The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
General Acid-Base Catalysis in the Mechanism of a Hepatitis Delta Virus Ribozyme
Abstract
Many protein enzymes use general acid-base catalysis as a way to increase reaction rates. The amino acid histidine is optimized for this function because it has a p K a (where K a is the acid dissociation constant) near physiological pH. The RNA enzyme (ribozyme) from hepatitis delta virus catalyzes self-cleavage of a phosphodiester bond. Reactivity-pH profiles in monovalent or divalent cations, as well as distance to the leaving-group oxygen, implicate cytosine 75 (C75) of the ribozyme as the general acid and ribozyme-bound hydrated metal hydroxide as the general base in the self-cleavage reaction. Moreover, C75 has a p K a perturbed to neutrality, making it “histidine-like.” Anticooperative interaction is observed between protonated C75 and a metal ion, which serves to modulate the p K a of C75. General acid-base catalysis expands the catalytic repertoire of RNA and may provide improved rate acceleration.
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Crystal structure of a hairpin ribozyme–inhibitor complex with implications for catalysis
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Metadata
- Authors
- Nakano, S.-I., Chadalavada, D. M., & Bevilacqua, P. C.
- Venue
- Science
- Published
- 2000-02-25
- Volume
- 287
- Issue
- 5457
- Pages
- 1493-1497
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1974000520
- Cited by
- 385
- References
- 41
- FWCI
- 9.80
- 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.