Výsledky vyhledávání

Akademický článek

Reduction of the off-pathway iron-sulphur cluster N1a of Escherichia coli respiratory complex I restrains NAD+ dissociation

Autor: Emmanuel Gnandt, Johannes Schimpf, Caroline Harter, Jo Hoeser, Thorsten Friedrich

Publikováno v: Scientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)

Abstract Respiratory complex I couples the electron transfer from NADH to ubiquinone with the translocation of protons across the membrane. The reaction starts with NADH oxidation by a flavin cofactor followed by transferring the electrons through a

Externí odkaz: https://doaj.org/article/b1d0d1caf25a474aa0e6f1325fcb53a5

Zobrazit plný text záznamu

Plný text ve formátu HTML

Akademický článek

Stabilization of the Highly Hydrophobic Membrane Protein, Cytochrome bd Oxidase, on Metallic Surfaces for Direct Electrochemical Studies

Autor: Anton Nikolaev, Iryna Makarchuk, Alexander Thesseling, Jo Hoeser, Thorsten Friedrich, Frédéric Melin, Petra Hellwig

Publikováno v: Molecules, Vol 25, Iss 14, p 3240 (2020)

The cytochrome bd oxidase catalyzes the reduction of oxygen to water in bacteria and it is thus an interesting target for electrocatalytic studies and biosensor applications. The bd oxidase is completely embedded in the phospholipid membrane. In this

Externí odkaz: https://doaj.org/article/dc07fb47323b4962b943b78f7d5e36fd

Zobrazit plný text záznamu

Plný text ve formátu HTML

Significance of [2Fe-2S] Cluster N1a for Electron Transfer and Assembly of Escherichia coli Respiratory Complex I

Autor: Katerina Dörner, Jo Hoeser, Marta Vranas, Thorsten Friedrich, Johannes Schimpf, Isabella R. Straub

Publikováno v: Biochemistry. 56:2770-2778

NADH:ubiquinone oxidoreductase, respiratory complex I, couples electron transfer from NADH to ubiquinone with proton translocation across the membrane. NADH reduces a noncovalently bound FMN, and the electrons are transported further to the quinone r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::827257d8a66e2b63dbbd0e4c0238b1b9
https://doi.org/10.1021/acs.biochem.6b01058

Zobrazit plný text záznamu

Stabilization of the Highly Hydrophobic Membrane Protein, Cytochrome bd Oxidase, on Metallic Surfaces for Direct Electrochemical Studies

Autor: Thorsten Friedrich, Frederic Melin, Petra Hellwig, Jo Hoeser, Anton Nikolaev, Alexander Thesseling, Iryna Makarchuk

Publikováno v: Molecules, Vol 25, Iss 3240, p 3240 (2020)
Molecules
Volume 25
Issue 14
Molecules, MDPI, 2020, 25 (14), ⟨10.3390/molecules25143240⟩

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4aaf632a4bce602b6e579e61d92ad97d
https://doi.org/10.3390/molecules25143240

Zobrazit plný text záznamu

Plný text ve formátu HTML

Low cost, microcontroller based heating device for multi-wavelength differential scanning fluorimetry

Autor: Jo Hoeser, Thorsten Friedrich, Emmanuel Gnandt

Publikováno v: Scientific Reports, Vol 8, Iss 1, Pp 1-10 (2018)
Scientific Reports

Differential scanning fluorimetry is a popular method to estimate the stability of a protein in distinct buffer conditions by determining its ‘melting point’. The method requires a temperature controlled fluorescence spectrometer or a RT-PCR mach

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0958231cc8b26a264866642ef41faf0
https://doi.org/10.1038/s41598-018-19702-6

Zobrazit plný text záznamu

Cytochrome bd Displays Significant Quinol Peroxidase Activity

Autor: Yuanjie Yu, Thorsten Friedrich, Jo Hoeser, Sinan Al-Attar, Simon de Vries, Martijn W. H. Pinkse, Dirk Bald

Publikováno v: Scientific Reports, 6(27631). Nature Publishing Group
Scientific Reports
Al-Attar, S, Yu, Y, Pinske, M, Hoeser, J, Friedrich, T, Bald, D & de Vries, S 2016, ' Cytochrome bd displays significant quinol peroxidase activity ', Scientific Reports, vol. 6, no. 27631 . https://doi.org/10.1038/srep27631
Scientific Reports, 6

Cytochrome bd is a prokaryotic terminal oxidase that catalyses the electrogenic reduction of oxygen to water using ubiquinol as electron donor. Cytochrome bd is a tri-haem integral membrane enzyme carrying a low-spin haem b558, and two high-spin haem

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a461342ef8568ace64dcaf5d28eaced
https://doi.org/10.1038/srep27631

Zobrazit plný text záznamu

Creation of a gold nanoparticle based electrochemical assay for the detection of inhibitors of bacterial cytochrome bd oxidases

Autor: Petra Hellwig, Jo Hoeser, Anton Nikolaev, Hamid R. Nasiri, Thorsten Friedrich, Frederic Melin, Eugénie Fournier

Publikováno v: Bioelectrochemistry
Bioelectrochemistry, 2016, 111, pp.109-114. ⟨10.1016/j.bioelechem.2016.06.001⟩

PMID: 27314676; Cytochrome bd oxidases are membrane proteins expressed by bacteria including a number of pathogens, which make them an attractive target for the discovery of new antibiotics. An electrochemical assay is developed to study the activity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e1de1d505b3c38fa491b222f7fadf90
https://hal.archives-ouvertes.fr/hal-03337399

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání