Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Hendrik Mohrmann"'
Autor:
Federico Baserga, Jovan Dragelj, Jacek Kozuch, Hendrik Mohrmann, Ernst-Walter Knapp, Sven T. Stripp, Joachim Heberle
Publikováno v:
Frontiers in Chemistry, Vol 9 (2021)
Cytochrome c oxidase (CcO) is a transmembrane protein complex that reduces molecular oxygen to water while translocating protons across the mitochondrial membrane. Changes in the redox states of its cofactors trigger both O2 reduction and vectorial p
Externí odkaz:
https://doaj.org/article/e864d34714b64a06af9763fda6cbeb98
Autor:
Patrycja Kielb, Murat Sezer, Ramona Schlesinger, Hendrik Mohrmann, Joachim Heberle, Claudia Schulz, Uwe Kuhlmann, Inez M. Weidinger, Dorothea Heinrich
Publikováno v:
The Journal of Physical Chemistry B. 119:9586-9591
Immobilization of Cytochrome c oxidase (CcO) on electrodes makes voltage-driven reduction of oxygen to water possible. Efficient catalytic turnover in CcO/electrode systems is, however, often observed at large overpotentials that cannot be rationaliz
Autor:
Joachim Heberle, Ernst-Walter Knapp, Sven T. Stripp, Hendrik Mohrmann, Jovan Dragelj, Federico Baserga
Publikováno v:
Physical chemistry chemical physics : PCCP. 19(47)
Retraction of ‘The reductive phase of Rhodobacter sphaeroides cytochrome c oxidase disentangled by CO ligation’ by Hendrik Mohrmann et al., Phys. Chem. Chem. Phys., 2017, DOI: 10.1039/c7cp06480b.
Autor:
Hendrik, Mohrmann, Jovan, Dragelj, Federico, Baserga, Ernst-Walter, Knapp, Sven T, Stripp, Joachim, Heberle
Publikováno v:
Physical chemistry chemical physics : PCCP.
Cytochrome c oxidase (CcO) is a membrane protein of the respiratory chain that catalytically reduces molecular oxygen (O
Autor:
Hendrik Mohrmann, Joachim Heberle
Publikováno v:
The journal of physical chemistry. B. 121(30)
Autor:
Federico Baserga, Joachim Heberle, Ernst-Walter Knapp, Jovan Dragelj, Sven T. Stripp, Hendrik Mohrmann
Publikováno v:
Physical Chemistry Chemical Physics.
Cytochrome c oxidase (CcO) is a membrane protein of the respiratory chain that catalytically reduces molecular oxygen (O2) to water while translocating protons across the membrane. The enzyme hosts two copper and two heme iron moieties (heme a/heme a
We have developed a spectrometer based on tunable quantum cascade lasers (QCLs) for recording time-resolved absorption spectra of proteins in the mid-infrared range. We illustrate its performance by recording time-resolved difference spectra of bacte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca8c8dd5d07bdfe83a0bc2f0cdae9917
Publikováno v:
The journal of physical chemistry. B. 120(19)
Sensory rhodopsin II (SRII) is the primary light sensor in the photophobic reaction of the halobacterium Natronomonas pharaonis. Photoactivation of SRII results in a movement of helices F and G of this seven-helical transmembrane protein. This confor
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1859:e71
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1859:e70