| pubmed-article:19032091 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19032091 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:19032091 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:19032091 | lifeskim:mentions | umls-concept:C2919017 | lld:lifeskim |
| pubmed-article:19032091 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:19032091 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:19032091 | pubmed:dateCreated | 2008-11-26 | lld:pubmed |
| pubmed-article:19032091 | pubmed:abstractText | Hemoproteins carry out diverse functions utilizing a wide range of chemical reactivity while employing the same heme prosthetic group. It is clear from high-resolution crystal structures and biochemical studies that protein-bound hemes are not planar and adopt diverse conformations. The crystal structure of an H-NOX domain from Thermoanaerobacter tengcongensis (Tt H-NOX) contains the most distorted heme reported to date. In this study, Tt H-NOX was engineered to adopt a flatter heme by mutating proline 115, a conserved residue in the H-NOX family, to alanine. Decreasing heme distortion in Tt H-NOX increases affinity for oxygen and decreases the reduction potential of the heme iron. Additionally, flattening the heme is associated with significant shifts in the N-terminus of the protein. These results show a clear link between the heme conformation and Tt H-NOX structure and demonstrate that heme distortion is an important determinant for maintaining biochemical properties in H-NOX proteins. | lld:pubmed |
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| pubmed-article:19032091 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19032091 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19032091 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19032091 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:19032091 | pubmed:issn | 1554-8937 | lld:pubmed |
| pubmed-article:19032091 | pubmed:author | pubmed-author:PellicenaPatr... | lld:pubmed |
| pubmed-article:19032091 | pubmed:author | pubmed-author:KuriyanJohnJ | lld:pubmed |
| pubmed-article:19032091 | pubmed:author | pubmed-author:BoonElizabeth... | lld:pubmed |
| pubmed-article:19032091 | pubmed:author | pubmed-author:MarlettaMicha... | lld:pubmed |
| pubmed-article:19032091 | pubmed:author | pubmed-author:OleaCharlesC | lld:pubmed |
| pubmed-article:19032091 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19032091 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:19032091 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:19032091 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19032091 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19032091 | pubmed:pagination | 703-10 | lld:pubmed |
| pubmed-article:19032091 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:19032091 | pubmed:meshHeading | pubmed-meshheading:19032091... | lld:pubmed |
| pubmed-article:19032091 | pubmed:meshHeading | pubmed-meshheading:19032091... | lld:pubmed |
| pubmed-article:19032091 | pubmed:meshHeading | pubmed-meshheading:19032091... | lld:pubmed |
| pubmed-article:19032091 | pubmed:meshHeading | pubmed-meshheading:19032091... | lld:pubmed |
| pubmed-article:19032091 | pubmed:meshHeading | pubmed-meshheading:19032091... | lld:pubmed |
| pubmed-article:19032091 | pubmed:meshHeading | pubmed-meshheading:19032091... | lld:pubmed |
| pubmed-article:19032091 | pubmed:meshHeading | pubmed-meshheading:19032091... | lld:pubmed |
| pubmed-article:19032091 | pubmed:meshHeading | pubmed-meshheading:19032091... | lld:pubmed |
| pubmed-article:19032091 | pubmed:meshHeading | pubmed-meshheading:19032091... | lld:pubmed |
| pubmed-article:19032091 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:19032091 | pubmed:articleTitle | Probing the function of heme distortion in the H-NOX family. | lld:pubmed |
| pubmed-article:19032091 | pubmed:affiliation | Department of Molecular and Cell Biology, California Institute for Quantitative Biosciences, University of California, Berkeley, California 94720, USA. | lld:pubmed |
| pubmed-article:19032091 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19032091 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19032091 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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