The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Thiyl Radicals in Ribonucleotide Reductases
Abstract
The ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii catalyzes adenosylcobalamin (AdoCbl)-dependent nucleotide reduction, as well as exchange of the 5′ hydrogens of AdoCbl with solvent. A protein-based thiyl radical is proposed as an intermediate in both of these processes. In the presence of RTPR containing specifically deuterated cysteine residues, the electron paramagnetic resonance (EPR) spectrum of an intermediate in the exchange reaction and the reduction reaction, trapped by rapid freeze quench techniques, exhibits narrowed hyperfine features relative to the corresponding unlabeled RTPR. The spectrum was interpreted to represent a thiyl radical coupled to cob(II)alamin. Another proposed intermediate, 5′-deoxyadenosine, was detected by rapid acid quench techniques. Similarities in mechanism between RTPR and the Escherichia coli ribonucleotide reductase suggest that both enzymes require a thiyl radical for catalysis.
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Cites
Structure of ribonucleotide reductase protein R1
Uhlin, U., & Eklund, H. (1994) · Nature · doi:10.1038/370533a0 · Cited by 573
From RNA to DNA, Why So Many Ribonucleotide Reductases?
Reichard, P. (1993) · Science · doi:10.1126/science.8511586 · Cited by 530
The free radical in pyruvate formate-lyase is located on glycine-734.
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Self-citationKARTHEIN, R., DIETZ, R., NASTAINCZYK, W., & RUF, H. H. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb13792.x · Cited by 284
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PROTEIN RADICAL INVOLVEMENT IN BIOLOGICAL CATALYSIS?
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Self-citationThe state of copper in stellacyanin and laccase from the lacquer tree Rhus vernicifera
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Stubbe, J., Nocera, D. G., Yee, C. S., & Chang, M. C. Y. (2003) · Chemical Reviews · doi:10.1021/cr020421u · Cited by 823
Self-citationStructure and function of the radical enzyme ribonucleotide reductase
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(2025) · doi:10.1038/s41467-025-57735-4 · Cited by 10
Metadata
- Authors
- Licht, S., Gerfen, G. J., & Stubbe, J.
- Venue
- Science
- Published
- 1996-01-26
- Volume
- 271
- Issue
- 5248
- Pages
- 477-481
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2050088367
- Cited by
- 317
- References
- 15
- FWCI
- 17.22
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
