Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Marta Albareda"'
Autor:
Marta Ballesteros-Gutiérrez, Marta Albareda, Coral Barbas, Ángeles López-Gonzálvez, Michael F. Dunn, José M. Palacios
Publikováno v:
Frontiers in Microbiology, Vol 14 (2023)
Rhizobium leguminosarum bv. viciae (Rlv) UPM791 effectively nodulates pea and lentil, but bacteroids contain a number of proteins differentially expressed depending on the host. One of these host-dependent proteins (C189) is similar to a diaminobutyr
Externí odkaz:
https://doaj.org/article/96f289fba7984a4ca8b450b607279944
The plant pathogen Pectobacterium atrosepticum contains a functional formate hydrogenlyase‐2 complex
Autor:
Frank Sargent, Marta Albareda, Alexander J. Finney, Sarah J. Coulthurst, Michal Fleszar, Rebecca Lowden
Publikováno v:
Molecular Microbiology
Summary Pectobacterium atrosepticum SCRI1043 is a phytopathogenic Gram‐negative enterobacterium. Genomic analysis has identified that genes required for both respiration and fermentation are expressed under anaerobic conditions. One set of anaerobi
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1860:325-340
Biological production and oxidation of hydrogen is mediated by hydrogenases, key enzymes for these energy-relevant reactions. Synthesis of [NiFe] hydrogenases involves a complex series of biochemical reactions to assemble protein subunits and metalli
Autor:
Tomás Ruiz-Argüeso, José Manuel Palacios, David Durán, Marta Albareda, Ana-Isabel Marina, Carmen García
Publikováno v:
Molecular & Cellular Proteomics : MCP
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC. Repositorio Institucional del CSIC
instname
The Rhizobium-legume symbiosis is a beneficial interaction in which the bacterium converts atmospheric nitrogen into ammonia and delivers it to the plant in exchange for carbon compounds. This symbiosis implies the adaptation of bacteria to live insi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::298b5cd885bef21cd94b52aaaef678c1
http://hdl.handle.net/10261/268536
http://hdl.handle.net/10261/268536
Publikováno v:
Febs Letters
FEBS Letters
FEBS Letters
Salmonella enterica serovar Typhimurium has the ability to use molecular hydrogen as a respiratory electron donor. This is facilitated by three [NiFe]‐hydrogenases termed Hyd‐1, Hyd‐2, and Hyd‐5. Hyd‐1 and Hyd‐5 are homologous oxygen‐to
Autor:
Rebecca Lowden, Alexander J. Finney, Marta Albareda, Frank Sargent, Sarah J. Coulthurst, Michal Fleszar
SummaryPectobacterium atrosepticumSCRI1043 is a phytopathogenic gram-negative enterobacterium. Genomic analysis has identified that genes required for both respiration and fermentation are expressed under anaerobic conditions. One set of anaerobicall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12f943f3c60119230b49915c78c8f17a
https://doi.org/10.1101/688135
https://doi.org/10.1101/688135
Autor:
José Manuel Palacios, Alba Pacheco-Moreno, Esperanza Martínez-Romero, Ernesto Ormeño-Orrillo, Marta Albareda, Lucía Domingo-Serrano, Luis Rey, David Durán, Alvaro Salinero-Lanzarote
Publikováno v:
FEMS microbiology ecology. 95(5)
The Type VI secretion systems (T6SSs) allow bacteria to translocate effector proteins to other bacteria or to eukaryotic cells. However, little is known about the role of T6SS in endosymbiotic bacteria. In this work we describe the T6SS of Rhizobium
Publikováno v:
The biological chemistry of nickel
Zamble D.,Garner C.D.,Rowinska-Zyrek M.,Kozlowski K. The biological chemistry of nickel, 10, Royal Society of Chemistry, pp.237-258, 2017, RCS Metallobiology, 978-1-78262-498-1. ⟨10.1039/9781788010580-00237⟩
The Biological Chemistry of Nickel ISBN: 9781782624981
Zamble D.,Garner C.D.,Rowinska-Zyrek M.,Kozlowski K. The biological chemistry of nickel, 10, Royal Society of Chemistry, pp.237-258, 2017, RCS Metallobiology, 978-1-78262-498-1. ⟨10.1039/9781788010580-00237⟩
The Biological Chemistry of Nickel ISBN: 9781782624981
International audience; In response to the low nickel availability in most natural environments, bacteria have developed high-affinity transporters to meet cell needs for the synthesis of nickel-containing enzymes. Two main categories of such importe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31c2243a37c2cd762aef03901f0dde26
https://hal.archives-ouvertes.fr/hal-01759790
https://hal.archives-ouvertes.fr/hal-01759790
Autor:
Tomás Ruiz-Argüeso, Luis F. Pacios, Hamid Manyani, Juan Imperial, Luis Rey, Marta Albareda, José Manuel Palacios, Belén Brito
Publikováno v:
Journal of Biological Chemistry. 289:21217-21229
[NiFe] hydrogenases are key enzymes for the energy and redox metabolisms of different microorganisms. Synthesis of these metalloenzymes involves a complex series of biochemical reactions catalyzed by a plethora of accessory proteins, many of them req
Publikováno v:
Journal of Physical Chemistry B, ISSN 1520-6106, 2013, Vol. 117, No. 43
Archivo Digital UPM
Universidad Politécnica de Madrid
Archivo Digital UPM
Universidad Politécnica de Madrid
In the intricate maturation process of [NiFe]-hydrogenases, the Fe(CN)2CO cofactor is first assembled in a HypCD complex with iron coordinated by cysteines from both proteins and CO is added after ligation of cyanides. The small accessory protein Hyp