Show simple item record

dc.contributorWichita State University. Department of Chemistryen_US
dc.contributor.authorWimalasena, Kandategeen_US
dc.contributor.authorDharmasena, Silpadipathialageen_US
dc.contributor.authorWimalasena, D. Shyamalien_US
dc.date.accessioned2012-02-06T17:15:55Z
dc.date.available2012-02-06T17:15:55Z
dc.date.issued1994-04-15en_US
dc.identifier8166679en_US
dc.identifier0372516en_US
dc.identifierS0006-291X(84)71422-7en_US
dc.identifierR29-GM45026en_US
dc.identifier.citationBiochemical and biophysical research communications. 1994 Apr 15; 200(1): 113-9.en_US
dc.identifier.issn0006-291Xen_US
dc.identifier.urihttp://dx.doi.org/10.1006/bbrc.1994.1422en_US
dc.identifier.urihttp://hdl.handle.net/10057/4279
dc.descriptionClick on the DOI link below to access the article (may not be free).en_US
dc.description.abstractA series of ascorbate derivatives has been used to examine the specificity and the chemistry of the reduction site of dopamine beta-monooxygenase (D beta M). Replacement of the 6-OH group of ascorbic acid with either bromine or hydrogen does not alter the enzyme reduction efficiency significantly. Unexpectedly, the 6-OH modified ascorbate derivatives, 6-S-phenyl-6-thio-L-ascorbic acid and 6-O-phenyl-L-ascorbic acid were found to have much higher affinity for the enzyme than the most effective known electron donor, ascorbic acid (AscH-). The affinity of 2-amino-6-S-phenyl-L-ascorbic acid was found to be similar to that of 2-amino-L-ascorbic acid. 6-Amino-6-deoxy-L-ascorbic acid is neither a substrate nor an inhibitor for the enzyme. Although glucoascorbic acid is an excellent substrate for the enzyme, imino glucoascorbic acid was found to be an extremely potent competitive inhibitor for the enzyme. The stereoelectronic properties and alternate binding modes of these molecules have been considered in explaining the observations.en_US
dc.description.sponsorshipNIGMS NIH HHSen_US
dc.format.extent113-9en_US
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.relation.ispartofseriesBiochemical and biophysical research communicationsen_US
dc.relation.ispartofseriesBiochem. Biophys. Res. Commun.en_US
dc.sourceNLMen_US
dc.subjectComparative Studyen_US
dc.subjectResearch Support, U.S. Gov't, P.H.S.en_US
dc.subject.lcshAscorbic Acid/chemical synthesisen_US
dc.subject.lcshAscorbic Acid/metabolismen_US
dc.subject.lcshAscorbic Acid/pharmacologyen_US
dc.subject.lcshDopamine beta-Hydroxylase/metabolismen_US
dc.subject.meshAdrenal Medulla/enzymologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAscorbic Acid/analogs & derivativesen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshBinding, Competitiveen_US
dc.subject.meshCattleen_US
dc.subject.meshChromaffin Granules/enzymologyen_US
dc.subject.meshDopamine beta-Hydroxylase/antagonists & inhibitorsen_US
dc.subject.meshIndicators and Reagentsen_US
dc.subject.meshKineticsen_US
dc.subject.meshMagnetic Resonance Spectroscopyen_US
dc.subject.meshSpectrophotometryen_US
dc.titleAscorbate based novel high affinity alternate reductants and competitive inhibitors of dopamine beta-monooxygenaseen_US
dc.typeArticleen_US
dc.coverage.spacialUnited Statesen_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 1994, Elsevieren_US


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record