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Could a Diiron‐Containing Four‐Helix‐Bundle Protein Have Been a Primitive Oxygen Reductase?
Author(s) -
Gomes Cláudio M.,
Le Gall Jean,
Xavier António V.,
Teixeira Miguel
Publication year - 2001
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20010803)2:7/8<583::aid-cbic583>3.0.co;2-5
Subject(s) - extant taxon , phylogenetic tree , biology , sequence (biology) , schematic , reductase , helix (gastropod) , evolutionary biology , enzyme , chemistry , biochemistry , ecology , gene , electronic engineering , engineering , snail
To fulfil the title hypothesis , such a protein would have to harbour a binuclear transition metal site that would allow the complete reduction of dioxygen to water, thus playing an important role in early oxygen defence mechanisms in primordial anaerobes. The hypothesis here raised is based on data concerning the oxygen reductase activity of the four‐helix diiron protein rubrerythrin (see schematic picture), and on sequence‐ and structure‐based phylogenetic relations between this and other diiron proteins. Interestingly, an evolutionary relationship between such an early system and the alternative oxidases present in extant eukaryotes can be depicted.