Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O

Autor: Rudolf K. Thauer, Ulrich Ermler, Christoph H. Hagemeier, Eberhard Warkentin, Henning Seedorf, Seigo Shima

Publikováno v: FEBS Journal. 274:1588-1599

The di-iron flavoprotein F(420)H(2) oxidase found in methanogenic Archaea catalyzes the four-electron reduction of O(2) to 2H(2)O with 2 mol of reduced coenzyme F(420)(7,8-dimethyl-8-hydroxy-5-deazariboflavin). We report here on crystal structures of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b31ade42e7b838697c0f3b28e67bd3f5
https://doi.org/10.1111/j.1742-4658.2007.05706.x

The structure of F420-dependent methylenetetrahydromethanopterin dehydrogenase: a crystallographic 'superstructure' of the selenomethionine-labelled protein crystal structure

Autor: Rudolf K. Thauer, Eberhard Warkentin, Ulrich Ermler, Seigo Shima, Christoph H. Hagemeier

Publikováno v: Acta Crystallographica Section D Biological Crystallography. 61:198-202

The diffraction pattern of native protein crystals of F(420)-dependent methylenetetrahydromethanopterin dehydrogenase from Methanopyrus kandleri shows weak additional reflections compared with the selenomethionine-labelled protein crystals, indicatin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::113e49d5053be781ee0c38be381c8f76
https://doi.org/10.1107/s0907444904030732

Structure of Methylene-Tetrahydromethanopterin Dehydrogenase from Methylobacterium extorquens AM1

Autor: Christoph H. Hagemeier, Eberhard Warkentin, Annette Roth, Ulrike Demmer, Julia A. Vorholt, Wolfgang Grabarse, Ulrich Ermler

Publikováno v: Structure. 10:1127-1137

NADP-dependent methylene-H 4 MPT dehydrogenase, MtdA, from Methylobacterium extorquens AM1 catalyzes the dehydrogenation of methylene-tetrahydromethanopterin and methylene-tetrahydrofolate with NADP + as cosubstrate. The X-ray structure of MtdA with

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed9c6ad25e605ef05d00003adcc525b1
https://doi.org/10.1016/s0969-2126(02)00802-x

Characterization of a second methylene tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1

Autor: Mary E. Lidstrom, Ludmila Chistoserdova, Rudolf K. Thauer, Julia A. Vorholt, Christoph H. Hagemeier

Publikováno v: European Journal of Biochemistry. 267:3762-3769

Cell extracts of Methylobacterium extorquens AM1 were recently found to catalyze the dehydrogenation of methylene tetrahydromethanopterin (methylene H4MPT) with NAD+ and NADP+. The purification of a 32-kDa NADP-specific methylene H4MPT dehydrogenase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::347f47110d87ccf65401753e61c5f29b
https://doi.org/10.1046/j.1432-1327.2000.01413.x

The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features

Autor: Holger Brüggemann, Rudolf K. Thauer, Henning Seedorf, Birgit Veith, Fu-Li Li, Axel Strittmatter, W. Florian Fricke, Marcus Miethke, Christoph H. Hagemeier, Heiko Liesegang, Wolfgang Buckel, Julia Hinderberger, Gerhard Gottschalk

Publikováno v: Seedorf, H, Fricke, W F, Veith, B, Brüggemann, H, Liesegang, H, Strittmatter, A, Miethke, M, Buckel, W, Hinderberger, J, Li, F, Hagemeier, C, Thauer, R K & Gottschalk, G 2008, ' The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features ' Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 6, pp. 2128-33 . https://doi.org/10.1073/pnas.0711093105

Clostridium kluyveriis unique among the clostridia; it grows anaerobically on ethanol and acetate as sole energy sources. Fermentation products are butyrate, caproate, and H2. We report here the genome sequence ofC. kluyveri, which revealed new insig

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfd54be157ff3fb5332e8eef744a3ff5
https://europepmc.org/articles/PMC2542871/