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Escherichia coli Contains a Protein That Is Homologous in Function and N-terminal Sequence to the Protein Encoded by the nifS Gene of Azotobacter vinelandii and That Can Participate in the Synthesis of the Fe-S Cluster of Dihydroxy-acid Dehydratase
Open accessAbstract
In this paper, I report the purification of a protein from Escherichia coli that is very similar in sequence, molecular weight, and the reactions it can catalyze to the protein encoded by the Azotobacter vinelandii nifS gene. This E. coli protein contains pyridoxal phosphate as a cofactor and catalyzes the removal of sulfur from cysteine to form alanine and S0. When dithiothreitol is present along with cysteine, the S0 formed is reduced to S2-. This protein has a reactive sulfhydryl group that is essential for activity. As isolated, this sulfhydryl group appears to be in a disulfide linkage with the sulfhydryl group from the phosphopantetheine moiety of the acyl carrier protein. The purified E. coli protein can mobilize the sulfur from cysteine and contribute it to the formation of a [4Fe-4S] cluster on the apoprotein of E. coli dihydroxy-acid dehydratase. A mechanism is proposed for the early stages of the synthesis of Fe-S clusters using this protein and sulfur in the S0 oxidation state.
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Citations
Cites
Sulphane sulphur in biological systems: a possible regulatory role
Toohey, J. I. (1989) · Biochemical Journal · doi:10.1042/bj2640625 · Cited by 246
Cited by
Chemical Biology of H2S Signaling through Persulfidation
Filipovic, M. R., Zivanovic, J., Alvarez, B., & Banerjee, R. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00205 · Cited by 1,046
Storz, G., & Imlayt, J. A. (1999) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(99)80033-2 · Cited by 1,021
Superoxide accelerates DNA damage by elevating free-iron levels
Keyer, K., & Imlay, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13635 · Cited by 841
Assembly of Iron-Sulfur Clusters
Zheng, L., Cash, V. L., Flint, D. H., & Dean, D. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13264 · Cited by 649
Self-citationA suf operon requirement for Fe–S cluster assembly during iron starvation in Escherichia coli
Outten, F. W., Djaman, O., & Storz, G. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04025.x · Cited by 448
Metadata
- Authors
- Flint, D. H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-07
- Volume
- 271
- Issue
- 27
- Pages
- 16068-16074
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1532421291
- Cited by
- 190
- References
- 1
- FWCI
- 15.15
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Escherichia coli Contains a Protein That Is Homologous in Function and N-terminal Sequence to the Protein Encoded by the nifS Gene of Azotobacter vinelandii and That Can Participate in the Synthesis of the Fe-S Cluster of Dihydroxy-acid Dehydratase. https://app.cochat.ai/papers/10.1016/s0021-9258(18)48580-8
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- Flint, D. H. (1996). Escherichia coli Contains a Protein That Is Homologous in Function and N-terminal Sequence to the Protein Encoded by the nifS Gene of Azotobacter vinelandii and That Can Participate in the Synthesis of the Fe-S Cluster of Dihydroxy-acid Dehydratase. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)48580-8
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