Could a Diiron-Containing Four-Helix-Bundle Protein Have Been a Primitive Oxygen Reductase?

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...

Full description

Saved in:
Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2001-08, Vol.2 (7-8), p.583-587
Main Authors: Gomes, Cláudio M., Le Gall, Jean, Xavier, António V., Teixeira, Miguel
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Evolution, Molecular
Ferredoxins - chemistry
Ferredoxins - genetics
Hemerythrin
iron
Iron - chemistry
metalloenzymes
Metalloproteins - chemistry
Metalloproteins - genetics
molecular evolution
Molecular Sequence Data
oxidoreductases
Oxidoreductases - chemistry
Oxidoreductases - genetics
oxygen
Oxygen - chemistry
Protein Conformation
Rubredoxins
Sequence Alignment
Sequence Homology, Amino Acid
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1439-4227
1439-7633
DOI:10.1002/1439-7633(20010803)2:7/8<583::AID-CBIC583>3.0.CO;2-5