| pubmed-article:3095321 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3095321 | lifeskim:mentions | umls-concept:C0038404 | lld:lifeskim |
| pubmed-article:3095321 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:3095321 | lifeskim:mentions | umls-concept:C0030012 | lld:lifeskim |
| pubmed-article:3095321 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:3095321 | lifeskim:mentions | umls-concept:C0068343 | lld:lifeskim |
| pubmed-article:3095321 | lifeskim:mentions | umls-concept:C0597331 | lld:lifeskim |
| pubmed-article:3095321 | pubmed:issue | 31 | lld:pubmed |
| pubmed-article:3095321 | pubmed:dateCreated | 1986-11-26 | lld:pubmed |
| pubmed-article:3095321 | pubmed:abstractText | The flavin-containing NADH peroxidase of Streptococcus faecalis 10C1, which catalyzes the reaction: NADH + H+ + H2O2----NAD+ + 2H2O, has been purified to homogeneity in our laboratory for analyses of both its structure and redox behavior. Our findings indicate that the enzyme is a tetramer of four apparently identical subunits (Mr = 46,000/subunit), each containing one FAD coenzyme and a second non-flavin, nonmetal redox center. There is no evidence of nonequivalence among the flavins. Dithionite reduction of the enzyme occurs in two steps, with end points of 0.96 and 2.05 eq/FAD. The first step generates a two-electron reduced form of the enzyme (EH2) which is spectrally identical with that generated by aerobic addition of NADH. Our studies suggest that the long-wavelength absorbance band (lambda max approximately 540 nm) exhibited by this form results from charge-transfer interaction between the reduced non-flavin redox center and the oxidized flavin. A second type of long-wavelength charge-transfer absorbance band (lambda max approximately 770 nm) is generated on anaerobic addition of 1 eq of NADH to EH2 and results from interaction between oxidized FAD and the reduced pyridine nucleotide. Either the EH2 X NAD+ or the EH2 X NAD+ X NADH forms may be involved in the catalytic mechanism of the enzyme, as both are reactive with hydrogen peroxide. | lld:pubmed |
| pubmed-article:3095321 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3095321 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3095321 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3095321 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3095321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3095321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3095321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3095321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3095321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3095321 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3095321 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3095321 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:3095321 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3095321 | pubmed:author | pubmed-author:ClaiborneAA | lld:pubmed |
| pubmed-article:3095321 | pubmed:author | pubmed-author:PoppoM JMJ | lld:pubmed |
| pubmed-article:3095321 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3095321 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:3095321 | pubmed:volume | 261 | lld:pubmed |
| pubmed-article:3095321 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3095321 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3095321 | pubmed:pagination | 14525-33 | lld:pubmed |
| pubmed-article:3095321 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3095321 | pubmed:meshHeading | pubmed-meshheading:3095321-... | lld:pubmed |
| pubmed-article:3095321 | pubmed:meshHeading | pubmed-meshheading:3095321-... | lld:pubmed |
| pubmed-article:3095321 | pubmed:meshHeading | pubmed-meshheading:3095321-... | lld:pubmed |
| pubmed-article:3095321 | pubmed:meshHeading | pubmed-meshheading:3095321-... | lld:pubmed |
| pubmed-article:3095321 | pubmed:meshHeading | pubmed-meshheading:3095321-... | lld:pubmed |
| pubmed-article:3095321 | pubmed:meshHeading | pubmed-meshheading:3095321-... | lld:pubmed |
| pubmed-article:3095321 | pubmed:meshHeading | pubmed-meshheading:3095321-... | lld:pubmed |
| pubmed-article:3095321 | pubmed:meshHeading | pubmed-meshheading:3095321-... | lld:pubmed |
| pubmed-article:3095321 | pubmed:meshHeading | pubmed-meshheading:3095321-... | lld:pubmed |
| pubmed-article:3095321 | pubmed:meshHeading | pubmed-meshheading:3095321-... | lld:pubmed |
| pubmed-article:3095321 | pubmed:meshHeading | pubmed-meshheading:3095321-... | lld:pubmed |
| pubmed-article:3095321 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3095321 | pubmed:articleTitle | Interactions of pyridine nucleotides with redox forms of the flavin-containing NADH peroxidase from Streptococcus faecalis. | lld:pubmed |
| pubmed-article:3095321 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3095321 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3095321 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:3095321 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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