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Article: DNA hydrolysis promoted by di- and multi-nuclear metal complexes

TitleDNA hydrolysis promoted by di- and multi-nuclear metal complexes
Authors
KeywordsArtificial nucleases
Catalytic cooperativity
Di- and multi-nuclear metal complexes
DNA hydrolysis
Phosphate diester bond
Structure-function relationships
Type II restriction endonucleases
Issue Date2004
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ccr
Citation
Coordination Chemistry Reviews, 2004, v. 248 n. 1-2, p. 147-168 How to Cite?
AbstractDNA hydrolysis mediated by di- and multi-nuclear metal complexes is of increasing importance in biotechnology and medicine. Many systems for enzyme-mediated nucleic acid hydrolysis, including type II restriction endonucleases and phosphatases, contain di- and multi-nuclear metal active sites. Recent progress in the design of di- and multi-nuclear metal artificial nucleases has included Fe 3+, Zn 2+, Cu 2+, Co 3+ and Ln 3+/4+-azamacrocyclic, aminocarboxylic and pyridyl- or benzimidazolyl-based organic ligands complexes and their conjugates to biomacromolecules. The focus in this article is on di- and multi-nuclear metal complexes that promote DNA cleavage via hydrolytic rather than oxidative pathway. Our purpose is to highlight the relationships between the structures of di- and multi-nuclear metal complexes and their functions, the cooperativities between metal and ligands and between metal sites in the course of DNA hydrolysis and the problems that are faced toward the development of di- and multi-nuclear metal-based artificial restriction enzymes by applying the principles of coordination chemistry and enzymatic chemistry. In order to be able to conveniently compare kinetic data that have been reported for many di- and multi-nuclear metal complexes, we propose two parameters α and β that are associated with the kinetic studies on DNA hydrolysis. The former α is defined as the ratio of the hydrolytic rate constant mediated by a di- or multi-nuclear metal complex to that by the analogous mononuclear complex under identical or similar conditions, indicating the degree of cooperativity between metal sites. The latter β is recognized as a rate enhancement over unhydrolyzed double-stranded DNA. © 2003 Published by Elsevier B.V.
Persistent Identifierhttp://hdl.handle.net/10722/69907
ISSN
2023 Impact Factor: 20.3
2023 SCImago Journal Rankings: 4.145
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLiu, Cen_HK
dc.contributor.authorWang, Men_HK
dc.contributor.authorZhang, Ten_HK
dc.contributor.authorSun, Hen_HK
dc.date.accessioned2010-09-06T06:17:55Z-
dc.date.available2010-09-06T06:17:55Z-
dc.date.issued2004en_HK
dc.identifier.citationCoordination Chemistry Reviews, 2004, v. 248 n. 1-2, p. 147-168en_HK
dc.identifier.issn0010-8545en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69907-
dc.description.abstractDNA hydrolysis mediated by di- and multi-nuclear metal complexes is of increasing importance in biotechnology and medicine. Many systems for enzyme-mediated nucleic acid hydrolysis, including type II restriction endonucleases and phosphatases, contain di- and multi-nuclear metal active sites. Recent progress in the design of di- and multi-nuclear metal artificial nucleases has included Fe 3+, Zn 2+, Cu 2+, Co 3+ and Ln 3+/4+-azamacrocyclic, aminocarboxylic and pyridyl- or benzimidazolyl-based organic ligands complexes and their conjugates to biomacromolecules. The focus in this article is on di- and multi-nuclear metal complexes that promote DNA cleavage via hydrolytic rather than oxidative pathway. Our purpose is to highlight the relationships between the structures of di- and multi-nuclear metal complexes and their functions, the cooperativities between metal and ligands and between metal sites in the course of DNA hydrolysis and the problems that are faced toward the development of di- and multi-nuclear metal-based artificial restriction enzymes by applying the principles of coordination chemistry and enzymatic chemistry. In order to be able to conveniently compare kinetic data that have been reported for many di- and multi-nuclear metal complexes, we propose two parameters α and β that are associated with the kinetic studies on DNA hydrolysis. The former α is defined as the ratio of the hydrolytic rate constant mediated by a di- or multi-nuclear metal complex to that by the analogous mononuclear complex under identical or similar conditions, indicating the degree of cooperativity between metal sites. The latter β is recognized as a rate enhancement over unhydrolyzed double-stranded DNA. © 2003 Published by Elsevier B.V.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ccren_HK
dc.relation.ispartofCoordination Chemistry Reviewsen_HK
dc.rightsCoordination Chemistry Reviews. Copyright © Elsevier BV.en_HK
dc.subjectArtificial nucleasesen_HK
dc.subjectCatalytic cooperativityen_HK
dc.subjectDi- and multi-nuclear metal complexesen_HK
dc.subjectDNA hydrolysisen_HK
dc.subjectPhosphate diester bonden_HK
dc.subjectStructure-function relationshipsen_HK
dc.subjectType II restriction endonucleasesen_HK
dc.titleDNA hydrolysis promoted by di- and multi-nuclear metal complexesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0010-8545&volume=248&spage=147&epage=168&date=2004&atitle=DNA+hydrolysis+promoted+by+di-+and+multi-nuclear+metal+complexesen_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.cct.2003.11.002en_HK
dc.identifier.scopuseid_2-s2.0-1142267465en_HK
dc.identifier.hkuros94331en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-1142267465&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume248en_HK
dc.identifier.issue1-2en_HK
dc.identifier.spage147en_HK
dc.identifier.epage168en_HK
dc.identifier.isiWOS:000220305000006-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridLiu, C=36068478700en_HK
dc.identifier.scopusauthoridWang, M=7407802742en_HK
dc.identifier.scopusauthoridZhang, T=7404373577en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.issnl0010-8545-

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