| pubmed-article:8312474 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8312474 | lifeskim:mentions | umls-concept:C1167297 | lld:lifeskim |
| pubmed-article:8312474 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:8312474 | lifeskim:mentions | umls-concept:C0016315 | lld:lifeskim |
| pubmed-article:8312474 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8312474 | pubmed:dateCreated | 1994-3-23 | lld:pubmed |
| pubmed-article:8312474 | pubmed:abstractText | It has been known for some time that dicyclohexylcarbodiimide (DCCD) inhibits the proton translocation function of the cytochrome c oxidase complex (CcO) and that there is one major site in subunit III which is modified upon reaction with DCCD (Glu-90 for the bovine enzyme). We have examined the reaction of bovine CcO with N-cyclohexyl-N'-(4-dimethylamino-alpha-napthyl)carbodiimide (NCD-4), a fluorescent analog of DCCD. NCD-4 labeling of CcO is strongly inhibited by DCCD implicating Glu-90 of subunit III as the site of chemical modification by NCD-4. The fluorescence of reconstituted NCD-4-labeled bovine CcO is strongly quenched by hydrophobic nitroxides, whereas hydrophilic nitroxides and iodide ions have a reduced quenching ability. It is concluded that the Glu-90 of subunit III resides near the protein-lipid interface of the membrane spanning region of the enzyme. Different quenching abilities of 5-, 7-, 10-, 12-, and 16-4,4-dimethyl-3-oxazolinyloxy-stearic acids suggest that the NCD-4 label is located in the membrane bilayer in the region near the middle of the hydrocarbon tail of stearic acid. In light of these results, it is unlikely that Glu-90 is part of a proton channel that is associated with the proton pumping machinery of the enzyme but the outcome of this study does not eliminate an allosteric regulatory role for this residue. | lld:pubmed |
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| pubmed-article:8312474 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8312474 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8312474 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8312474 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8312474 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8312474 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:8312474 | pubmed:author | pubmed-author:ChanS ISI | lld:pubmed |
| pubmed-article:8312474 | pubmed:author | pubmed-author:LarsenR WRW | lld:pubmed |
| pubmed-article:8312474 | pubmed:author | pubmed-author:MusserS MSM | lld:pubmed |
| pubmed-article:8312474 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8312474 | pubmed:volume | 65 | lld:pubmed |
| pubmed-article:8312474 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8312474 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8312474 | pubmed:pagination | 2348-59 | lld:pubmed |
| pubmed-article:8312474 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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