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Studies on flavin binding in flavodoxins

dc.contributor.authorMayhew, Stephen G.en_US
dc.date.accessioned2006-04-17T16:26:47Z
dc.date.available2006-04-17T16:26:47Z
dc.date.issued1971-05-12en_US
dc.identifier.citationMayhew, Stephen G. (1971/05/12)."Studies on flavin binding in flavodoxins." Biochimica et Biophysica Acta (BBA) - Enzymology 235(2): 289-302. <http://hdl.handle.net/2027.42/33652>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B73GH-47GGN9W-3/2/e86482e84311bf8a41cdc198b8e46f09en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/33652
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5317635&dopt=citationen_US
dc.description.abstract1. 1. Stable apoproteins have been prepared from Peptostreptococcus elsdenii, C. pasteurianum and Clostridium MP flavodoxins by dialysis of the native proteins against 2 M KBr at pH 3.9 and 3.10[middle dot]10-4 M EDTA. The apoproteins each bind 1 molecule of FMN to give complexes identical with the native flavodoxins.2. 2. Binding causes almost complete quenching of both protein and FMN fluorescence. This property has been used to determine the dissociation constant for the dissociation of P. elsdenii flavodoxin into apoprotein and FMN, and to follow the kinetics of the interaction. The dissociation constant determined at pH 6.55 and 20[deg] was 4.26[middle dot]10-10 M. The maximum rate of binding occurs at pH 4.4 and is described by a second order rate constant of 2.6[middle dot]105 M-1[middle dot]cm-1 at 0.5[deg]. The rate is markedly influenced by the salt composition of the solution.3. 3. Addition of excess apoprotein to FAD, riboflavin or lumiflavin causes only a small decrease in the flavin fluorescence, suggesting that binding of these compounds is weak.4. 4. Two derivatives of FMN, iso-FMN and 3,4-dihydro FMN form strong, complexes with apoflavodoxin. In the case of iso-FMN and P. elsdenii apoflavodoxin the complex is catalytically active, and it is reduced by systems which reduce native flavodoxin. The complex of 3,4-dihydro FMN is catalytically inactive.5. 5. C. pasteurianum, P. elsdenii and Clostridium MP flavodoxins contain 1, 2 and 3 sulfhydryl groups, respectively. Experiments with p-chloromercuribenzoate and N-ethylmaleimide indicate that at least one sulfhydryl group is important for flavin binding.en_US
dc.format.extent886518 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleStudies on flavin binding in flavodoxinsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48104, U.S.A.en_US
dc.identifier.pmid5317635en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/33652/1/0000161.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0005-2744(71)90207-5en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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