Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Dmitry A. Bloch"'
Autor:
Michael I. Verkhovsky, Andreas S. Bommarius, Laren M. Tolbert, Kyril M. Solntsev, Anna I. Krylov, Russell B. Vegh, Ksenia B. Bravaya, Dmitry A. Bloch
Publikováno v:
The Journal of Physical Chemistry. B
Red fluorescent proteins (RFPs) are indispensable tools for deep-tissue imaging, fluorescence resonance energy transfer applications, and super-resolution microscopy. Using time-resolved optical spectroscopy this study investigated photoinduced dynam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::590be1f9abc3b41a5a0cbcc6c497ad85
https://doi.org/10.1021/jp500919a
https://doi.org/10.1021/jp500919a
Publikováno v:
Molecular Microbiology. 90:1190-1200
Summary Reactive oxygen species (ROS) production by respira- tory Complex I from Escherichia coli was studied in bacterial membrane fragments and in the isolated and purified enzyme, either solubilized or incorporated in proteoliposomes. We found tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1e687ce1119f4c0f46b571d63c7a3a0f
https://doi.org/10.1111/mmi.12424
https://doi.org/10.1111/mmi.12424
Autor:
Dmitry A. Bloch, Marina Verkhovskaya
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 45:491-511
In respiring organisms the major energy transduction flux employs the transmembrane electrochemical proton gradient as a physical link between exergonic redox reactions and endergonic ADP phosphorylation. Establishing the gradient involves electrogen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::318eeaf397397d746be123326f7a9423
https://doi.org/10.1016/j.biocel.2012.08.024
https://doi.org/10.1016/j.biocel.2012.08.024
Publikováno v:
Molecular Microbiology. 86:1452-1463
Summary Interpretation of the constantly expanding body of genomic information requires that the function of each gene be established. Here we report the genomic analysis and structural modelling of a previously uncharacterized redox-metabolism prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f44a048da3c9a35c1f1301ea0e2794ba
https://doi.org/10.1111/mmi.12067
https://doi.org/10.1111/mmi.12067
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817:1550-1556
NADH:ubiquinone oxidoreductase (Complex I), the electron input enzyme in the respiratory chain of mitochondria and many bacteria, couples electron transport to proton translocation across the membrane. Complex I is a primary proton pump; although its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94fbed2eaaa164dc3da86ba7bc72ca61
https://doi.org/10.1016/j.bbabio.2012.04.013
https://doi.org/10.1016/j.bbabio.2012.04.013
Publikováno v:
Proceedings of the National Academy of Sciences. 109:7286-7291
Cytochrome cbb 3 belongs to the superfamily of respiratory heme-copper oxidases that couple the reduction of molecular oxygen to proton translocation across the bacterial or mitochondrial membrane. The cbb 3 -type enzymes are found only in bacteria,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae637085a2d931c8c11038a270638feb
https://doi.org/10.1073/pnas.1202151109
https://doi.org/10.1073/pnas.1202151109
Autor:
Esko Oksanen, Michael I. Verkhovsky, Dmitry A. Bloch, Ville R. I. Kaila, Mårten Wikström, Dage Sundholm, Adrian Goldman
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1807:769-778
Cytochrome c oxidase (CcO) is the terminal enzyme of the respiratory chain. By reducing oxygen to water, it generates a proton gradient across the mitochondrial or bacterial membrane. Recently, two independent X-ray crystallographic studies ((Aoyama
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6b7434b90382869f4afdb238245e383
https://doi.org/10.1016/j.bbabio.2010.12.016
https://doi.org/10.1016/j.bbabio.2010.12.016
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1787:1246-1253
Cytochrome bd is a terminal component of the respiratory chain of Escherichia coli catalyzing reduction of molecular oxygen to water. It contains three hemes, b(558), b(595), and d. The detailed spectroelectrochemical redox titration and numerical mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb837d7054674daa0bb9f0655372f1b1
https://doi.org/10.1016/j.bbabio.2009.05.003
https://doi.org/10.1016/j.bbabio.2009.05.003
Publikováno v:
Journal of Biological Chemistry. 284:11301-11308
Cytochrome cbb(3) is the most distant member of the heme-copper oxidase family still retaining the following major feature typical of these enzymes: reduction of molecular oxygen to water coupled to proton translocation across the membrane. The therm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb19e64f970ab29cec366592e2daeed0
https://doi.org/10.1074/jbc.m808839200
https://doi.org/10.1074/jbc.m808839200
Publikováno v:
Biochemistry. 47:7907-7914
Cytochrome bd is a terminal quinol:O 2 oxidoreductase of the respiratory chain of Escherichia coli. The enzyme generates protonmotive force without proton pumping and contains three hemes, b 558, b 595, and d. A highly conserved glutamic acid residue
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cfe9d47247dea3e38816ff94236e0ad
https://doi.org/10.1021/bi800435a
https://doi.org/10.1021/bi800435a