Could a diiron-containing four-helix-bundle protein have been a primitive oxygen reductase?

Citation
Cm. Gomes et al., Could a diiron-containing four-helix-bundle protein have been a primitive oxygen reductase?, CHEMBIOCHEM, 2(7-8), 2001, pp. 583
Citations number
28
Categorie Soggetti
Chemistry & Analysis
Journal title
CHEMBIOCHEM
ISSN journal
14394227 → ACNP
Volume
2
Issue
7-8
Year of publication
2001
Database
ISI
SICI code
1439-4227(20010803)2:7-8<583:CADFPH>2.0.ZU;2-S
Abstract
To fulfil the title hypothesis, such a protein would have to harbour a binu clear transition metal site that would allow the complete reduction of diox ygen to water, thus playing an important role in early oxygen defence mecha nisms in primordial anaerobes. The hypothesis here raised is based on data concerning the oxygen reductase activity of the four-helix diiron protein r ubrerythrin (see schematic picture), and on sequence- and structure-based p hylogenetic relations between this and other diiron proteins. Interestingly , an evolutionary relationship between such an early system and the alterna tive oxidases present in extant eukaryotes can be depicted.