Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Alexander H. Haas"'
Autor:
Wei Gu, C. Roy D. Lancaster, Elena Herzog, Jörg Simon, Werner Mäntele, Alexander H. Haas, Hanno Juhnke, Volkhard Helms
Publikováno v:
Biophysical Journal. 103(6):1305-1314
The E-pathway of transmembrane proton transfer has been demonstrated previously to be essential for catalysis by the diheme-containing quinol:fumarate reductase (QFR) of Wolinella succinogenes. Two constituents of this pathway, Glu-C180 and heme b(D)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70840f0c332d3119ed629e3cd573ddf4
Publikováno v:
Biochemistry. 44:16718-16728
Quinol:fumarate reductase (QFR) is the terminal enzyme of anaerobic fumarate respiration. This membrane protein complex couples the oxidation of menaquinol to menaquinone to the reduction of fumarate to succinate. Although the diheme-containing QFR f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86bf293268c266456fde57e15add088a
https://doi.org/10.1021/bi051034s
https://doi.org/10.1021/bi051034s
Autor:
Ursula S. Sauer, Alexander H. Haas, Roland Gross, C. Roy D. Lancaster, Jörg Simon, Werner Mäntele
Publikováno v:
Biochemistry. 44:13949-13961
Electrochemically induced static FTIR difference spectroscopy has been employed to investigate redox-driven protonation changes of individual amino acid residues in the quinol:fumarate reductase (QFR) from Wolinella succinogenes. The difference spect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf6321b38ba0d6fd453cd09c96b56ed9
https://doi.org/10.1021/bi051011d
https://doi.org/10.1021/bi051011d
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1744(3):383-395
In this review we will focus on the recent advances in how coiled-coil proteins of the golgin family give identity and structure to the Golgi apparatus in animal cells. A number of recent studies reveal a common theme for the targeting of golgins con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2df15f45f0feebbed855649b8a938cca
Autor:
Robert Kopajtich, Benjamin Short, Christian Preisinger, Jan Gettemans, Francis A. Barr, Erik Bruyneel, Veerle De Corte, Alexander H. Haas
Publikováno v:
The Journal of Cell Biology
The Golgi apparatus has long been suggested to be important for directing secretion to specific sites on the plasma membrane in response to extracellular signaling events. However, the mechanisms by which signaling events are coordinated with Golgi a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c11ae13cf296b22dba9a608c6ed5b8de
http://europepmc.org/articles/PMC2172068
http://europepmc.org/articles/PMC2172068
Autor:
Mauro Mileni, Klaus Zwicker, Fraser MacMillan, C. Roy D. Lancaster, Jörg Simon, Werner Mäntele, Christos Tziatzios, Alexander H. Haas
The ϵ-proteobacteria Helicobacter pylori and Campylobacter jejuni are both human pathogens. They colonize mucosal surfaces causing severe diseases. The membrane protein complex QFR (quinol:fumarate reductase) from H. pylori has previously been estab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::637977cdfb574baf51b72d62d26bcd19
https://europepmc.org/articles/PMC1409705/
https://europepmc.org/articles/PMC1409705/
Publikováno v:
Biochimica et biophysica acta. 1757(8)
Reconciliation of apparently contradictory experimental results obtained on the quinol: fumarate reductase (QFR), a dihaem-containing respiratory membrane protein complex from Wolinella succinogenes, was previously obtained by the proposal of the so-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14b75a8137071ca8b7a4618504fe9c6b
https://pubmed.ncbi.nlm.nih.gov/16790236
https://pubmed.ncbi.nlm.nih.gov/16790236
Autor:
C. Roy D. Lancaster, Roland Groß, Alexander H. Haas, Jürgen Graf, M. Gregor Madej, Jörg Simon, Harald Schwalbe, Werner Mäntele, Ursula S. Sauer
Reconciliation of apparently contradictory experimental results obtained on the quinol:fumarate reductase, a diheme-containing respiratory membrane protein complex from Wolinella succinogenes , was previously obtained by the proposal of the so-called
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09c3b4ec61c5eec1e5b6ed4a443d1166
https://europepmc.org/articles/PMC1323215/
https://europepmc.org/articles/PMC1323215/
Autor:
C. Roy D. Lancaster, Alexander H. Haas
The quinol:fumarate reductase of Wolinella succinogenes binds a low- and a high-potential heme b group in its transmembrane subunit C. Both hemes are part of the electron transport chain between the two catalytic sites of this redox enzyme. The oxida
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::928eae3cf82c99c249f8df5009c8114a
https://europepmc.org/articles/PMC1304937/
https://europepmc.org/articles/PMC1304937/
Autor:
Alexander H. Haas, Jörg Simon, C. Roy D. Lancaster, Werner Mäntele, Roland Groß, Achim Kröger, Michaela Ritter
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 97(24)
Quinol:fumarate reductase (QFR) is a membrane protein complex that couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalyzed by the related enzyme succinate:quinone reductase (succi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6421b5ea7347a2b341aec09eea1e1ad
https://pubmed.ncbi.nlm.nih.gov/11186225
https://pubmed.ncbi.nlm.nih.gov/11186225