| pubmed-article:19691141 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19691141 | lifeskim:mentions | umls-concept:C0132555 | lld:lifeskim |
| pubmed-article:19691141 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
| pubmed-article:19691141 | lifeskim:mentions | umls-concept:C0456962 | lld:lifeskim |
| pubmed-article:19691141 | lifeskim:mentions | umls-concept:C2346592 | lld:lifeskim |
| pubmed-article:19691141 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:19691141 | pubmed:dateCreated | 2009-8-18 | lld:pubmed |
| pubmed-article:19691141 | pubmed:abstractText | During catalysis, the heme in nitric oxide synthase (NOS) binds NO before releasing it to the environment. Oxidation of the NOS ferrous heme-NO complex by O2 is key for catalytic cycling, but the mechanism is unclear. We utilized stopped-flow methods to study the reaction of O2 with ferrous heme-NO complexes of inducible and neuronal NOS enzymes. We found that the reaction does not involve heme-NO dissociation, but instead proceeds by a rapid direct reaction of O2 with the ferrous heme-NO complex. This behavior is novel and may distinguish heme-thiolate enzymes, such as NOS, from related heme proteins. | lld:pubmed |
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| pubmed-article:19691141 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19691141 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19691141 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19691141 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:19691141 | pubmed:issn | 1742-4658 | lld:pubmed |
| pubmed-article:19691141 | pubmed:author | pubmed-author:StuehrDennis... | lld:pubmed |
| pubmed-article:19691141 | pubmed:author | pubmed-author:SantoliniJérô... | lld:pubmed |
| pubmed-article:19691141 | pubmed:author | pubmed-author:TejeroJesúsJ | lld:pubmed |
| pubmed-article:19691141 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19691141 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:19691141 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19691141 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19691141 | pubmed:pagination | 4505-14 | lld:pubmed |
| pubmed-article:19691141 | pubmed:dateRevised | 2011-6-15 | lld:pubmed |
| pubmed-article:19691141 | pubmed:meshHeading | pubmed-meshheading:19691141... | lld:pubmed |
| pubmed-article:19691141 | pubmed:meshHeading | pubmed-meshheading:19691141... | lld:pubmed |
| pubmed-article:19691141 | pubmed:meshHeading | pubmed-meshheading:19691141... | lld:pubmed |
| pubmed-article:19691141 | pubmed:meshHeading | pubmed-meshheading:19691141... | lld:pubmed |
| pubmed-article:19691141 | pubmed:meshHeading | pubmed-meshheading:19691141... | lld:pubmed |
| pubmed-article:19691141 | pubmed:meshHeading | pubmed-meshheading:19691141... | lld:pubmed |
| pubmed-article:19691141 | pubmed:meshHeading | pubmed-meshheading:19691141... | lld:pubmed |
| pubmed-article:19691141 | pubmed:meshHeading | pubmed-meshheading:19691141... | lld:pubmed |
| pubmed-article:19691141 | pubmed:meshHeading | pubmed-meshheading:19691141... | lld:pubmed |
| pubmed-article:19691141 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19691141 | pubmed:articleTitle | Fast ferrous heme-NO oxidation in nitric oxide synthases. | lld:pubmed |
| pubmed-article:19691141 | pubmed:affiliation | Department of Pathobiology, The Cleveland Clinic Foundation, Lerner Research Institute, 9500 Euclid Ave., Cleveland, OH 44195, USA. | lld:pubmed |
