pubmed-article:7656985 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7656985 | lifeskim:mentions | umls-concept:C0599132 | lld:lifeskim |
pubmed-article:7656985 | lifeskim:mentions | umls-concept:C0008260 | lld:lifeskim |
pubmed-article:7656985 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:7656985 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:7656985 | lifeskim:mentions | umls-concept:C0206055 | lld:lifeskim |
pubmed-article:7656985 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:7656985 | pubmed:dateCreated | 1995-10-4 | lld:pubmed |
pubmed-article:7656985 | pubmed:abstractText | A Fourier transform infrared (FTIR) difference spectrum upon photooxidation of the accessory chlorophyll (Chlz) of photosystem II (PS II) was obtained at 210 K with Mn-depleted PS II membranes in the presence of fericyanide and silicomolybdate. The observed Chlz+/Chlz spectrum showed two differential bands at 1747/1736 and 1714/1684 cm-1. The former was assigned to the free carbomethoxy C = 0 and the latter to the keto C = 0 that is hydrogen-bonded or in a highly polar environment. Also, the negative 1614 cm-1 band assignable to the macrocycle mode indicated 5-coordination of the central Mg. The negative 1660 cm-1 band, possibly due to the strongly hydrogen-bonded keto C = 0, may suggest oxidation of one more Chlz, although an alternative assignment, the amide I mode of proteins perturbed by Chlz oxidation, is also possible. | lld:pubmed |
pubmed-article:7656985 | pubmed:language | eng | lld:pubmed |
pubmed-article:7656985 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7656985 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7656985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7656985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7656985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7656985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7656985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7656985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7656985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7656985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7656985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7656985 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7656985 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7656985 | pubmed:month | Aug | lld:pubmed |
pubmed-article:7656985 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:7656985 | pubmed:author | pubmed-author:InoueYY | lld:pubmed |
pubmed-article:7656985 | pubmed:author | pubmed-author:NoguchiTT | lld:pubmed |
pubmed-article:7656985 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7656985 | pubmed:day | 21 | lld:pubmed |
pubmed-article:7656985 | pubmed:volume | 370 | lld:pubmed |
pubmed-article:7656985 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7656985 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7656985 | pubmed:pagination | 241-4 | lld:pubmed |
pubmed-article:7656985 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:meshHeading | pubmed-meshheading:7656985-... | lld:pubmed |
pubmed-article:7656985 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7656985 | pubmed:articleTitle | Molecular interactions of the redox-active accessory chlorophyll on the electron-donor side of photosystem II as studied by Fourier transform infrared spectroscopy. | lld:pubmed |
pubmed-article:7656985 | pubmed:affiliation | Photosynthesis Research laboratory, Institute of Physical and Chemical Research (RIKEN), Saitama, Japan. | lld:pubmed |
pubmed-article:7656985 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7656985 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |