Zobrazeno 1 - 10
of 83
pro vyhledávání: '"Eliane Nabedryk"'
Publikováno v:
Photosynthesis Research
Photosynthesis Research, Springer Verlag, 2019, 140 (3), pp.263-274. ⟨10.1007/s11120-019-00618-9⟩
Photosynthesis Research, 2019, 140 (3), pp.263-274. ⟨10.1007/s11120-019-00618-9⟩
Photosynthesis Research, Springer Verlag, 2019, 140 (3), pp.263-274. ⟨10.1007/s11120-019-00618-9⟩
Photosynthesis Research, 2019, 140 (3), pp.263-274. ⟨10.1007/s11120-019-00618-9⟩
International audience; Jacques Breton spent his 39 years of professional life at Saclay, a center of the French Atomic Energy Commission. He studied photosynthesis with various advanced biophysical tools, often developed by himself and his numerous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e2ebfd72df36d7adb0e487c32eb02d5
https://hal.archives-ouvertes.fr/hal-02196743
https://hal.archives-ouvertes.fr/hal-02196743
Publikováno v:
Biochemistry. 46:6468-6476
In native reaction centers (RCs) from photosynthetic purple bacteria the primary quinone (QA) and the secondary quinone (QB) are interconnected via a specific His-Fe-His bridge. In Rhodobacter sphaeroides RCs the C4=O carbonyl of QA forms a very stro
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1656(2-3):127-138
In Rhodobacter sphaeroides reaction centers (RCs) containing the mutation Ala M260 to Trp (AM260W), transmembrane electron transfer along the full-length of the A-branch of cofactors is prevented by the loss of the Q(A) ubiquinone, but it is possible
Publikováno v:
Biochemistry. 43:4755-4763
In Rhodobacter sphaeroides reaction centers containing the mutation Ala M260 to Trp (AM260W), transmembrane electron transfer along the A-branch of cofactors is prevented by the loss of the QA ubiquinone. Reaction centers that contain this AM260W mut
Publikováno v:
Biochemistry. 42:5819-5827
The effect of substituting Pro-L209 with Tyr, Phe, Glu, and Thr in photosynthetic reaction centers (RCs) from Rhodobacter sphaeroides was investigated by monitoring the light-induced FTIR absorption changes associated with the photoreduction of the s
Publikováno v:
FEBS Letters. 537:161-165
The photoreduction of the quinone (Q) pool in the photosynthetic membrane of the purple bacterium Rhodobacter sphaeroides was investigated by steady-state and time-resolved Fourier transform infrared difference spectroscopy. The results are consisten
Autor:
Eliane Nabedryk, Richard J. Cogdell, Bruno Robert, Neil W. Isaacs, Michael R. Jones, Katherine McAuley, Jacques Breton, Aleksander W. Roszak, Kimberley McKendrick, Diane Spiedel, Paul K. Fyfe
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1554(1-2):75-93
A series of mutations have been introduced at residue 168 of the L-subunit of the reaction centre from Rhodobacter sphaeroides. In the wild-type reaction centre, residue His L168 donates a strong hydrogen bond to the acetyl carbonyl group of one of t
Autor:
Giovanni Giacometti, Melvin Y. Okamura, Jacques Breton, Winfried Leibl, Alberto Mezzetti, Eliane Nabedryk, Mark L. Paddock
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1553(3):320-330
Rapid-scan Fourier transform infrared (FTIR) difference spectroscopy was used to investigate the electron transfer reaction Q(A-)Q(B)--Q(A)Q(B-) (k(AB)(1)) in mutant reaction centers of Rhodobacter sphaeroides, where Asp-L210 and/or Asp-M17 have been
Publikováno v:
Biochemistry. 40:13826-13832
In the photosynthetic reaction center (RC) from Rhodobacter sphaeroides, the first electron transfer to the secondary quinone acceptor Q(B) is coupled to the protonation of Glu-L212, located approximately 5 A from the center of Q(B). Upon the second
Publikováno v:
The Journal of Physical Chemistry B. 103:6363-6370
Stable conformations and vibrational spectra of 2-methoxy-3-methyl-1,4-benzoquinone were calculated using density functional methods. Two stable conformers have been found which differ in their vib...