Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Stella Vitt"'
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
Rnf reversibly reduces NAD+ by ferredoxin coupled with Na+/H+ pumping for microbial ion gradient or reduced ferredoxin formation. Here, a cryo-EM structure provides information about the participating iron and flavin cofactors, the electron transfer
Externí odkaz:
https://doaj.org/article/0a2f0d9666854fc4b13aad9e063d9310
Publikováno v:
Frontiers in Microbiology, Vol 11 (2020)
Some anaerobic bacteria use biotin-dependent Na+-translocating decarboxylases (Bdc) of β-keto acids or their thioester analogs as key enzymes in their energy metabolism. Glutaconyl-CoA decarboxylase (Gcd), a member of this protein family, drives the
Externí odkaz:
https://doaj.org/article/5751821786ec432f85bde657305dd461
Publikováno v:
eLife, Vol 2 (2013)
Methanogenic archaea use a [NiFe]-hydrogenase, Frh, for oxidation/reduction of F420, an important hydride carrier in the methanogenesis pathway from H2 and CO2. Frh accounts for about 1% of the cytoplasmic protein and forms a huge complex consisting
Externí odkaz:
https://doaj.org/article/22294937e4b147abb9ab57dffd3c9c31
Publikováno v:
Frontiers in Microbiology
Frontiers in Microbiology, Vol 11 (2020)
Frontiers in Microbiology, Vol 11 (2020)
Some anaerobic bacteria use biotin-dependent Na+-translocating decarboxylases (Bdc) of β-keto acids or their thioester analogues as key enzymes in their energy metabolism. Glutaconyl-CoA decarboxylase (Gcd), a member of this protein family, drives t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5066203cfd9f14fd9438e9a3e667bbf
http://europepmc.org/articles/PMC7145394
http://europepmc.org/articles/PMC7145394
Autor:
Kesen Ma, Ulrich Ermler, Stella Vitt, Antonio J. Pierik, Eberhard Warkentin, Johanna Moll, Seigo Shima
Publikováno v:
Journal of Molecular Biology. 426:2813-2826
The reversible redox reaction between coenzyme F420 and H2 to F420H2 is catalyzed by an F420-reducing [NiFe]-hydrogenase (FrhABG), which is an enzyme of the energy metabolism of methanogenic archaea. FrhABG is a group 3 [NiFe]-hydrogenase with a dode
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::686dc7c4a96a9f2f35e493fb35e2442b
https://doi.org/10.1016/j.jmb.2014.05.024
https://doi.org/10.1016/j.jmb.2014.05.024
Publikováno v:
Journal of Bacteriology. 193:971-978
Acetobacterium woodii is an acetogenic bacterium that grows by oxidation of various electron donors, such as molecular hydrogen, C1 compounds such as methanol or formate, and sugars (31). Electrons are funneled to carbon dioxide, which is reduced to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33204c225a129e0ff15063b41a620776
https://doi.org/10.1128/jb.01126-10
https://doi.org/10.1128/jb.01126-10
Autor:
Stella, Vitt, Kesen, Ma, Eberhard, Warkentin, Johanna, Moll, Antonio J, Pierik, Seigo, Shima, Ulrich, Ermler
Publikováno v:
Journal of molecular biology. 426(15)
The reversible redox reaction between coenzyme F420 and H2 to F420H2 is catalyzed by an F420-reducing [NiFe]-hydrogenase (FrhABG), which is an enzyme of the energy metabolism of methanogenic archaea. FrhABG is a group 3 [NiFe]-hydrogenase with a dode
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5e81c5c785075566b52833dde80e1f8f
https://pubmed.ncbi.nlm.nih.gov/24887099
https://pubmed.ncbi.nlm.nih.gov/24887099
Publikováno v:
eLife, Vol 2 (2013)
eLife
eLife
Methanogenic archaea use a [NiFe]-hydrogenase, Frh, for oxidation/reduction of F420, an important hydride carrier in the methanogenesis pathway from H2 and CO2. Frh accounts for about 1% of the cytoplasmic protein and forms a huge complex consisting
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c4bd6a93e71a180a785f01226b9507d
https://elifesciences.org/articles/00218
https://elifesciences.org/articles/00218
