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A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/ Acetyl-CoA Synthase
Abstract
A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica (f. Clostridium thermoaceticum ). Our structure at 2.2 angstrom resolution reveals that the cofactor responsible for the assembly of acetyl-CoA contains a [Fe 4 S 4 ] cubane bridged to a copper-nickel binuclear site. The presence of these three metals together in one cluster was unanticipated and suggests a newly discovered role for copper in biology. The different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit.
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The Genetic Basis for Bacterial Mercury Methylation
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Metadata
- Authors
- Doukov, T. I., Iverson, T. M., Seravalli, J., Ragsdale, S. W., & Drennan, C. L.
- Venue
- Science
- Published
- 2002-10-18
- Volume
- 298
- Issue
- 5593
- Pages
- 567-572
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1983644317
- Cited by
- 529
- References
- 4
- FWCI
- 44.64
- Type
- journal article
- Language
- en
- Open access
- closed
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- Doukov, T. I., Iverson, T. M., Seravalli, J., Ragsdale, S. W., & Drennan, C. L. (2002). A Ni-Fe-Cu Center in a Bifunctional Carbon Monoxide Dehydrogenase/ Acetyl-CoA Synthase. Science. https://doi.org/10.1126/science.1075843
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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