DC Field | Value | Language |
---|---|---|
dc.contributor.author | Park, Kiyoung | ko |
dc.contributor.author | Mera, Paola E. | ko |
dc.contributor.author | Escalante-Semerena, Jorge C. | ko |
dc.contributor.author | Brunold, Thomas C. | ko |
dc.date.accessioned | 2015-11-20T10:27:53Z | - |
dc.date.available | 2015-11-20T10:27:53Z | - |
dc.date.created | 2014-08-05 | - |
dc.date.created | 2014-08-05 | - |
dc.date.issued | 2008-08 | - |
dc.identifier.citation | BIOCHEMISTRY, v.47, no.34, pp.9007 - 9015 | - |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.uri | http://hdl.handle.net/10203/201425 | - |
dc.description.abstract | The PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reitteri (LrPduO) catalyzes the formation of the essential Co-C bond of adenosylcobalamin (coenzyme B(12)) by transferring the adenosyl group from cosubstrate ATP to a transient Co(1+) corrinoid species generated in the enzyme active site. While PduO-type enzymes have previously been believed to be capable of adenosylating only Collcobalamin (Co(1+)Cbi), our kinetic data obtained in this study provide in vitro evidence that LrPduO can in fact also utilize the incomplete corrinoid Co(1+) cobinamide (Co(1+)Cbi) as an alternative substrate. To explore the mechanism by which LrPduO overcomes the thermodynamically challenging reduction of its Co(2+) Corrinoid substrates, we have examined how the enzyme active site alters the geometric and electronic properties of Co(2+)Cbl and Co(2+)Cbi(+) by using electronic absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopic techniques. Our data reveal that upon binding to LrPduO that was preincubated with ATP, both Co(2+) Corrinoids undergo a partial (similar to 40-50%) conversion to distinct paramagnetic Co(2+) species. The spectroscopic signatures of these species are consistent with essentially four-coordinate, square-planar Co(2+) complexes, based on a comparison with the results obtained in outprevious studies of related enzymes. Consequently, it appears that the general strategy employed by adenosyltransferases for effecting Co(2+) -> Co(1+) reduction involves the formation of an "activated" Co(2+)corrinoid intermediate that lacks any significant axial bonding interactions, to stabilize the redox-active, Co 3d(Z)(2)-based molecular orbital. | - |
dc.language | English | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | METHYLMALONYL-COA MUTASE | - |
dc.subject | METHIONINE SYNTHASE REDUCTASE | - |
dc.subject | CARBON BOND HOMOLYSIS | - |
dc.subject | ATP-COB(I)ALAMIN ADENOSYLTRANSFERASE | - |
dc.subject | SALMONELLA-TYPHIMURIUM | - |
dc.subject | ADENOSYLCOBALAMIN BIOSYNTHESIS | - |
dc.subject | COMPLEMENTATION GROUP | - |
dc.subject | ELECTRONIC-PROPERTIES | - |
dc.subject | ENZYMATIC CONVERSION | - |
dc.subject | CIRCULAR-DICHROISM | - |
dc.title | Kinetic and spectroscopic studies of the ATP: Corrinoid adenosyltransferase PduO from Lactobacillus reuteri: Substrate specificity and insights into the mechanism of Co(II)corrinoid reduction | - |
dc.type | Article | - |
dc.identifier.wosid | 000258579700021 | - |
dc.identifier.scopusid | 2-s2.0-50149093644 | - |
dc.type.rims | ART | - |
dc.citation.volume | 47 | - |
dc.citation.issue | 34 | - |
dc.citation.beginningpage | 9007 | - |
dc.citation.endingpage | 9015 | - |
dc.citation.publicationname | BIOCHEMISTRY | - |
dc.identifier.doi | 10.1021/bi800419e | - |
dc.contributor.localauthor | Park, Kiyoung | - |
dc.contributor.nonIdAuthor | Mera, Paola E. | - |
dc.contributor.nonIdAuthor | Escalante-Semerena, Jorge C. | - |
dc.contributor.nonIdAuthor | Brunold, Thomas C. | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | METHYLMALONYL-COA MUTASE | - |
dc.subject.keywordPlus | METHIONINE SYNTHASE REDUCTASE | - |
dc.subject.keywordPlus | CARBON BOND HOMOLYSIS | - |
dc.subject.keywordPlus | ATP-COB(I)ALAMIN ADENOSYLTRANSFERASE | - |
dc.subject.keywordPlus | SALMONELLA-TYPHIMURIUM | - |
dc.subject.keywordPlus | ADENOSYLCOBALAMIN BIOSYNTHESIS | - |
dc.subject.keywordPlus | COMPLEMENTATION GROUP | - |
dc.subject.keywordPlus | ELECTRONIC-PROPERTIES | - |
dc.subject.keywordPlus | ENZYMATIC CONVERSION | - |
dc.subject.keywordPlus | CIRCULAR-DICHROISM | - |
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