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| pubmed-article:9095195 | lifeskim:mentions | umls-concept:C0004611 | lld:lifeskim |
| pubmed-article:9095195 | lifeskim:mentions | umls-concept:C0995425 | lld:lifeskim |
| pubmed-article:9095195 | lifeskim:mentions | umls-concept:C1324275 | lld:lifeskim |
| pubmed-article:9095195 | lifeskim:mentions | umls-concept:C0063148 | lld:lifeskim |
| pubmed-article:9095195 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9095195 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9095195 | pubmed:dateCreated | 1997-4-30 | lld:pubmed |
| pubmed-article:9095195 | pubmed:abstractText | The 2.8 A crystal structure of hydroxylamine oxidoreductase of a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea, is described. Twenty-four haems lie in the centre bottom of the trimeric molecule, localized in four clusters within each monomer. The haem clusters within the trimer are aligned to form a ring that has inlet and outlet sites. The inlet is occupied by a novel haem, P460, and there are two possible outlet sites per monomer formed by paired haems lying within a cavity or cleft on the protein surface. The structure suggests pathways by which electron transfer may occur through the precisely arranged haems and provides a framework for the interpretation of previous and future biochemical and genetic observations. | lld:pubmed |
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| pubmed-article:9095195 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9095195 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9095195 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9095195 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9095195 | pubmed:issn | 1072-8368 | lld:pubmed |
| pubmed-article:9095195 | pubmed:author | pubmed-author:TanakaNN | lld:pubmed |
| pubmed-article:9095195 | pubmed:author | pubmed-author:FujiwaraTT | lld:pubmed |
| pubmed-article:9095195 | pubmed:author | pubmed-author:MoriyamaHH | lld:pubmed |
| pubmed-article:9095195 | pubmed:author | pubmed-author:IgarashiNN | lld:pubmed |
| pubmed-article:9095195 | pubmed:author | pubmed-author:FukumoriYY | lld:pubmed |
| pubmed-article:9095195 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9095195 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:9095195 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9095195 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9095195 | pubmed:pagination | 276-84 | lld:pubmed |
| pubmed-article:9095195 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9095195 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9095195 | pubmed:articleTitle | The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea. | lld:pubmed |
| pubmed-article:9095195 | pubmed:affiliation | Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan. | lld:pubmed |
| pubmed-article:9095195 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9095195 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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