Zobrazeno 1 - 10
of 10
pro vyhledávání: '"José Vazquez Ramos"'
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 9 (2022)
Microbial resource mining of electroactive microorganism (EAM) is currently methodically hampered due to unavailable electrochemical screening tools. Here, we introduce an electrochemical microwell plate (ec-MP) composed of a 96 electrochemical deepw
Externí odkaz:
https://doaj.org/article/7c41134a172e4476b34cb6aa03fecd66
Autor:
Ronny Frank, José Vazquez Ramos, Ronny Azendorf, Christoph Prönnecke, Sabine Schmidt, Heinz-Georg Jahnke, Andrea A. Robitzki
Publikováno v:
Sensors and Actuators B: Chemical. 361:131752
Autor:
Dieter Jahn, Christian Trncik, Gunhild Layer, Jan Jasper, Jürgen Moser, Oliver Einsle, José Vazquez Ramos
Publikováno v:
Chembiochem
The engineering of transgenic organisms with the ability to fix nitrogen is an attractive possibility. However, oxygen sensitivity of nitrogenase, mainly conferred by the reductase component (NifH)2, is an imminent problem. Nitrogenase‐like enzymes
Autor:
Melanie Kühner, José Vazquez Ramos, Martin Hoffmann, Gunhild Layer, Peter Schweyen, Martin Bröring, Edward J. Reijerse, Wolfgang Lubitz
Publikováno v:
Chemical Science. 7:4633-4643
The heme synthase AhbD catalyzes the oxidative decarboxylation of two propionate side chains of iron-coproporphyrin III to the corresponding vinyl groups of heme during the alternative heme biosynthesis pathway occurring in sulfate-reducing bacteria
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1876
Nitrogenase-like enzymes play a vital role in the reduction of the conjugated ring systems of diverse tetrapyrrole molecules. The biosynthesis of all bacteriochlorophylls involves the two-electron reduction of the C7-C8 double bond of the green pigme
Publikováno v:
Methods in Molecular Biology ISBN: 9781493988631
Nitrogenase-like enzymes play a vital role in the reduction of the conjugated ring systems of diverse tetrapyrrole molecules. The biosynthesis of all bacteriochlorophylls involves the two-electron reduction of the C7-C8 double bond of the green pigme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36bbf1f41bef947c439de09f8cd94139
https://doi.org/10.1007/978-1-4939-8864-8_8
https://doi.org/10.1007/978-1-4939-8864-8_8
Autor:
Simon J, Moore, Sven T, Sowa, Christopher, Schuchardt, Evelyne, Deery, Andrew D, Lawrence, José Vazquez, Ramos, Susan, Billig, Claudia, Birkemeyer, Peter T, Chivers, Mark J, Howard, Stephen E J, Rigby, Gunhild, Layer, Martin J, Warren
Publikováno v:
Nature
Summary Methane biogenesis in methanogens is mediated by methyl-coenzyme M reductase, an enzyme that is also responsible for the utilisation of methane through anaerobic methane oxidation. The enzyme employs an ancillary factor called coenzyme F430,
Autor:
Simon J, Moore, Sven T, Sowa, Christopher, Schuchardt, Evelyne, Deery, Andrew D, Lawrence, José Vazquez, Ramos, Susan, Billig, Claudia, Birkemeyer, Peter T, Chivers, Mark J, Howard, Stephen E J, Rigby, Gunhild, Layer, Martin J, Warren
Publikováno v:
Nature. 543(7643)
Methane biogenesis in methanogens is mediated by methyl-coenzyme M reductase, an enzyme that is also responsible for the utilization of methane through anaerobic methane oxidation. The enzyme uses an ancillary factor called coenzyme F
Autor:
Evelyne Deery, Susan Billig, Claudia Birkemeyer, Martin J. Warren, Stephen E. J. Rigby, Peter T. Chivers, Andy Lawrence, Sven T. Sowa, Gunhild Layer, José Vazquez Ramos, Simon J. Moore, Mark J. Howard, Christopher Schuchardt
Publikováno v:
Nature. 545:116-116
Nature 543, 78–82 (2017); doi:10.1038/nature21427 In this Article, we omitted to cite a relevant paper1 on coenzyme F430 biosynthesis, which identified the genes that encode the enzymes required for the transformation of sirohydrochlorin into coenz
Publikováno v:
Nucleic Acids Research
We describe the construction and application of elements for random insertion of promoter containing DNA into the genome of Bacillus subtilis. The outward-facing promoter of these integrative elements termed InsTet(G+) is inducible by tetracycline so