| pubmed-article:19154182 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19154182 | lifeskim:mentions | umls-concept:C1882071 | lld:lifeskim |
| pubmed-article:19154182 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:19154182 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:19154182 | lifeskim:mentions | umls-concept:C0205108 | lld:lifeskim |
| pubmed-article:19154182 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:19154182 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:19154182 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:19154182 | lifeskim:mentions | umls-concept:C0150312 | lld:lifeskim |
| pubmed-article:19154182 | lifeskim:mentions | umls-concept:C2346592 | lld:lifeskim |
| pubmed-article:19154182 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:19154182 | pubmed:dateCreated | 2009-3-24 | lld:pubmed |
| pubmed-article:19154182 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19154182 | pubmed:abstractText | HO (haem oxygenase) catalyses the degradation of haem to biliverdin, CO and ferrous iron via three successive oxygenation reactions, i.e. haem to alpha-hydroxyhaem, alpha-hydroxyhaem to alpha-verdohaem and alpha-verdohaem to ferric biliverdin-iron chelate. In the present study, we determined the crystal structure of ferrous alpha-verdohaem-rat HO-1 complex at 2.2 A (1 A=0.1 nm) resolution. The overall structure of the verdohaem complex was similar to that of the haem complex. Water or OH- was co-ordinated to the verdohaem iron as a distal ligand. A hydrogen-bond network consisting of water molecules and several amino acid residues was observed at the distal side of verdohaem. Such a hydrogen-bond network was conserved in the structures of rat HO-1 complexes with haem and with the ferric biliverdin-iron chelate. This hydrogen-bond network may act as a proton donor to form an activated oxygen intermediate, probably a ferric hydroperoxide species, in the degradation of alpha-verdohaem to ferric biliverdin-iron chelate similar to that seen in the first oxygenation step. | lld:pubmed |
| pubmed-article:19154182 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19154182 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19154182 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19154182 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19154182 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19154182 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19154182 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19154182 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19154182 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:19154182 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:19154182 | pubmed:author | pubmed-author:HigashimotoYu... | lld:pubmed |
| pubmed-article:19154182 | pubmed:author | pubmed-author:FukuyamaKeiic... | lld:pubmed |
| pubmed-article:19154182 | pubmed:author | pubmed-author:SakamotoHiros... | lld:pubmed |
| pubmed-article:19154182 | pubmed:author | pubmed-author:SugishimaMasa... | lld:pubmed |
| pubmed-article:19154182 | pubmed:author | pubmed-author:NoguchiMasato... | lld:pubmed |
| pubmed-article:19154182 | pubmed:author | pubmed-author:SatoHideakiH | lld:pubmed |
| pubmed-article:19154182 | pubmed:author | pubmed-author:PalmerGrahamG | lld:pubmed |
| pubmed-article:19154182 | pubmed:author | pubmed-author:ShimokawaChiz... | lld:pubmed |
| pubmed-article:19154182 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19154182 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:19154182 | pubmed:volume | 419 | lld:pubmed |
| pubmed-article:19154182 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19154182 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19154182 | pubmed:pagination | 339-45 | lld:pubmed |
| pubmed-article:19154182 | pubmed:meshHeading | pubmed-meshheading:19154182... | lld:pubmed |
| pubmed-article:19154182 | pubmed:meshHeading | pubmed-meshheading:19154182... | lld:pubmed |
| pubmed-article:19154182 | pubmed:meshHeading | pubmed-meshheading:19154182... | lld:pubmed |
| pubmed-article:19154182 | pubmed:meshHeading | pubmed-meshheading:19154182... | lld:pubmed |
| pubmed-article:19154182 | pubmed:meshHeading | pubmed-meshheading:19154182... | lld:pubmed |
| pubmed-article:19154182 | pubmed:meshHeading | pubmed-meshheading:19154182... | lld:pubmed |
| pubmed-article:19154182 | pubmed:meshHeading | pubmed-meshheading:19154182... | lld:pubmed |
| pubmed-article:19154182 | pubmed:meshHeading | pubmed-meshheading:19154182... | lld:pubmed |
| pubmed-article:19154182 | pubmed:meshHeading | pubmed-meshheading:19154182... | lld:pubmed |
| pubmed-article:19154182 | pubmed:meshHeading | pubmed-meshheading:19154182... | lld:pubmed |
| pubmed-article:19154182 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19154182 | pubmed:articleTitle | Crystal structure of rat haem oxygenase-1 in complex with ferrous verdohaem: presence of a hydrogen-bond network on the distal side. | lld:pubmed |
| pubmed-article:19154182 | pubmed:affiliation | Department of Medical Biochemistry, Kurume University School of Medicine, 67 Asahi-machi, Kurume 830-0011, Japan. | lld:pubmed |
| pubmed-article:19154182 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19154182 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19154182 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19154182 | lld:pubmed |
