| pubmed-article:10781602 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C0024432 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C0016213 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C0132555 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C0806140 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C0599946 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C0013852 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:10781602 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:10781602 | pubmed:issue | 29 | lld:pubmed |
| pubmed-article:10781602 | pubmed:dateCreated | 2000-8-24 | lld:pubmed |
| pubmed-article:10781602 | pubmed:abstractText | The sequences of nitric-oxide synthase (NOS) flavin domains closely resemble that of NADPH-cytochrome P450 reductase (CPR), with the exception of a few regions. One such region is the C terminus; all NOS isoforms are 20-40 amino acids longer than CPR, forming a "tail" that is absent in CPR. To investigate its function, we removed the 21-amino acid C-terminal tail from murine macrophage inducible NOS (iNOS) holoenzyme and from a flavin domain construct. Both the truncated holoenzyme and reductase domain exhibited cytochrome c reductase activities that were 7-10-fold higher than the nontruncated forms. The truncated holoenzyme catalyzed NO formation approximately 20% faster than the intact form. Using stopped-flow spectrophotometry, we demonstrated that electron transfer into and between the two flavins and from the flavin to the heme domain is 2-5-fold faster in the absence of the C-terminal tail. The heme-nitrosyl complex, formed in all NOS isoforms during NO catalysis, is 5-fold less stable in truncated iNOS. Although both CPR and intact NOS can exist in a stable, one electron-reduced semiquinone form, neither the truncated holoenzyme nor the truncated flavin domain demonstrate such a form. We propose that this C-terminal tail curls back to interact with the flavin domain in such a way as to modulate the interaction between the two flavin moieties. | lld:pubmed |
| pubmed-article:10781602 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10781602 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10781602 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10781602 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10781602 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10781602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10781602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10781602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10781602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10781602 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10781602 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10781602 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10781602 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10781602 | pubmed:author | pubmed-author:MillerR TRT | lld:pubmed |
| pubmed-article:10781602 | pubmed:author | pubmed-author:KimJ JJJ | lld:pubmed |
| pubmed-article:10781602 | pubmed:author | pubmed-author:RomanL JLJ | lld:pubmed |
| pubmed-article:10781602 | pubmed:author | pubmed-author:Siler... | lld:pubmed |
| pubmed-article:10781602 | pubmed:author | pubmed-author:de La... | lld:pubmed |
| pubmed-article:10781602 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10781602 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:10781602 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10781602 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10781602 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10781602 | pubmed:pagination | 21914-9 | lld:pubmed |
| pubmed-article:10781602 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10781602 | pubmed:meshHeading | pubmed-meshheading:10781602... | lld:pubmed |
| pubmed-article:10781602 | pubmed:meshHeading | pubmed-meshheading:10781602... | lld:pubmed |
| pubmed-article:10781602 | pubmed:meshHeading | pubmed-meshheading:10781602... | lld:pubmed |
| pubmed-article:10781602 | pubmed:meshHeading | pubmed-meshheading:10781602... | lld:pubmed |
| pubmed-article:10781602 | pubmed:meshHeading | pubmed-meshheading:10781602... | lld:pubmed |
| pubmed-article:10781602 | pubmed:meshHeading | pubmed-meshheading:10781602... | lld:pubmed |
| pubmed-article:10781602 | pubmed:meshHeading | pubmed-meshheading:10781602... | lld:pubmed |
| pubmed-article:10781602 | pubmed:meshHeading | pubmed-meshheading:10781602... | lld:pubmed |
| pubmed-article:10781602 | pubmed:meshHeading | pubmed-meshheading:10781602... | lld:pubmed |
| pubmed-article:10781602 | pubmed:meshHeading | pubmed-meshheading:10781602... | lld:pubmed |
| pubmed-article:10781602 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10781602 | pubmed:articleTitle | The C terminus of mouse macrophage inducible nitric-oxide synthase attenuates electron flow through the flavin domain. | lld:pubmed |
| pubmed-article:10781602 | pubmed:affiliation | Department of Biochemistry, The University of Texas Health Science Center, San Antonio, Texas 78229, USA. | lld:pubmed |
| pubmed-article:10781602 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10781602 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10781602 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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