| pubmed-article:19356022 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19356022 | lifeskim:mentions | umls-concept:C0004927 | lld:lifeskim |
| pubmed-article:19356022 | lifeskim:mentions | umls-concept:C0010749 | lld:lifeskim |
| pubmed-article:19356022 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:19356022 | lifeskim:mentions | umls-concept:C0030012 | lld:lifeskim |
| pubmed-article:19356022 | lifeskim:mentions | umls-concept:C0220825 | lld:lifeskim |
| pubmed-article:19356022 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:19356022 | lifeskim:mentions | umls-concept:C0013812 | lld:lifeskim |
| pubmed-article:19356022 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19356022 | pubmed:dateCreated | 2009-4-9 | lld:pubmed |
| pubmed-article:19356022 | pubmed:abstractText | Electrochemical studies of three c-type cytochromes (cyt c from horse heart, cyt c(2) from Rhodospirillum rubrum, and cyt c(553) from Alcaligenes xylosoxidans GIFU 1051) were performed by using the optically active Co(III) complex-modified Au electrode. Three cytochromes gave different redox behaviors reflected from the respective structural information. From relationship between their redox behaviors and their structural characteristics, we evaluated the solution structure around heme center of cyt c(553). | lld:pubmed |
| pubmed-article:19356022 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19356022 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19356022 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19356022 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19356022 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19356022 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19356022 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19356022 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19356022 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19356022 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19356022 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19356022 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19356022 | pubmed:issn | 1872-3128 | lld:pubmed |
| pubmed-article:19356022 | pubmed:author | pubmed-author:MasudaHidekiH | lld:pubmed |
| pubmed-article:19356022 | pubmed:author | pubmed-author:TakahashiIsao... | lld:pubmed |
| pubmed-article:19356022 | pubmed:author | pubmed-author:OzawaTomohiro... | lld:pubmed |
| pubmed-article:19356022 | pubmed:author | pubmed-author:FunahashiYasu... | lld:pubmed |
| pubmed-article:19356022 | pubmed:author | pubmed-author:InomataTomohi... | lld:pubmed |
| pubmed-article:19356022 | pubmed:author | pubmed-author:NishijimaChik... | lld:pubmed |
| pubmed-article:19356022 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19356022 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:19356022 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19356022 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19356022 | pubmed:pagination | 73-5 | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:meshHeading | pubmed-meshheading:19356022... | lld:pubmed |
| pubmed-article:19356022 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:19356022 | pubmed:articleTitle | Structures of various cytochromes c evaluated from the redox behaviors using the optically active Co(III) complex-modified Au electrode. | lld:pubmed |
| pubmed-article:19356022 | pubmed:affiliation | Department of Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan. | lld:pubmed |
| pubmed-article:19356022 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19356022 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
