Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Lina Salomonsson"'
Publikováno v:
Proceedings of the National Academy of Sciences. 102:17624-17629
In mitochondria and aerobic bacteria energy conservation involves electron transfer through a number of membrane-bound protein complexes to O 2 . The reduction of O 2 , accompanied by the uptake of substrate protons to form H 2 O, is catalyzed by cyt
Publikováno v:
Proceedings of the National Academy of Sciences. 101:11617-11621
Proteins undergo structural fluctuations between nearly isoenergetic substates. Such fluctuations are often intimately linked with the functional properties of proteins. However, in some cases, such as in transmembrane ion transporters, the control o
Autor:
Jimmy Gray, Gwen Gilderson, Peter Brzezinski, Jonathan P. Hosler, Anna Aagaard, Lina Salomonsson
Publikováno v:
Biochemistry. 42:7400-7409
The catalytic core of cytochrome c oxidase is composed of three subunits where subunits I and II contain all of the redox-active metal centers and subunit III is a seven transmembrane helix protein that binds to subunit I. The N-terminal region of su
Autor:
Hyun Ju Lee, Davinia Arjona, Nathalie Gonska, Joachim Reimann, Josy ter Beek, Pia Ädelroth, Lina Salomonsson
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817
Autor:
Takehiko Tosha, Joachim Reimann, Nils Krause, Pia Ädelroth, Nathalie Gonska, Lina Salomonsson, Yoshitsugu Shiro
Bacterial nitric oxide reductases (NOR) are integral membrane proteins that catalyse the reduction of nitric oxide to nitrous oxide, often as a step in the process of denitrification. Most functional data has been obtained with NORs that receive thei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0302393e18b2554c9cad93749ba98a8a
https://refubium.fu-berlin.de/handle/fub188/14455
https://refubium.fu-berlin.de/handle/fub188/14455
Proton-transfer reactions across and at the surface of biological membranes are central for maintaining the transmembrane proton electrochemical gradients involved in cellular energy conversion. In this study, fluorescence correlation spectroscopy wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f831aadedd8915baf222adca004f796b
http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-10399
http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-10399
Publikováno v:
Biochimica et biophysica acta. 1777(4)
In mitochondria and many aerobic bacteria cytochrome c oxidase is the terminal enzyme of the respiratory chain where it catalyses the reduction of oxygen to water. The free energy released in this process is used to translocate (pump) protons across
Redox-driven proton pumps such as cytochrome c oxidase (C c O) are fundamental elements of the energy transduction machinery in biological systems. C c O is an integral membrane protein that acts as the terminal electron acceptor in respiratory chain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3d28e655d21090a4e5a22dd573c255f
https://europepmc.org/articles/PMC1622835/
https://europepmc.org/articles/PMC1622835/
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. (5-6):388-394
Cytochrome c oxidase (CytcO) is a redox-driven proton pump in the respiratory chain of mitochondria and many aerobic bacteria. The results from several studies have shown that zinc ions interfere with both the uptake and release of protons, presumabl
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. (7-8):897-903
Cytochrome c oxidase is a membrane-bound enzyme, which catalyses the one-electron oxidation of four molecules of cytochrome c and the four-electron reduction of O(2) to water. Electron transfer through the enzyme is coupled to proton pumping across t