The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
The Mismetallation of Enzymes during Oxidative Stress
Open accessAbstract
Mononuclear iron enzymes can tightly bind non-activating metals. How do cells avoid mismetallation? The model bacterium Escherichia coli may control its metal pools so that thermodynamics favor the correct metallation of each enzyme. This system is disrupted, however, by superoxide and hydrogen peroxide. These species oxidize ferrous iron and thereby displace it from many iron-dependent mononuclear enzymes. Ultimately, zinc binds in its place, confers little activity, and imposes metabolic bottlenecks. Data suggest that E. coli compensates by using thiols to extract the zinc and by importing manganese to replace the catalytic iron atom. Manganese resists oxidants and provides substantial activity.
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Metadata
- Authors
- Imlay, J. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2014-10
- Volume
- 289
- Issue
- 41
- Pages
- 28121-28128
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2077883858
- Cited by
- 270
- References
- 10
- FWCI
- 8.47
- Type
- journal article
- Language
- en
- Open access
- hybrid
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