Venue
- Dalton Transactions
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2026
- Volume
- 55
- Issue
- 9
- Pages
- 3795-3805
- ISSN
- 1477-9226 (ISSN-L)
- 1477-9234
- PMC
- PMC12933262
- OpenAlex
- W7128700347
- Cited by
- 2
- References
- 10
- Citations by year
- 2026: 2
- FWCI
- 2.59
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- Dalton Transactions (publishedVersion)
- ChemRxiv (acceptedVersion, cc-by-nc-nd)
- ChemRxiv (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R35-GM139516)
- National Science Foundation (CHE-1919417)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Physical Sciences › Materials Science › Materials Chemistry › Porphyrin and Phthalocyanine Chemistry
- Keywords
- Staphylococcus aureus, compound I, compound E, biliverdin, product selectivity, heme oxygenase, electron spin resonance
- MeSH terms
- Bacterial Proteins, Electron Spin Resonance Spectroscopy, Heme, Oxygenases, Staphylococcus aureus, Tryptophan
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