Evidence for a novel flavin prosthetic group associated with NADH dehydrogenase from Peptostreptococcus elsdenii
dc.contributor.author | Mayhew, Stephen G. | en_US |
dc.contributor.author | Massey, Vincent | en_US |
dc.date.accessioned | 2006-04-17T16:26:50Z | |
dc.date.available | 2006-04-17T16:26:50Z | |
dc.date.issued | 1971-05-12 | en_US |
dc.identifier.citation | Mayhew, Stephen G., Massey, Vincent (1971/05/12)."Evidence for a novel flavin prosthetic group associated with NADH dehydrogenase from Peptostreptococcus elsdenii." Biochimica et Biophysica Acta (BBA) - Enzymology 235(2): 303-310. <http://hdl.handle.net/2027.42/33653> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73GH-47GGN9W-4/2/314b563e1b47ce5f088af797eeac2315 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/33653 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5317636&dopt=citation | en_US |
dc.description.abstract | 1. 1. NADH dehydrogenase (EC 1.6.99.3) has been purified from the strictly anaerobic rumen bacterium Peptostreptococcus elsdenii. The purified protein is specific for NADH as electron donor; it can use 2,6-dichlorophenolindophenol (DCIP), cytochrome c, K3FE(CN)6 or flavodoxin as electron acceptor. It has a molecular weight of about 63 000. The absorption spectrum shows maxima at 475, 375, 356, 318, and 273 nm. It has shoulders at 425, 460, and 510 nm. The protein is fluorescent with an emission maximum at 550 nm.2. 2. The chromophore is released from the NADH dehydrogenase by either heat treatment or extraction with trichloroacetic acid. The free chromophore shows an increase of absorption in the visible spectrum and a shift of the maximum to 470 nm. The fluorescence emission maximum is shifted to 530 nm, but the intensity is unchanged.3. 3. Hydrolysis of the free chromophore with phosphodiesterase causes a 12% increase in the visible absorption and a 2-fold increase in the fluorescence (exciting light at 480 nm). The chromatographic behavior is also affected by this treatment.4. 4. The hydrolysed chromophore is bound by apoflavodoxin with 95% quenching of the fluorescence and an 18% decrease in the visible absorption. The complex of apoflavodoxin and the unknown chromophore is reduced by light irradiation in the presence of EDTA to an intermediate similar to flavodoxin semiquinone but with a distinctively different absorption spectrum. It is concluded that the chromophore in the NADH dehydrogenase is a flavin dinucleotide similar to FAD but modified in the isoalloxazine ring. | en_US |
dc.format.extent | 463021 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Evidence for a novel flavin prosthetic group associated with NADH dehydrogenase from Peptostreptococcus elsdenii | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.identifier.pmid | 5317636 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/33653/1/0000162.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2744(71)90208-7 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.