| pubmed-article:7703349 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7703349 | lifeskim:mentions | umls-concept:C0010760 | lld:lifeskim |
| pubmed-article:7703349 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:7703349 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:7703349 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7703349 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7703349 | pubmed:dateCreated | 1995-5-9 | lld:pubmed |
| pubmed-article:7703349 | pubmed:abstractText | Cytochrome c is responsible for over 90% of the dioxygen consumption in the living cell and contributes to the build-up of a proton electrochemical gradient derived by the vectorial transfer of electrons between cytochrome c and molecular oxygen. The metal ions found in cytochrome oxidases play a crucial role in these processes and have been extensively studied. In this review we present and discuss some of the relevant spectroscopic and kinetic properties of the prosthetic groups of cytochrome c oxidase. | lld:pubmed |
| pubmed-article:7703349 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7703349 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7703349 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7703349 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7703349 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7703349 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7703349 | pubmed:issn | 0301-4622 | lld:pubmed |
| pubmed-article:7703349 | pubmed:author | pubmed-author:BrunoriMM | lld:pubmed |
| pubmed-article:7703349 | pubmed:author | pubmed-author:SartiPP | lld:pubmed |
| pubmed-article:7703349 | pubmed:author | pubmed-author:AntoniniGG | lld:pubmed |
| pubmed-article:7703349 | pubmed:author | pubmed-author:MalatestaFF | lld:pubmed |
| pubmed-article:7703349 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7703349 | pubmed:volume | 54 | lld:pubmed |
| pubmed-article:7703349 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7703349 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7703349 | pubmed:pagination | 1-33 | lld:pubmed |
| pubmed-article:7703349 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7703349 | pubmed:meshHeading | pubmed-meshheading:7703349-... | lld:pubmed |
| pubmed-article:7703349 | pubmed:meshHeading | pubmed-meshheading:7703349-... | lld:pubmed |
| pubmed-article:7703349 | pubmed:meshHeading | pubmed-meshheading:7703349-... | lld:pubmed |
| pubmed-article:7703349 | pubmed:meshHeading | pubmed-meshheading:7703349-... | lld:pubmed |
| pubmed-article:7703349 | pubmed:meshHeading | pubmed-meshheading:7703349-... | lld:pubmed |
| pubmed-article:7703349 | pubmed:meshHeading | pubmed-meshheading:7703349-... | lld:pubmed |
| pubmed-article:7703349 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7703349 | pubmed:articleTitle | Structure and function of a molecular machine: cytochrome c oxidase. | lld:pubmed |
| pubmed-article:7703349 | pubmed:affiliation | Department of Experimental Medicine, University of Rome, Tor Vergata, Italy. | lld:pubmed |
| pubmed-article:7703349 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7703349 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:7703349 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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