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Cited by 385

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

Nakano, Shu-ichi, Chadalavada, Durga M., Bevilacqua, Philip C.·2000·Science

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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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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CoChat. (2026). Citation check: General Acid-Base Catalysis in the Mechanism of a Hepatitis Delta Virus Ribozyme. https://app.cochat.ai/papers/10.1126/science.287.5457.1493
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Nakano, S.-I., Chadalavada, D. M., & Bevilacqua, P. C. (2000). General Acid-Base Catalysis in the Mechanism of a Hepatitis Delta Virus Ribozyme. Science. https://doi.org/10.1126/science.287.5457.1493

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