| pubmed-article:10074352 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10074352 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:10074352 | lifeskim:mentions | umls-concept:C0014653 | lld:lifeskim |
| pubmed-article:10074352 | lifeskim:mentions | umls-concept:C0085494 | lld:lifeskim |
| pubmed-article:10074352 | lifeskim:mentions | umls-concept:C0030012 | lld:lifeskim |
| pubmed-article:10074352 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:10074352 | lifeskim:mentions | umls-concept:C0205099 | lld:lifeskim |
| pubmed-article:10074352 | lifeskim:mentions | umls-concept:C0332514 | lld:lifeskim |
| pubmed-article:10074352 | lifeskim:mentions | umls-concept:C0528631 | lld:lifeskim |
| pubmed-article:10074352 | lifeskim:mentions | umls-concept:C0131722 | lld:lifeskim |
| pubmed-article:10074352 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:10074352 | pubmed:dateCreated | 1999-3-23 | lld:pubmed |
| pubmed-article:10074352 | pubmed:abstractText | Recent studies [Mallett, T. C., and Claiborne, A. (1998) Biochemistry 37, 8790-8802] of the O2 reactivity of C42S NADH oxidase (O2 --> H2O2) revealed an asymmetric mechanism in which the two FADH2.NAD+ per reduced dimer display kinetic inequivalence. In this report we provide evidence indicating that the fully active, recombinant wild-type oxidase (O2 --> 2H2O) displays thermodynamic inequivalence between the two active sites per dimer. Using NADPH to generate the free reduced wild-type enzyme (EH2'/EH4), we have shown that NAD+ titrations lead to differential behavior as only one FADH2 per dimer binds NAD+ tightly to give the charge-transfer complex. The second FADH2, in contrast, transfers its electrons to the single Cys42-sulfenic acid (Cys42-SOH) redox center, which remains oxidized during the reductive titration. Titrations of the reduced NADH oxidase with oxidized 3-acetylpyridine and 3-aminopyridine adenine dinucleotides further support the conclusion that the two FADH2 per dimer in wild-type enzyme can be described as distinct "charge-transfer" and "electron-transfer" sites, with the latter site giving rise to either intramolecular (Cys42-SOH) or bimolecular (pyridine nucleotide) reduction. The reduced C42S mutant is not capable of intramolecular electron transfer on binding pyridine nucleotides, thus confirming that the Cys42-SOH center is in fact the source of the redox asymmetry observed with wild-type oxidase. These observations on the role of Cys42-SOH in the expression of thermodynamic inequivalence as observed in wild-type NADH oxidase complement the previously described kinetic inequivalence of the C42S mutant; taken together, these results provide the overlapping framework for an alternating sites cooperativity model of oxidase action. | lld:pubmed |
| pubmed-article:10074352 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10074352 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10074352 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10074352 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10074352 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10074352 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10074352 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10074352 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10074352 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:10074352 | pubmed:author | pubmed-author:ClaiborneAA | lld:pubmed |
| pubmed-article:10074352 | pubmed:author | pubmed-author:ParsonageDD | lld:pubmed |
| pubmed-article:10074352 | pubmed:author | pubmed-author:MallettT CTC | lld:pubmed |
| pubmed-article:10074352 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10074352 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:10074352 | pubmed:volume | 38 | lld:pubmed |
| pubmed-article:10074352 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10074352 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10074352 | pubmed:pagination | 3000-11 | lld:pubmed |
| pubmed-article:10074352 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10074352 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10074352 | pubmed:articleTitle | Equilibrium analyses of the active-site asymmetry in enterococcal NADH oxidase: role of the cysteine-sulfenic acid redox center. | lld:pubmed |
| pubmed-article:10074352 | pubmed:affiliation | Department of Biochemistry, Wake Forest University Medical Center, Winston-Salem, North Carolina 27157, USA. | lld:pubmed |
| pubmed-article:10074352 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10074352 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10074352 | lld:pubmed |
