Výsledky vyhledávání - "Audrius Jasaitis"

Best versatility/localization precision combination in single molecule localization microscopy enabled by adaptive optics: MicAO 3DSR

Autor: Cynthia Veilly, Fabrice Harms, Xavier Levecq, Audrius Jasaitis

Publikováno v: Single Molecule Spectroscopy and Superresolution Imaging XIV.

PSF engineering has been widely used over the past years to enable 3D localization in Single Molecule Localization Microscopy (SMLM) techniques, such as PALM/STORM superresolution methods. It can make use of a cylindrical lens, a phase mask, a Spatia

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1a36898aab7635d372bac754ec2e3cea
https://doi.org/10.1117/12.2583292

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Ultrafast heme–ligand recombination in truncated hemoglobin HbO from Mycobacterium tuberculosis: A ligand cage

Autor: Joel M. Friedman, Marten H. Vos, Hugues Ouellet, Audrius Jasaitis, Michel Guertin, Jean-Louis Martin, Jean Christophe Lambry

Publikováno v: Chemical Physics
Chemical Physics, Elsevier, 2012, 396, pp.10-16. ⟨10.1016/j.chemphys.2011.04.003⟩

International audience; Truncated hemoglobin HbO from Mycobacterium tuberculosis displays very slow exchange of diatomic ligands with its environment. Using femtosecond spectroscopy, we show that upon photoexcitation, ligands rebind with unusual spee

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d22fe1bf72976c9b2c25201ba2dcc3e
https://doi.org/10.1016/j.chemphys.2011.04.003

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Additive Effect of Mutations Affecting the Rate of Phylloquinone Reoxidation and Directionality of Electron Transfer within Photosystem I†

Autor: Stefano Santabarbara, Fabrice Rappaport, Martin Byrdin, Kevin Redding, Feifei Gu, Audrius Jasaitis

Publikováno v: Photochemistry and Photobiology. 84:1381-1387

Optical pump-probe spectroscopy in the nanosecond-microsecond timescale has been used to study the electron transfer reactions taking place within the Photosystem I reaction center of intact Chlamydomonas reinhardtii cells. The biphasic kinetics of p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c74a753ba162e6060e2f5530d8f599c
https://doi.org/10.1111/j.1751-1097.2008.00458.x

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Subpicosecond oxygen trapping in the heme pocket of the oxygen sensor FixL observed by time-resolved resonance Raman spectroscopy

Autor: Audrius Jasaitis, Klara Hola, Jean-Louis Martin, Taku Yamashita, Sergei G. Kruglik, Marten H. Vos, Ursula Liebl

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2007, 104 (18), pp.7408-7413. ⟨10.1073/pnas.0700445104⟩
Proceedings of the National Academy of Sciences of the United States of America, 2007, 104 (18), pp.7408-7413. ⟨10.1073/pnas.0700445104⟩

Dissociation of oxygen from the heme domain of the bacterial oxygen sensor protein FixL constitutes the first step in hypoxia-induced signaling. In the present study, the photodissociation of the heme-O 2 bond was used to synchronize this event, and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1e084a36c18bb349e2dff80ebf5106a
https://doi.org/10.1073/pnas.0700445104

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Plasticity of Proton Pathway Structure and Water Coordination in Cytochrome c Oxidase

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

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Ligand Dynamics in an Electron Transfer Protein

Autor: Marten H. Vos, Audrius Jasaitis, Gary Silkstone, Michael T. Wilson

Publikováno v: Journal of Biological Chemistry. 282:1638-1649

Substitution of the heme coordination residue Met-80 of the electron transport protein yeast iso-1-cytochrome c allows external ligands like CO to bind and thus increase the effective redox potential. This mutation, in principle, turns the protein in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e39180f10ad5898b9acdcb1898c38835
https://doi.org/10.1074/jbc.m605760200

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Activationless electron transfer through the hydrophobic core of cytochrome c oxidase

Autor: Marten H. Vos, Ursula Liebl, Fabrice Rappaport, Audrius Jasaitis, Eric Pilet

Electron transfer (ET) within proteins occurs by means of chains of redox intermediates that favor directional and efficient electron delivery to an acceptor. Individual ET steps are energetically characterized by the electronic coupling V , driving

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::237ca9f5531c67c7ed08106956683578
https://doi.org/10.1073/pnas.0503001102

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Ultrafast haem–haem electron transfer in cytochrome c oxidase

Autor: Audrius Jasaitis, Michael I. Verkhovsky, Mårten Wikström

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1506(3):143-146

Electron transfer between the redox centres is essential for the function of the haem–copper oxidases. To date, the fastest rate of electron transfer between the haem groups has been determined to be ca. 3×105 s−1. Here, we show by optical spect

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