The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Heme Oxygenase: Evolution, Structure, and Mechanism
Abstract
Heme oxygenase has evolved to carry out the oxidative cleavage of heme, a reaction essential in physiological processes as diverse as iron reutilization and cellular signaling in mammals, synthesis of essential light-harvesting pigments in cyanobacteria and higher plants, and the acquisition of iron by bacterial pathogens. In all of these processes, heme oxygenase has evolved a similar structural and mechanistic scaffold to function within seemingly diverse physiological pathways. The heme oxygenase reaction is catalytically distinct from that of other hemoproteins such as the cytochromes P450, peroxidases, and catalases, but shares a hemoprotein scaffold that has evolved to generate a distinct activated oxygen species. In the following review we discuss the evolution of the structural and functional properties of heme oxygenase in light of the recent crystal structures of the mammalian and bacterial enzymes.
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Cites
Schmitt, M. P. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.3.838-845.1997 · Cited by 234 · cited 1×
“…identification and characterization of a HO (HmuO) from the heme-utilizing bacterial pathogen Corynebacterium diphtheriae , with 33% sequence identity and 70% homology to the human HO-1, again showed the highest identity in residues 122–145, corresponding to residues 125–150 in HO-1 (37, 54) (Fig.”
Zhu, W., Wilks, A., & Stojiljkovic, I. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.23.6783-6790.2000 · Cited by 186
Lee-Robichaud, P., Wright, J. N., Akhtar, M. E., & Akhtar, M. (1995) · Biochemical Journal · doi:10.1042/bj3080901 · Cited by 145
Use of Heme Compounds as Iron Sources by Pathogenic Neisseriae Requires the Product of the hemO Gene
Zhu, W., Hunt, D. J., Richardson, A. R., & Stojiljkovic, I. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.2.439-447.2000 · Cited by 108
Cited by
Nutritional immunity: transition metals at the pathogen–host interface
Hood, M. I., & Skaar, E. P. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2836 · Cited by 1,535
Mechanisms of Cell Protection by Heme Oxygenase-1
Gozzelino, R., Jeney, V., & Soares, M. P. (2010) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.010909.105600 · Cited by 1,241
The Battle for Iron between Bacterial Pathogens and Their Vertebrate Hosts
Skaar, E. P. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000949 · Cited by 796
The Aspergillus nidulans Phytochrome FphA Represses Sexual Development in Red Light
Blumenstein, A., Vienken, K., Tasler, R., Purschwitz, J., Veith, D., Frankenberg-Dinkel, N., & Fischer, R. (2005) · Current Biology · doi:10.1016/j.cub.2005.08.061 · Cited by 357
Recent developments in understanding the iron acquisition strategies of gram positive pathogens
Sheldon, J. R., & Heinrichs, D. E. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv009 · Cited by 272
Metadata
- Authors
- Wilks, A.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2002-08
- Volume
- 4
- Issue
- 4
- Pages
- 603-614
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2141514162
- Cited by
- 204
- References
- 4
- FWCI
- 1.84
- Type
- journal article
- Language
- en
- Open access
- closed
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