| pubmed-article:10092615 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10092615 | lifeskim:mentions | umls-concept:C0054563 | lld:lifeskim |
| pubmed-article:10092615 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10092615 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:10092615 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10092615 | lifeskim:mentions | umls-concept:C0072628 | lld:lifeskim |
| pubmed-article:10092615 | lifeskim:mentions | umls-concept:C2348951 | lld:lifeskim |
| pubmed-article:10092615 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:10092615 | pubmed:dateCreated | 1999-4-27 | lld:pubmed |
| pubmed-article:10092615 | pubmed:abstractText | During the monooxygenase reaction catalyzed by cytochrome P450cam (P450cam), a ternary complex of P450cam, reduced putidaredoxin, and d-camphor is formed as an obligatory reaction intermediate. When ligands such as CO, NO, and O2 bind to the heme iron of P450cam in the intermediate complex, the EPR spectrum of reduced putidaredoxin with a characteristic signal at 346 millitesla at 77 K changed into a spectrum having a new signal at 348 millitesla. The experiment with O2 was carried out by employing a mutant P450cam with Asp251 --> Asn or Gly where the rate of electron transfer from putidaredoxin to oxyferrous P450cam is considerably reduced. Such a ligand-induced EPR spectral change of putidaredoxin was also shown in situ in Pseudomonas putida. Mutations introduced into the neighborhood of the iron-sulfur cluster of putidaredoxin revealed that a Ser44 --> Gly mutation mimicked the ligand-induced spectral change of putidaredoxin. Arg109 and Arg112, which are in the putative putidaredoxin binding site of P450cam, were essential for the spectral changes of putidaredoxin in the complex. These results indicate that a change in the P450cam active site that is the consequence of an altered spin state is transmitted to putidaredoxin within the ternary complex and produces a conformational change of the 2Fe-2S active center. | lld:pubmed |
| pubmed-article:10092615 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10092615 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092615 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10092615 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10092615 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10092615 | pubmed:author | pubmed-author:ShimadaHH | lld:pubmed |
| pubmed-article:10092615 | pubmed:author | pubmed-author:IshimuraYY | lld:pubmed |
| pubmed-article:10092615 | pubmed:author | pubmed-author:ObataTT | lld:pubmed |
| pubmed-article:10092615 | pubmed:author | pubmed-author:NaganoSS | lld:pubmed |
| pubmed-article:10092615 | pubmed:author | pubmed-author:HoriHH | lld:pubmed |
| pubmed-article:10092615 | pubmed:author | pubmed-author:EgawaTT | lld:pubmed |
| pubmed-article:10092615 | pubmed:author | pubmed-author:UnnoMM | lld:pubmed |
| pubmed-article:10092615 | pubmed:author | pubmed-author:ArigaYY | lld:pubmed |
| pubmed-article:10092615 | pubmed:author | pubmed-author:MasuyaFF | lld:pubmed |
| pubmed-article:10092615 | pubmed:author | pubmed-author:HishikiTT | lld:pubmed |
| pubmed-article:10092615 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10092615 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:10092615 | pubmed:volume | 274 | lld:pubmed |
| pubmed-article:10092615 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10092615 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10092615 | pubmed:pagination | 9363-9 | lld:pubmed |
| pubmed-article:10092615 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10092615 | pubmed:meshHeading | pubmed-meshheading:10092615... | lld:pubmed |
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| pubmed-article:10092615 | pubmed:meshHeading | pubmed-meshheading:10092615... | lld:pubmed |
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| pubmed-article:10092615 | pubmed:meshHeading | pubmed-meshheading:10092615... | lld:pubmed |
| pubmed-article:10092615 | pubmed:meshHeading | pubmed-meshheading:10092615... | lld:pubmed |
| pubmed-article:10092615 | pubmed:meshHeading | pubmed-meshheading:10092615... | lld:pubmed |
| pubmed-article:10092615 | pubmed:meshHeading | pubmed-meshheading:10092615... | lld:pubmed |
| pubmed-article:10092615 | pubmed:meshHeading | pubmed-meshheading:10092615... | lld:pubmed |
| pubmed-article:10092615 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10092615 | pubmed:articleTitle | Putidaredoxin-cytochrome p450cam interaction. Spin state of the heme iron modulates putidaredoxin structure. | lld:pubmed |
| pubmed-article:10092615 | pubmed:affiliation | Department of Biochemistry, School of Medicine, Keio University, Shinano-machi, Shinjuku-ku, Tokyo 160-8582, Japan. shimada@med.keio.ac.jp | lld:pubmed |
| pubmed-article:10092615 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10092615 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10092615 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10092615 | lld:pubmed |
