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Article: Synthesis, structure, and activity of supramolecular mimics for the active site and Arg141 residue of copper, zinc-superoxide dismutase

TitleSynthesis, structure, and activity of supramolecular mimics for the active site and Arg141 residue of copper, zinc-superoxide dismutase
Authors
Issue Date2007
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/ic
Citation
Inorganic Chemistry, 2007, v. 46 n. 3, p. 734-739 How to Cite?
AbstractTwo supramolecular complexes, [Cu(L)(H 2O) 2(β-CD) ](ClO 4) 2·10.5H 2O·CH 3OH (1) and [Cu(L)(H 2O) 2(β-GCD)](HClO 4)-(ClO 4) 2·10H 2O (2) (L = 4-(4′-tert-butyl-benzyl)diethylenetriamine, β-CD = β-cyclodextrin, and β-GCD = mono-6-deoxy-6-guanidinocycloheptaamylose cation), have been synthesized. The structure of 1 has been characterized by X-ray crystallography. The 4-tert-butyl-benzyl of [Cu(L)(H 2O) 2] 2+ moiety in 1 as a guest inserts into the hydrophobic cavity of the β-CD as a host along the primary hydroxyl side. On the basis of the structure data of 1, complex 2 was modeled, which showed that the distance between the Cu and C atom of the guanidinium is 5.2 Å, comparable to the corresponding distance in bovine erythrocyte Cu, Zn-SOD (5.9 Å) (SOD = superoxide dismutase). Apparent inclusion stability constants of the host and the guest were measured to be 0.66 (±0.01) × 10 4 and 1.15 (±0.03) × 10 4 M -1 for 1 and 2 respectively. The electronic absorption bands and electronic reflection bands of each complex are almost the same, indicating an identical structure of the complex in aqueous solution and in solid state. The two complexes showed quasi-reversible one-electron Cu(II)/Cu(I) redox waves with redox potentials of -0.345 and -0.338 V for 1 and 2, respectively. Their SOD-like activities (IC 50) were measured to be 0.30 ± 0.01 and 0.17 ± 0.01 μM by xanthine/xanthine oxidase-NBT assay. The enhanced SOD activity of 2 by ∼40% compared with 1 suggests that the guanidyl cation in the host of the supramolecular system of 2 can effectively mimic the side chain of Arg141 in the enzyme, which is known to be essential for high SOD activity possibly through steering of the superoxide substrate to and from the active copper ion. © 2007 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/168095
ISSN
2015 Impact Factor: 4.82
2015 SCImago Journal Rankings: 1.873
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhou, YHen_US
dc.contributor.authorFu, Hen_US
dc.contributor.authorZhao, WXen_US
dc.contributor.authorChen, WLen_US
dc.contributor.authorSu, CYen_US
dc.contributor.authorSun, Hen_US
dc.contributor.authorJi, LNen_US
dc.contributor.authorMao, ZWen_US
dc.date.accessioned2012-10-08T03:15:01Z-
dc.date.available2012-10-08T03:15:01Z-
dc.date.issued2007en_US
dc.identifier.citationInorganic Chemistry, 2007, v. 46 n. 3, p. 734-739en_US
dc.identifier.issn0020-1669en_US
dc.identifier.urihttp://hdl.handle.net/10722/168095-
dc.description.abstractTwo supramolecular complexes, [Cu(L)(H 2O) 2(β-CD) ](ClO 4) 2·10.5H 2O·CH 3OH (1) and [Cu(L)(H 2O) 2(β-GCD)](HClO 4)-(ClO 4) 2·10H 2O (2) (L = 4-(4′-tert-butyl-benzyl)diethylenetriamine, β-CD = β-cyclodextrin, and β-GCD = mono-6-deoxy-6-guanidinocycloheptaamylose cation), have been synthesized. The structure of 1 has been characterized by X-ray crystallography. The 4-tert-butyl-benzyl of [Cu(L)(H 2O) 2] 2+ moiety in 1 as a guest inserts into the hydrophobic cavity of the β-CD as a host along the primary hydroxyl side. On the basis of the structure data of 1, complex 2 was modeled, which showed that the distance between the Cu and C atom of the guanidinium is 5.2 Å, comparable to the corresponding distance in bovine erythrocyte Cu, Zn-SOD (5.9 Å) (SOD = superoxide dismutase). Apparent inclusion stability constants of the host and the guest were measured to be 0.66 (±0.01) × 10 4 and 1.15 (±0.03) × 10 4 M -1 for 1 and 2 respectively. The electronic absorption bands and electronic reflection bands of each complex are almost the same, indicating an identical structure of the complex in aqueous solution and in solid state. The two complexes showed quasi-reversible one-electron Cu(II)/Cu(I) redox waves with redox potentials of -0.345 and -0.338 V for 1 and 2, respectively. Their SOD-like activities (IC 50) were measured to be 0.30 ± 0.01 and 0.17 ± 0.01 μM by xanthine/xanthine oxidase-NBT assay. The enhanced SOD activity of 2 by ∼40% compared with 1 suggests that the guanidyl cation in the host of the supramolecular system of 2 can effectively mimic the side chain of Arg141 in the enzyme, which is known to be essential for high SOD activity possibly through steering of the superoxide substrate to and from the active copper ion. © 2007 American Chemical Society.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/icen_US
dc.relation.ispartofInorganic Chemistryen_US
dc.subject.meshArginineen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshKineticsen_US
dc.subject.meshMolecular Mimicryen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshOxidation-Reductionen_US
dc.subject.meshPeptide Fragments - Chemical Synthesis - Chemistry - Metabolismen_US
dc.subject.meshSuperoxide Dismutase - Chemistryen_US
dc.subject.meshXanthine - Metabolismen_US
dc.subject.meshBeta-Cyclodextrinsen_US
dc.titleSynthesis, structure, and activity of supramolecular mimics for the active site and Arg141 residue of copper, zinc-superoxide dismutaseen_US
dc.typeArticleen_US
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_US
dc.identifier.authoritySun, H=rp00777en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/ic061541den_US
dc.identifier.pmid17257014-
dc.identifier.scopuseid_2-s2.0-33847158296en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33847158296&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume46en_US
dc.identifier.issue3en_US
dc.identifier.spage734en_US
dc.identifier.epage739en_US
dc.identifier.isiWOS:000243789400017-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridZhou, YH=13104031900en_US
dc.identifier.scopusauthoridFu, H=55231387400en_US
dc.identifier.scopusauthoridZhao, WX=15924710900en_US
dc.identifier.scopusauthoridChen, WL=36044051200en_US
dc.identifier.scopusauthoridSu, CY=7402819718en_US
dc.identifier.scopusauthoridSun, H=7404827446en_US
dc.identifier.scopusauthoridJi, LN=7201376856en_US
dc.identifier.scopusauthoridMao, ZW=7202633935en_US

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