Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Håkan Lepp"'
Autor:
Peter Brzezinski, Hyun Ju Lee, Robert B. Gennis, Jessica M. J. Swanson, Håkan Lepp, Emelie Svahn, Gregory A. Voth
Publikováno v:
Journal of the American Chemical Society. 132:16225-16239
Cytochrome c oxidase (CytcO), the final electron acceptor in the respiratory chain, catalyzes the reduction of O(2) to H(2)O while simultaneously pumping protons across the inner mitochondrial or bacterial membrane to maintain a transmembrane electro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::364228bd7414715bba342e0667993936
https://doi.org/10.1021/ja107244g
https://doi.org/10.1021/ja107244g
Publikováno v:
Biochemistry. 47:4929-4935
Cytochrome c oxidase couples electron transfer from cytochrome c to O 2 to proton pumping across the membrane. In the initial part of the reaction of the reduced cytochrome c oxidase with O 2, an electron is transferred from heme a to the catalytic s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a13c1293f037cb63271af82855f909f3
https://doi.org/10.1021/bi7024707
https://doi.org/10.1021/bi7024707
Autor:
Magnus Brändén, Audrius Jasaitis, Håkan Lepp, Peter Brzezinski, Andreas Namslauer, Michael I. Verkhovsky
Publikováno v:
Journal of Biological Chemistry. 282:15148-15158
Cytochrome c oxidase (CytcO) is a redox-driven, membrane-bound proton pump. One of the proton transfer pathways of the enzyme, the D pathway, used for the transfer of both substrate and pumped protons, accommodates a network of hydrogen-bonded water
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e34c89d6f93ad6839afc94c2f8d9826
https://doi.org/10.1074/jbc.m700348200
https://doi.org/10.1074/jbc.m700348200
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1767:362-373
Nitric oxide reductase (NOR) from P. denitrificans is a membrane-bound protein complex that catalyses the reduction of NO to N(2)O (2NO+2e(-)+2H(+)-->N(2)O+H(2)O) as part of the denitrification process. Even though NO reduction is a highly exergonic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::548e35f9ef781caf177901765df4ad69
https://doi.org/10.1016/j.bbabio.2007.03.006
https://doi.org/10.1016/j.bbabio.2007.03.006
Autor:
Peter Brzezinski, Håkan Lepp
Publikováno v:
Biochimica et biophysica acta. 1790(6)
Background In the membrane-bound enzyme cytochrome c oxidase, electron transfer from cytochrome c to O2 is linked to proton uptake from solution to form H2O, resulting in a charge separation across the membrane. In addition, the reaction drives pumpi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::521f2e1ccf841019c202550f36bfe752
https://pubmed.ncbi.nlm.nih.gov/19344748
https://pubmed.ncbi.nlm.nih.gov/19344748
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 105(51)
The heme-copper oxidase (HCuO) superfamily consists of integral membrane proteins that catalyze the reduction of either oxygen or nitric oxide. The HCuOs that reduce O 2 to H 2 O couple this reaction to the generation of a transmembrane proton gradie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fcdb6eb5a735d7e62f697dfde8221dc
https://pubmed.ncbi.nlm.nih.gov/19074284
https://pubmed.ncbi.nlm.nih.gov/19074284
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1777:S69-S70
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d5115ad0cc10cedd926c34a6941c753
https://doi.org/10.1016/j.bbabio.2008.05.274
https://doi.org/10.1016/j.bbabio.2008.05.274
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b351afbc2590a770ff09145d635880c