Prokaryotic origins for the mitochondrial alternative oxidase and plastid terminal oxidase nuclear genes

Patrick Finnegan, A.L. Umbach, J.A. Wilce

    Research output: Contribution to journalArticle

    32 Citations (Scopus)

    Abstract

    The mitochondrial alternative oxidase is a diiron carboxylate quinol oxidase (Dox) found in plants and some fungi and protists, but not animals. The plastid terminal oxidase is distantly related to alternative oxidase and is most likely also a Dox protein. Database searches revealed that the alpha-proteobacterium Novosphingobium aromaticivorans and the cyanobacteria Nostoc sp. PCC7120, Synechococcus sp. WH8102 and Prochlorococcus marinus subsp. pastoris CCMP1378 each possess a Dox homolog. Each prokaryotic protein conforms to the current structural models of the Dox active site and phylogenetic analyses suggest that the eukaryotic Dox genes arose from an ancestral prokaryotic gene. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
    Original languageEnglish
    Pages (from-to)425-430
    JournalFEBS Letters
    Volume555
    Issue number3
    DOIs
    Publication statusPublished - 2003

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