scholarly journals Genomic and cDNA Sequence Tags of the Hyperthermophilic Archaeon Pyrobaculum Aerophilum

1996 ◽  
Vol 24 (22) ◽  
pp. 4373-4378 ◽  
Author(s):  
P. Volkl ◽  
P. Markiewicz ◽  
C. Baikalov ◽  
S. Fitz-Gibbon ◽  
K. O. Stetter ◽  
...  
Keyword(s):  
Cdna Sequence ◽  
Pyrobaculum Aerophilum ◽  
Hyperthermophilic Archaeon

A fosmid-based genomic map and identification of 474 genes of the hyperthermophilic archaeon Pyrobaculum aerophilum

Extremophiles ◽  
1997 ◽  
Vol 1 (1) ◽  
pp. 36-52 ◽  
Author(s):  
Sorel Fitz-Gibbon ◽  
Anthony J. Choi ◽  
Jeffrey H. Miller ◽  
Karl O. Stetter ◽  
Melvin I. Simon ◽  
...  
Keyword(s):  
Pyrobaculum Aerophilum ◽  
Hyperthermophilic Archaeon ◽  
Genomic Map

Catalytic properties and crystal structure of quinoprotein aldose sugar dehydrogenase from hyperthermophilic archaeon Pyrobaculum aerophilum

2010 ◽  
Vol 502 (2) ◽  
pp. 81-88 ◽  
Author(s):  
Haruhiko Sakuraba ◽  
Kaori Yokono ◽  
Kazunari Yoneda ◽  
Akira Watanabe ◽  
Yasuhiko Asada ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Properties ◽  
Pyrobaculum Aerophilum ◽  
Hyperthermophilic Archaeon

scholarly journals 1P045 Crystal structure of 2-Deoxyribose-5-PhosphateAldolase from hyperthermophilic archaeon Pyrobaculum aerophilum

2005 ◽  
Vol 45 (supplement) ◽  
pp. S43
Author(s):  
K. Yoneda ◽  
K. Yoshihara ◽  
H. Sakuraba ◽  
H. Tsuge ◽  
N. Katunuma ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Pyrobaculum Aerophilum ◽  
Hyperthermophilic Archaeon

Construction of a biocathode using the multicopper oxidase from the hyperthermophilic archaeon, Pyrobaculum aerophilum: towards a long-life biobattery

2015 ◽  
Vol 37 (7) ◽  
pp. 1399-1404 ◽  
Author(s):  
Hiroaki Sakamoto ◽  
Toshiki Uchii ◽  
Kayo Yamaguchi ◽  
Ayako Koto ◽  
Ei-ichiro Takamura ◽  
...  
Keyword(s):  
Multicopper Oxidase ◽  
Pyrobaculum Aerophilum ◽  
Hyperthermophilic Archaeon ◽  
Long Life

scholarly journals Properties of a Thermostable Nitrate Reductase from the Hyperthermophilic Archaeon Pyrobaculum aerophilum

2001 ◽  
Vol 183 (19) ◽  
pp. 5491-5495 ◽  
Author(s):  
Sepideh Afshar ◽  
Eric Johnson ◽  
Simon de Vries ◽  
Imke Schröder
Keyword(s):  
Nitrate Reductase ◽  
Specific Activity ◽  
Reductase Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
High Specific Activity ◽  
Competitive Inhibitor ◽  
Pyrobaculum Aerophilum ◽  
Benzyl Viologen ◽  
Hyperthermophilic Archaeon

ABSTRACT The nitrate reductase of the hyperthermophilic archaeonPyrobaculum aerophilum was purified 137-fold from the cytoplasmic membrane. Based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, the enzyme complex consists of three subunits with apparent molecular weights of 130,000, 52,000, and 32,000. The enzyme contained molybdenum (0.8-mol/mol complex), iron (15.4-mol/mol complex) and cytochrome b (0.49-mol/mol complex) as cofactors. The P. aerophilum nitrate reductase distinguishes itself from nitrate reductases of mesophilic bacteria and archaea by its very high specific activity using reduced benzyl viologen as the electron donor (V max with nitrate, 1,162 s−1 (326 U/mg);V max with chlorate, 1,348 s−1 (378 U/mg) [assayed at 75°C]). The Km values for nitrate and chlorate were 58 and 140 μM, respectively. Azide was a competitive inhibitor and cyanide was a noncompetitive inhibitor of the nitrate reductase activity. The temperature optimum for activity was >95°C. When incubated at 100°C, the purified nitrate reductase had a half-life of 1.5 h. This study constitutes the first description of a nitrate reductase from a hyperthermophilic archaeon.

Unique active site formation in a novel galactose 1‐phosphate uridylyltransferase from the hyperthermophilic archaeon Pyrobaculum aerophilum

2020 ◽  
Vol 88 (5) ◽  
pp. 669-678 ◽  
Author(s):  
Tatsuya Ohshida ◽  
Junji Hayashi ◽  
Kazunari Yoneda ◽  
Toshihisa Ohshima ◽  
Haruhiko Sakuraba
Keyword(s):  
Active Site ◽  
Site Formation ◽  
Pyrobaculum Aerophilum ◽  
Hyperthermophilic Archaeon

scholarly journals Effect of Tungstate on Nitrate Reduction by the Hyperthermophilic Archaeon Pyrobaculum aerophilum

1998 ◽  
Vol 64 (8) ◽  
pp. 3004-3008 ◽  
Author(s):  
Sepideh Afshar ◽  
Christopher Kim ◽  
Harold G. Monbouquette ◽  
Imke Schröder
Keyword(s):  
Nitric Oxide ◽  
Nitrate Reductase ◽  
Culture Medium ◽  
Specific Activity ◽  
Molecular Nitrogen ◽  
High Specific Activity ◽  
Anaerobic Growth ◽  
Pyrobaculum Aerophilum ◽  
Hyperthermophilic Archaeon ◽  
Thermophilic Archaeon

ABSTRACT Pyrobaculum aerophilum, a hyperthermophilic archaeon, can respire either with low amounts of oxygen or anaerobically with nitrate as the electron acceptor. Under anaerobic growth conditions, nitrate is reduced via the denitrification pathway to molecular nitrogen. This study demonstrates that P. aerophilumrequires the metal oxyanion WO4 2− for its anaerobic growth on yeast extract, peptone, and nitrate as carbon and energy sources. The addition of 1 μM MoO4 2−did not replace WO4 2− for the growth ofP. aerophilum. However, cell growth was completely inhibited by the addition of 100 μM MoO4 2−to the culture medium. At lower tungstate concentrations (0.3 μM and less), nitrite was accumulated in the culture medium. The accumulation of nitrite was abolished at higher WO4 2−concentrations (<0.7 μM). High-temperature enzyme assays for the nitrate, nitrite, and nitric oxide reductases were performed. The majority of all three denitrification pathway enzyme activities was localized to the cytoplasmic membrane, suggesting their involvement in the energy metabolism of the cell. While nitrite and nitric oxide specific activities were relatively constant at different tungstate concentrations, the activity of nitrate reductase was decreased fourfold at WO4 2− levels of 0.7 μM or higher. The high specific activity of the nitrate reductase enzyme observed at low WO4 2− levels (0.3 μM or less) coincided with the accumulation of nitrite in the culture medium. This study documents the first example of the effect of tungstate on the denitrification process of an extremely thermophilic archaeon. We demonstrate here that nitrate reductase synthesis inP. aerophilum occurs in the presence of high concentrations of tungstate.

Alcohol dehydrogenase from the hyperthermophilic archaeon Pyrobaculum aerophilum: Stability at high temperature

2012 ◽  
Vol 525 (1) ◽  
pp. 40-46 ◽  
Author(s):  
Alessio Ausili ◽  
Annalisa Vitale ◽  
Tullio Labella ◽  
Francesco Rosso ◽  
Alfonso Barbarisi ◽  
...  
Keyword(s):  
High Temperature ◽  
Alcohol Dehydrogenase ◽  
Pyrobaculum Aerophilum ◽  
Hyperthermophilic Archaeon
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