Source:http://linkedlifedata.com/resource/pubmed/id/19647436
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
2009-8-14
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pubmed:abstractText |
Understanding the origin and evolution of haem copper dioxygen reductases (HCO O(2)Red), the terminal enzymes of aerobic respiratory chains, is fundamental to clarify the emergence of this important cellular process. Phylogenetic analyses of HCO O(2)Red have led to contradictory results, suggesting, in turn, that they predate oxygenic photosynthesis and already reduced oxygen as their function; they predate oxygenic photosynthesis, but did not reduce oxygen; they postdate oxygenic photosynthesis. Here, we present a discussion of current data on the distribution and phylogeny of HCO O(2)Red, which leads to a novel and clearer picture of the origin and evolution of these key enzymes as well as their function.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Archaeal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/copper oxidase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0968-0004
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
375-81
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pubmed:meshHeading |
pubmed-meshheading:19647436-Archaeal Proteins,
pubmed-meshheading:19647436-Bacterial Proteins,
pubmed-meshheading:19647436-Evolution, Molecular,
pubmed-meshheading:19647436-Genetic Variation,
pubmed-meshheading:19647436-Heme,
pubmed-meshheading:19647436-Oxidation-Reduction,
pubmed-meshheading:19647436-Oxidoreductases,
pubmed-meshheading:19647436-Oxygen,
pubmed-meshheading:19647436-Phylogeny
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pubmed:year |
2009
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pubmed:articleTitle |
Evolution of the haem copper oxidases superfamily: a rooting tale.
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pubmed:affiliation |
Institut Pasteur, Unité de Biologie Moléculaire chez les Extremophiles, Département de Microbiologie, 28 rue du Dr Roux, 75724 Paris Cedex 15, France. simonetta.gribaldo@pasteur.fr
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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