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Bacterial Heme Oxygenases
Abstract
The importance of heme oxygenases in heme catabolism, iron utilization, and cellular signaling has been recognized for many years and is a well studied process in eukaryotes. Through the accessibility of an increasing number of bacterial genomes, it has become evident that heme oxygenases are also widespread in prokaryotes. In these organisms, the heme oxygenase reaction serves a similar function as in eukaryotes. A major role of bacterial heme oxygenases has been attributed to acquisition of iron in prokaryotic pathogens, but other functions, such as involvement in phytobilin biosynthesis, have been described. This review summarizes the current state of the art on bacterial heme oxygenase research. The various biological roles of this enzyme in prokaryotes and their biochemical properties will be discussed.
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“Other bacteria predicted to encode an HO family heme monooxygenase include Deinococcus radiodurans , Agrobacterium tumefaciens , and cyanobacteria, including Anabaena sp. PCC7120, Thermosynechococcus elongatus , Prochlorococcus marinus , and Nostoc punctiforme (30).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [30]
In the citing paper
“In cyanobacteria, algae, and plants, biliverdin is a precursor for light-harvesting phytobilin pigments (30).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [30]
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“EME OXYGENASES (HOs) (E.C. 1.14.99.3), first identified in eukaryotes, have key functions in the catabolism of heme and in the biosynthesis of phytobilins, in addition to their involvement in iron metabolism, oxidative stress, and pathogen responses (1, 11, 37, 39, 53 .”
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Cited by
Sorted by citations
Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens
Anzaldi, L. L., & Skaar, E. P. (2010) · Infection and Immunity · doi:10.1128/iai.00613-10 · Cited by 295
Heme oxygenase-1: from biology to therapeutic potential
Soares, M. P., & Bach, F. H. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.12.004 · Cited by 257
Heme uptake in bacterial pathogens
Contreras, H., Chim, N., Credali, A., & Goulding, C. W. (2014) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2013.12.014 · Cited by 146
Bacillus anthracis IsdG, a Heme-Degrading Monooxygenase
Skaar, E. P., Gaspar, A. H., & Schneewind, O. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.3.1071-1080.2006 · Cited by 123
Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis
Chim, N., Iniguez, A., Nguyen, T. Q., & Goulding, C. W. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.11.025 · Cited by 102
Metadata
- Authors
- Frankenberg-Dinkel, N.
- Affiliations
- Institute for Microbiology, Technical University Braunschweig, Braunschweig, Germany.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2004-10
- Volume
- 6
- Issue
- 5
- Pages
- 825-834
- ISSN
- 1523-0864
- 1557-7716
- Cited by
- 63
- References
- 5
- Language
- en
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