Hydrogen metabolism in the hyperthermophilic bacterium Aquifex aeolicus

2005 ◽  
Vol 33 (1) ◽  
pp. 22-24 ◽  
Author(s):  
M. Guiral ◽  
C. Aubert ◽  
M.-T. Giudici-Orticoni
Keyword(s):  
Energy Conservation ◽  
Co2 Fixation ◽  
Cellular Function ◽  
Hydrogen Metabolism ◽  
Aquifex Aeolicus ◽  
Hyperthermophilic Bacterium ◽  
Co2 Fixation Pathway ◽  
Membrane Bound

Aquifex aeolicus is a microaerophilic, hydrogen-oxidizing, hyperthermophilic bacterium containing three [NiFe] hydrogenases. Two of these three enzymes (one membrane-bound and one soluble) have been purified and characterized. The Aquifex hydrogenases are thermostable and tolerant to oxygen. A cellular function for the three hydrogenases has been proposed. The two membrane-bound periplasmic hydrogenases may function in energy conservation, whereas the soluble cytoplasmic hydrogenase is probably involved in the CO2 fixation pathway.

scholarly journals Light-induced reactivation of O2-tolerant membrane-bound [Ni–Fe] hydrogenase from the hyperthermophilic bacterium Aquifex aeolicus under turnover conditions

2013 ◽  
Vol 15 (39) ◽  
pp. 16463 ◽  
Author(s):  
Alexandre Ciaccafava ◽  
Cyrille Hamon ◽  
Pascale Infossi ◽  
Valérie Marchi ◽  
Marie-Thérèse Giudici-Orticoni ◽  
...  
Keyword(s):  
Aquifex Aeolicus ◽  
Hyperthermophilic Bacterium ◽  
Membrane Bound

scholarly journals A new sulfurtransferase from the hyperthermophilic bacterium Aquifex aeolicus

FEBS Journal ◽  
2007 ◽  
Vol 274 (17) ◽  
pp. 4572-4587 ◽  
Author(s):  
Marie-Cécile Giuliani ◽  
Pascale Tron ◽  
Gisèle Leroy ◽  
Corinne Aubert ◽  
Patrick Tauc ◽  
...  
Keyword(s):  
Aquifex Aeolicus ◽  
Hyperthermophilic Bacterium

scholarly journals Minimal and RNA-free RNase P in Aquifex aeolicus

2017 ◽  
Vol 114 (42) ◽  
pp. 11121-11126 ◽  
Author(s):  
Astrid I. Nickel ◽  
Nadine B. Wäber ◽  
Markus Gößringer ◽  
Marcus Lechner ◽  
Uwe Linne ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Rnase P ◽  
Aquifex Aeolicus ◽  
Trna Processing ◽  
Hyperthermophilic Bacterium ◽  
Domains Of Life

RNase P is an essential tRNA-processing enzyme in all domains of life. We identified an unknown type of protein-only RNase P in the hyperthermophilic bacterium Aquifex aeolicus: Without an RNA subunit and the smallest of its kind, the 23-kDa polypeptide comprises a metallonuclease domain only. The protein has RNase P activity in vitro and rescued the growth of Escherichia coli and Saccharomyces cerevisiae strains with inactivations of their more complex and larger endogenous ribonucleoprotein RNase P. Homologs of Aquifex RNase P (HARP) were identified in many Archaea and some Bacteria, of which all Archaea and most Bacteria also encode an RNA-based RNase P; activity of both RNase P forms from the same bacterium or archaeon could be verified in two selected cases. Bioinformatic analyses suggest that A. aeolicus and related Aquificaceae likely acquired HARP by horizontal gene transfer from an archaeon.

Crystal structure of Aquifex aeolicus gene product Aq1627: a putative phosphoglucosamine mutase reveals a unique C-terminal end-to-end disulfide linkage

2017 ◽  
Vol 13 (7) ◽  
pp. 1370-1376
Author(s):  
Upasana Sridharan ◽  
Seiki Kuramitsu ◽  
Shigeyuki Yokoyama ◽  
Thirumananseri Kumarevel ◽  
Karthe Ponnuraj
Keyword(s):  
Crystal Structure ◽  
Gene Product ◽  
Aquifex Aeolicus ◽  
Disulfide Linkage ◽  
Hyperthermophilic Bacterium ◽  
End To End

The crystal structure of Aq1627 protein from Aquifex aeolicus, a hyperthermophilic bacterium has been solved, which reveals a unique end-to-end disulfide linkage.

[NiFe] hydrogenases from the hyperthermophilic bacterium Aquifex aeolicus: properties, function, and phylogenetics

Extremophiles ◽  
2003 ◽  
Vol 7 (2) ◽  
pp. 145-157 ◽  
Author(s):  
Marianne Brugna-Guiral ◽  
Pascale Tron ◽  
Wolfgang Nitschke ◽  
Karl-Otto Stetter ◽  
Benedicte Burlat ◽  
...  
Keyword(s):  
Aquifex Aeolicus ◽  
Hyperthermophilic Bacterium

The structure ofAquifex aeolicusFtsH in the ADP-bound state reveals aC2-symmetric hexamer

2015 ◽  
Vol 71 (6) ◽  
pp. 1307-1318 ◽  
Author(s):  
Marina Vostrukhina ◽  
Alexander Popov ◽  
Elena Brunstein ◽  
Martin A. Lanz ◽  
Renato Baumgartner ◽  
...  
Keyword(s):  
Active Site ◽  
Thermotoga Maritima ◽  
Adenosine Diphosphate ◽  
Crystal Form ◽  
Bound State ◽  
Aquifex Aeolicus ◽  
Protein Activity ◽  
Quadruple Mutant ◽  
Membrane Bound ◽  
Open Issues

The crystal structure of a truncated, soluble quadruple mutant of FtsH fromAquifex aeolicuscomprising the AAA and protease domains has been determined at 2.96 Å resolution in space groupI222. The protein crystallizes as a hexamer, with the protease domain forming layers in theabplane. Contacts between these layers are mediated by the AAA domains. These are highly disordered in one crystal form, but are clearly visible in a related form with a shortercaxis. Here, adenosine diphosphate (ADP) is bound to each subunit and the AAA ring exhibits twofold symmetry. The arrangement is different from the ADP-bound state of an analogously truncated, soluble FtsH construct fromThermotoga maritima. The pore is completely closed and the phenylalanine residues in the pore line a contiguous path. The protease hexamer is very similar to those described for other FtsH structures. To resolve certain open issues regarding a conserved glycine in the linker between the AAA and protease domains, as well as the active-site switch β-strand, mutations have been introduced in the full-length membrane-bound protein. Activity analysis of these point mutants reveals the crucial importance of these residues for proteolytic activity and is in accord with previous interpretation of the active-site switch and the importance of the linker glycine residue.

Characterization of a extreme thermostable fructose-1,6-bisphosphate aldolase from hyperthermophilic bacterium Aquifex aeolicus

2009 ◽  
Vol 45 (4) ◽  
pp. 261-266 ◽  
Author(s):  
Im-Joung La ◽  
Da-Young Eum ◽  
Vinayakumar Gedi ◽  
Jinheung Kim ◽  
Byeongmoon Jeong ◽  
...  
Keyword(s):  
Aquifex Aeolicus ◽  
Hyperthermophilic Bacterium ◽  
Fructose 1,6 Bisphosphate

Characterization of a new periplasmic single-domain rhodanese encoded by a sulfur-regulated gene in a hyperthermophilic bacterium Aquifex aeolicus

Biochimie ◽  
2010 ◽  
Vol 92 (4) ◽  
pp. 388-397 ◽  
Author(s):  
Marie-Cécile Giuliani ◽  
Cécile Jourlin-Castelli ◽  
Gisèle Leroy ◽  
Aderrahman Hachani ◽  
Marie Thérèse Giudici-Orticoni
Keyword(s):  
Single Domain ◽  
Aquifex Aeolicus ◽  
Hyperthermophilic Bacterium

Sulfide:quinone oxidoreductase in membranes of the hyperthermophilic bacterium Aquifex aeolicus (VF5)

2000 ◽  
Vol 173 (4) ◽  
pp. 233-244 ◽  
Author(s):  
Tobias Nübel ◽  
Christof Klughammer ◽  
Robert Huber ◽  
Günter Hauska ◽  
Michael Schütz
Keyword(s):  
Aquifex Aeolicus ◽  
Hyperthermophilic Bacterium ◽  
Sulfide:Quinone Oxidoreductase
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