| pubmed-article:1444257 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1444257 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:1444257 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1444257 | lifeskim:mentions | umls-concept:C0599874 | lld:lifeskim |
| pubmed-article:1444257 | pubmed:dateCreated | 1992-12-14 | lld:pubmed |
| pubmed-article:1444257 | pubmed:abstractText | The degradation of aromatic compounds by aerobic bacteria frequently begins with the dihydroxylation of the substrate by nonheme iron-containing dioxygenases. These enzymes consist of two or three soluble proteins that interact to form an electron-transport chain that transfers electrons from reduced nucleotides (NADH) via flavin and [2Fe-2S] redox centers to a terminal dioxygenase. The dioxygenases may be classified in terms of the number of constituent components and the nature of the redox centers. Class I consists of two-component enzymes in which the first protein is a reductase containing both a flavin and a [2Fe-2S] redox center and the second component is the oxygenase; Class II consists of three-component enzymes in which the flavin and [2Fe-2S] redox centers of the reductase are on a separate flavoprotein and ferredoxin, respectively; and Class III consists of three-component enzymes in which the reductase contains both a flavin and [2Fe-2S] redox center but also requires a second [2Fe-2S] center on a ferredoxin for electron transfer to the terminal oxygenase. Further subdivision is based on the the type of flavin (FMN or FAD) in the reductase, the coordination of the [2Fe-2S] center in the ferredoxin, and the number of terminal oxygenase subunits. From the deduced amino acid sequence of several dioxygenases the ligands involved in the coordination of the nucleotides, iron-sulfur centers, and mononuclear nonheme iron active site are proposed. On the basis of their spectroscopic properties and unusually high redox potentials, the [2Fe-2S] clusters of the ferredoxins and terminal oxygenases have been assigned to the class of Rieske-type iron-sulfur proteins. The iron atoms in the Rieske iron-sulfur cluster are coordinated to the protein by two histidine nitrogens and two cysteine sulfurs. | lld:pubmed |
| pubmed-article:1444257 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1444257 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1444257 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1444257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1444257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1444257 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1444257 | pubmed:issn | 0066-4227 | lld:pubmed |
| pubmed-article:1444257 | pubmed:author | pubmed-author:CammackRR | lld:pubmed |
| pubmed-article:1444257 | pubmed:author | pubmed-author:MasonJ RJR | lld:pubmed |
| pubmed-article:1444257 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1444257 | pubmed:volume | 46 | lld:pubmed |
| pubmed-article:1444257 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1444257 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1444257 | pubmed:pagination | 277-305 | lld:pubmed |
| pubmed-article:1444257 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1444257 | pubmed:meshHeading | pubmed-meshheading:1444257-... | lld:pubmed |
| pubmed-article:1444257 | pubmed:meshHeading | pubmed-meshheading:1444257-... | lld:pubmed |
| pubmed-article:1444257 | pubmed:meshHeading | pubmed-meshheading:1444257-... | lld:pubmed |
| pubmed-article:1444257 | pubmed:meshHeading | pubmed-meshheading:1444257-... | lld:pubmed |
| pubmed-article:1444257 | pubmed:meshHeading | pubmed-meshheading:1444257-... | lld:pubmed |
| pubmed-article:1444257 | pubmed:meshHeading | pubmed-meshheading:1444257-... | lld:pubmed |
| pubmed-article:1444257 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1444257 | pubmed:articleTitle | The electron-transport proteins of hydroxylating bacterial dioxygenases. | lld:pubmed |
| pubmed-article:1444257 | pubmed:affiliation | Division of Biosphere Sciences, King's College London, United Kingdom. | lld:pubmed |
| pubmed-article:1444257 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1444257 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:1444257 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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