Zobrazeno 1 - 10
of 184
pro vyhledávání: '"Ernst Walter Knapp"'
Publikováno v:
ACS Omega, Vol 3, Iss 2, Pp 1653-1662 (2018)
Externí odkaz:
https://doaj.org/article/4a60f9dc621d422c86990e8e83df187b
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
Publikováno v:
The Journal of Physical Chemistry B. 125:9668-9677
Cytochrome c oxidase (CcO) pumps protons from the N-side to the P-side and consumes electrons from the P-side of the mitochondrial membrane driven by energy gained from reduction of dioxygen to water. ATP synthesis uses the resulting proton gradient
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a265a1b00c1e14ee36783355581cf7fe
https://doi.org/10.1021/acs.jpcb.1c03619
https://doi.org/10.1021/acs.jpcb.1c03619
Autor:
Anna Lena Woelke, Ulrike Alexiev, Juliane Wonneberg, Milan Hodoscek, Ernst-Walter Knapp, Alexander Wolf, Jens Balke, Jovan Dragelj, Johannes Stellmacher
Publikováno v:
Chemical Science. 11:3804-3811
Cytochrome c oxidase (CcO), a redox-coupled proton pump, catalyzes the reduction of molecular oxygen to water, thereby establishing the transmembrane proton gradient that fuels ATP synthesis. CcO employs two channels for proton uptake, the D- and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6881873805b0226689920cf623ada35
https://doi.org/10.1039/c9sc06463j
https://doi.org/10.1039/c9sc06463j
Publikováno v:
The journal of physical chemistry. B. 125(34)
Cytochrome
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::83265d4824512739977bf8a0cc5861f4
https://pubmed.ncbi.nlm.nih.gov/34427096
https://pubmed.ncbi.nlm.nih.gov/34427096
Publikováno v:
ACS Omega, Vol 3, Iss 2, Pp 1653-1662 (2018)
ACS Omega
ACS Omega
An empirical conversion method (ECM) that transforms pKa values of arbitrary organic compounds from one solvent to the other is introduced. We demonstrate the method’s usefulness and performance on pKa conversions involving water and organic solven
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4998ecc38197a822d5efd77878440542
https://doi.org/10.1021/acsomega.7b01895
https://doi.org/10.1021/acsomega.7b01895
Autor:
Ernst-Walter Knapp, Emanuele Rossini
Publikováno v:
Coordination Chemistry Reviews. 345:16-30
We report state-of-the-art pKA computations of manganese model systems. The employed methods can be used to perform pKA computations on the oxygen evolving Mn4CaO5 cluster (OEC) in photosystem II (PSII). These computations are very useful for underst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e2b0200ba6b302d2f75b9a4204df0c9d
https://doi.org/10.1016/j.ccr.2017.02.017
https://doi.org/10.1016/j.ccr.2017.02.017
Autor:
Till Stensitzki, Yang Yang, Ernst-Walter Knapp, Anna Lena Wölke, Maria Andrea Mroginski, Karsten Heyne, Jon Hughes
Publikováno v:
Photochemistry and Photobiology. 93:703-712
Photoisomerization of a protein-bound chromophore is the basis of light sensing and signaling in many photoreceptors. Phytochrome photoreceptors can be photoconverted reversibly between the Pr and Pfr states through photoisomerization of the methine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8663bb6273901c91700db8157500e04a
https://doi.org/10.1111/php.12743
https://doi.org/10.1111/php.12743
Autor:
Inez M. Weidinger, Murat Sezer, Ernst-Walter Knapp, Ramona Schlesinger, Maria Andrea Mroginski, Anna Lena Woelke
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1858:103-108
Understanding the coupling between heme reduction and proton translocation in cytochrome c oxidase (CcO) is still an open problem. The propionic acids of heme a3 have been proposed to act as a proton loading site (PLS) in the proton pumping pathway,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::853f3238bb6ce402392e9f116637feda
https://doi.org/10.1016/j.bbabio.2016.10.009
https://doi.org/10.1016/j.bbabio.2016.10.009
Autor:
Artur Galstyan, Holger Dau, Petko Chernev, Ivelina Zaharieva, Ernst-Walter Knapp, Emanuele Rossini
Publikováno v:
The Journal of Physical Chemistry B. 120:10899-10922
Structural data of the oxygen-evolving complex (OEC) in photosystem II (PSII) determined by X-ray crystallography, quantum chemistry (QC), and extended X-ray absorption fine structure (EXAFS) analyses are presently inconsistent. Therefore, a detailed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::798fb2138bea2fb9c24c29538e1ab1a1
https://doi.org/10.1021/acs.jpcb.6b05800
https://doi.org/10.1021/acs.jpcb.6b05800