Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Sulfhydrogenase"'
Autor:
Guanghua Wang, Yuanjin Li, Jianfeng Liu, Biao Chen, Hongfei Su, Jiayuan Liang, Wen Huang, Kefu Yu
Publikováno v:
Frontiers in Microbiology, Vol 13 (2022)
Members of the phylum Acidobacteria are ubiquitous in various environments. Soil acidobacteria have been reported to present a variety of strategies for their success in terrestrial environments. However, owing to lack of pure culture, information on
Externí odkaz:
https://doaj.org/article/5020dd04149c401a8803cb99aa9e8dd9
Akademický článek
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Autor:
T. B. K. Reddy, Hans-Peter Klenk, Ilya V. Kublanov, Chris Daum, Mikhail S. Gelfand, Christian Rinke, Oleg N. Reva, Stefan Spring, Olga M. Sigalova, Natalia Ivanova, Nikos C. Kyrpides, Markus Göker, Elizaveta A. Bonch-Osmolovskaya, Nikolai A. Chernyh, Alexander V. Lebedinsky, Margarita L. Miroshnichenko, Sergey N. Gavrilov, Olga L. Kovaleva, Tanja Woyke
Publikováno v:
Frontiers in Microbiology
Kublanov, IV; Sigalova, OM; Gavrilov, SN; Lebedinsky, AV; Rinke, C; Kovaleva, O; et al.(2017). Genomic analysis of Caldithrix abyssi, the thermophilic anaerobic bacterium of the novel bacterial phylum Calditrichaeota. Frontiers in Microbiology, 8(FEB). doi: 10.3389/fmicb.2017.00195. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/3f41m67w
Frontiers in microbiology, vol 8, iss FEB
Kublanov, IV; Sigalova, OM; Gavrilov, SN; Lebedinsky, AV; Rinke, C; Kovaleva, O; et al.(2017). Genomic analysis of Caldithrix abyssi, the thermophilic anaerobic bacterium of the novel bacterial phylum Calditrichaeota. Frontiers in Microbiology, 8(FEB). doi: 10.3389/fmicb.2017.00195. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/3f41m67w
Frontiers in microbiology, vol 8, iss FEB
© 2017 Kublanov, Sigalova, Gavrilov, Lebedinsky, Rinke, Kovaleva, Chernyh, Ivanova, Daum, Reddy, Klenk, Spring, Göker, Reva, Miroshnichenko, Kyrpides, Woyke, Gelfand, Bonch-Osmolovskaya. The genome of Caldithrix abyssi, the first cultivated represe
Autor:
Eric N. Kaufman, Charlene A. Woodward
Publikováno v:
Biotechnology and Bioengineering. 52:423-428
Naturally occurring enzymes may be modified by covalently attaching hydrophobic groups that render the enzyme soluble and active in organic solvents, and have the potential to greatly expand applications of enzymatic catalysis. The reduction of eleme
Autor:
Elisabetta Franchi, Claudio Tosi, U Barberini, A Selvaggi, Francesco Rodriguez, Paola Maria Pedroni
Publikováno v:
Journal of Photochemistry and Photobiology A: Chemistry. 125:107-112
The [NiFe] sulfhydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus has been tested as a biological catalyst in a light-driven in vitro hydrogen evolution system, using a solar simulator apparatus as a source of light. The enzyme is ac
Publikováno v:
FEMS Microbiology Letters. 122:245-250
The archaeon Pyrococcus furiosus grows optimally at 100°C during the fermentation of peptides and carbohydrates to yield organic acids, CO2 and H2. It also reduces elemental sulfur (S°) to H2S. The production of H2 is catalyzed by a Ni-containing h
Publikováno v:
Scopus-Elsevier
Microorganisms growing near and above 100 degrees C have recently been discovered near shallow and deep sea hydrothermal vents. Most are obligately dependent upon the reduction of elemental sulfur (S0) to hydrogen sulfide (H2S) for optimal growth, ev
Publikováno v:
Journal of bacteriology. 182(7)
The fermentative hyperthermophile Pyrococcus furiosus contains an NADPH-utilizing, heterotetrameric (αβγδ), cytoplasmic hydrogenase (hydrogenase I) that catalyzes both H 2 production and the reduction of elemental sulfur to H 2 S. Herein is descr
Publikováno v:
Journal of Biological Inorganic Chemistry, 4, 284-291
Journal of Biological Inorganic Chemistry 4 (1999)
Journal of Biological Inorganic Chemistry 4 (1999)
The sulfhydrogenase complex of Pyrococcus furiosus is an alpha beta gamma delta heterotetramer with both hydrogenase activity (borne by the alpha delta subunits) and sulfur reductase activity (carried by the beta gamma subunits). The beta-subunit con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::319b338fff55e7d3ed567189f515b663
https://research.wur.nl/en/publications/on-the-prosthetic-groups-of-the-nife-sulfhydrogenase-from-pyrococ
https://research.wur.nl/en/publications/on-the-prosthetic-groups-of-the-nife-sulfhydrogenase-from-pyrococ
Publikováno v:
FEBS Letters 368 (1995)
FEBS Letters, 368, 117-121
FEBS Letters, 368, 117-121
The sulfhydrogenase from the extreme thermophile Pyrococcus furiosus has been re-investigated. The αβγδ heterotetrameric enzyme of 153.3 kDa was found to contain 17 Fe, 17 S2−, and 0.74 Ni. The specific activity of the purified protein was 80 U
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1724f7091d8c0b8ffd78f41a5007d16
https://research.wur.nl/en/publications/redox-properties-of-the-sulfhydrogenase-from-pyrococcus-furiosus
https://research.wur.nl/en/publications/redox-properties-of-the-sulfhydrogenase-from-pyrococcus-furiosus