Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Microbiology 155 (2009), 3015-3020; DOI  10.1099/mic.0.030320-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
mic.0.030320-0v1
155/9/3015    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Google Scholar
Right arrow Articles by van Vugt-Lussenburg, B. M. A.
Right arrow Articles by Hagedoorn, P.-L.
PubMed
Right arrow PubMed Citation
Right arrow Articles by van Vugt-Lussenburg, B. M. A.
Right arrow Articles by Hagedoorn, P.-L.
Agricola
Right arrow Articles by van Vugt-Lussenburg, B. M. A.
Right arrow Articles by Hagedoorn, P.-L.
Microbiology 155 (2009), 3015-3020; DOI  10.1099/mic.0.030320-0
© 2009 Society for General Microbiology

Identification of two [4Fe–4S]-cluster-containing hydro-lyases from Pyrococcus furiosus

Barbara M. A. van Vugt-Lussenburg, Laura van der Weel, Wilfred R. Hagen and Peter-Leon Hagedoorn

Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands

The hyperthermophilic archaeon Pyrococcus furiosus is a strict anaerobe. It is therefore not expected to use the oxidative tricarboxylic acid (TCA) cycle for energy transduction. Nonetheless, its genome encodes more putative TCA cycle enzymes than the closely related Pyrococcus horikoshii and Pyrococcus abyssi, including an aconitase (PF0201). Furthermore, a two-subunit fumarase (PF1755 and PF1754) is encoded on the Pyr. furiosus genome. In the present study, these three genes were heterologously overexpressed in Escherichia coli to enable characterization of the enzymes. PF1755 and PF1754 were shown to form a [4Fe–4S]-cluster-containing heterodimeric enzyme, able to catalyse the reversible hydratation of fumarate. The aconitase PF0201 also contained an Fe–S cluster, and catalysed the conversion from citrate to isocitrate. The fumarase belongs to the class of two-subunit, [4Fe–4S]-cluster-containing fumarate hydratases exemplified by MmcBC from Pelotomaculum thermopropionicum; the aconitase belongs to the aconitase A family. Aconitase probably plays a role in amino acid synthesis when the organism grows on carbohydrates. However, the function of the seemingly metabolically isolated fumarase in Pyr. furiosus has yet to be established.

Correspondence
Peter-Leon Hagedoorn
p.l.hagedoorn{at}tudelft.nl

Abbreviations: FumA, fumarase A; FumB, fumarase B; TCA, tricarboxylic acid






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2009 Society for General Microbiology.