pubmed-article:8119391 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8119391 | lifeskim:mentions | umls-concept:C0004595 | lld:lifeskim |
pubmed-article:8119391 | lifeskim:mentions | umls-concept:C0009968 | lld:lifeskim |
pubmed-article:8119391 | lifeskim:mentions | umls-concept:C0242417 | lld:lifeskim |
pubmed-article:8119391 | lifeskim:mentions | umls-concept:C0205099 | lld:lifeskim |
pubmed-article:8119391 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:8119391 | pubmed:dateCreated | 1994-4-4 | lld:pubmed |
pubmed-article:8119391 | pubmed:abstractText | A copper-containing domain of the caa3-type oxidase from Bacillus subtilis has been expressed as a water-soluble protein in the cytoplasm of Escherichia coli. Electron paramagnetic resonance (EPR) spectra of this purple domain show well-resolved lines in the gz resonance, both at X-band and S-band frequencies. Interpretation of EPR spectra and analytical data indicate a binuclear copper site consisting of one Cu2+ and one Cu1+. This copper site closely resembles CuA in subunit II of cytochrome c oxidase and is shown here to be a mixed-valence [Cu2+-Cu1+] binuclear centre. | lld:pubmed |
pubmed-article:8119391 | pubmed:language | eng | lld:pubmed |
pubmed-article:8119391 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8119391 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8119391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8119391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8119391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8119391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8119391 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8119391 | pubmed:month | Feb | lld:pubmed |
pubmed-article:8119391 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:8119391 | pubmed:author | pubmed-author:de VriesSS | lld:pubmed |
pubmed-article:8119391 | pubmed:author | pubmed-author:van der... | lld:pubmed |
pubmed-article:8119391 | pubmed:author | pubmed-author:von... | lld:pubmed |
pubmed-article:8119391 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8119391 | pubmed:day | 28 | lld:pubmed |
pubmed-article:8119391 | pubmed:volume | 340 | lld:pubmed |
pubmed-article:8119391 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8119391 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8119391 | pubmed:pagination | 109-13 | lld:pubmed |
pubmed-article:8119391 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:8119391 | pubmed:meshHeading | pubmed-meshheading:8119391-... | lld:pubmed |
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pubmed-article:8119391 | pubmed:meshHeading | pubmed-meshheading:8119391-... | lld:pubmed |
pubmed-article:8119391 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:8119391 | pubmed:articleTitle | The CuAsite of the caa3-type oxidase of Bacillus subtilis is a mixed-valence binuclear copper centre. | lld:pubmed |
pubmed-article:8119391 | pubmed:affiliation | Department of Molecular and Cellular Biology, BioCentrum Amsterdam, Vrije Universiteit, The Netherlands. | lld:pubmed |
pubmed-article:8119391 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8119391 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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