The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Mechanism for the Desulfurization of L-Cysteine Catalyzed by the nifS Gene Product
Abstract
The nifS gene product (NIFS) is a pyridoxal phosphate binding enzyme that catalyzes the desulfurization of L-cysteine to yield L-alanine and sulfur. In Azotobacter vinelandii this activity is required for the full activation of the nitrogenase component proteins. Because the nitrogenase component proteins, Fe protein and MoFe protein, both contain metalloclusters which are required for their respective activities, it is suggested that NIFS participates in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for Fe-S core formation [Zheng, L., White, R. H., Cash, V. L. Jack, R. F., & Dean, D. R. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 2754-2758]. In the present study the mechanism for the desulfurization of L-cysteine catalyzed by NIFS was determined in the following ways. First, the substrate analogs, L-allylglycine and vinylglycine, were shown to irreversibly inactivate NIFS by formation of a gamma-methylcystathionyl or cystathionyl residue, respectively, through nucleophilic attack by an active site cysteinyl residue on the corresponding analog-pyridoxal phosphate adduct. Second, this reactive cysteinyl residue, which is required for L-cysteine desulfurization activity, was identified as Cys325 by the specific alkylation of that residue and by site-directed mutagenesis experiments. Third, the formation of an enzyme-bound cysteinyl persulfide was identified as an intermediate in the NIFS-catalyzed reaction. Fourth, evidence was obtained for an enamine intermediate in the formation of L-alanine.(ABSTRACT TRUNCATED AT 250 WORDS)
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Citations
Cites
Structural Models for the Metal Centers in the Nitrogenase Molybdenum-Iron Protein
Kim, J., & Rees, D. C. (1992) · Science · doi:10.1126/science.1529354 · Cited by 837
Crystallographic Structure of the Nitrogenase Iron Protein from Azotobacter vinelandii
Georgiadis, M. M., Komiya, H., Chakrabarti, P., Woo, D., Kornuc, J. J., & Rees, D. C. (1992) · Science · doi:10.1126/science.1529353 · Cited by 693
Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis.
Zheng, L., White, R. H., Cash, V. L., Jack, R. F., & Dean, D. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2754 · Cited by 595
Self-citationBIOCHEMISTRY OF SULFUR-CONTAINING AMINO ACIDS
Cooper, A. J. L. (1983) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.52.070183.001155 · Cited by 409
The iron-molybdenum cofactor of nitrogenase
Burgess, B. K. (1990) · Chemical Reviews · doi:10.1021/cr00106a002 · Cited by 351
Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii
Jacobson, M. R., Cash, V. L., Weiss, M. C., Laird, N. F., Newton, W. E., & Dean, D. R. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00261156 · Cited by 329
Self-citationEsaki, N., Nakamura, T., Tanaka, H., & Soda, K. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34734-3 · Cited by 237
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Beynon, J., Ally, A. H., Cannon, M. C., Cannon, F. C., Jacobson, M. R., Cash, V. L., & Dean, D. R. (1987) · Journal of Bacteriology · doi:10.1128/jb.169.9.4024-4029.1987 · Cited by 57
Self-citationSPL1-1, a Saccharomyces cerevisiae mutation affecting tRNA splicing
Kolman, C. J., & Söll, D. G. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.5.1433-1442.1993 · Cited by 50
The origin of the nitrogen atom in the thiazole ring of thiamine in Escherichia coli
White, R. H., & Rudolph, F. B. (1978) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(78)90029-6 · Cited by 42
Self-citationSynthesis and some properties of 1‐alkenyl alkyl disulfides and di(1‐alkenyl) disulfides
Wijers, H. E., Boelens, H., GEN, A. V. D., & Brandsma, L. (1969) · Recueil des Travaux Chimiques des Pays-Bas · doi:10.1002/recl.19690880503 · Cited by 41
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Cited by
Structure, function, and formation of biological iron-sulfur clusters
Johnson, D. C., Dean, D. R., Smith, A. D., & Johnson, M. K. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133518 · Cited by 1,438
Structural basis of biological nitrogen fixation
Rees, D. C., Akif Tezcan, F., Haynes, C. A., Walton, M. Y., Andrade, S., Einsle, O., & Howard, J. B. (2005) · Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences · doi:10.1098/rsta.2004.1539 · Cited by 1,120
Structural Basis of Biological Nitrogen Fixation
Howard, J. B., & Rees, D. C. (1996) · Chemical Reviews · doi:10.1021/cr9500545 · Cited by 1,044
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-citationMitochondrial remnant organelles of Giardia function in iron-sulphur protein maturation
Tovar, J., León-Avila, G., Sánchez, L. B., Sutak, R., Tachezy, J., van der Giezen, M., Hernández, M., Müller, M., & Lucocq, J. M. (2003) · Nature · doi:10.1038/nature01945 · Cited by 608
Metadata
- Authors
- Zheng, L., White, R. H., Cash, V. L., & Dean, D. R.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1994-04-19
- Volume
- 33
- Issue
- 15
- Pages
- 4714-4720
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1985844569
- Cited by
- 395
- References
- 13
- FWCI
- 8.17
- Type
- journal article
- Language
- en
- Open access
- closed
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