Zobrazeno 1 - 10
of 42
pro vyhledávání: '"E. C. Abresch"'
Publikováno v:
Biochemistry. 47:13318-13325
The role of short-range hydrogen bond interactions at the interface between electron transfer proteins cytochrome c(2) (cyt) and the reaction center (RC) from Rhodobacter sphaeroides was studied by mutation (to Ala) of RC residues Asn M187, Asn M188,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8762f800db278ce9b9645cf21c8a3c36
https://doi.org/10.1021/bi801675a
https://doi.org/10.1021/bi801675a
Publikováno v:
Biochemistry. 46:8234-8243
Proton ENDOR spectroscopy was used to monitor local conformational changes in bacterial reaction centers (RC) associated with the electron transfer reaction DQB → D+•QB−• using mutant RCs capable of photo-reducing QB at cryogenic temperatures
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ccee40611f31a35b7504a7ecda354c4
https://doi.org/10.1021/bi7005256
https://doi.org/10.1021/bi7005256
Publikováno v:
Biophysical Journal. 92:671-682
The geometry of the hydrogen bonds to the two carbonyl oxygens of the semiquinone QA ⋅ − in the reaction center (RC) from the photosynthetic purple bacterium Rhodobacter sphaeroides R-26 were determined by fitting a spin Hamiltonian to the da
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b16b215861896c4f2028481e8646af2b
https://doi.org/10.1529/biophysj.106.092460
https://doi.org/10.1529/biophysj.106.092460
Publikováno v:
Biophysical Journal. 90:3356-3362
Hydrogen bonds are important in determining the structure and function of biomolecules. Of particular interest are hydrogen bonds to quinones, which play an important role in the bioenergetics of respiration and photosynthesis. In this work we invest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2d6ccc39f7f94c74996fedcfd28cae0a
https://doi.org/10.1529/biophysj.105.077883
https://doi.org/10.1529/biophysj.105.077883
Autor:
Rachel Nechushtai, Herbert L. Axelrod, E. C. Abresch, J.A. Johnson, J. T. Beatty, Mark L. Paddock
Publikováno v:
Photosynthesis Research. 86:61-70
Photosynthetic complexes in bacteria absorb light and undergo photochemistry with high quantum efficiency. We describe the isolation of a highly purified, active, reaction center-light-harvesting 1-PufX complex (RC-LH1-PufX core complex) from a strai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3691f57388a037cfd61e8cc13571c32d
https://doi.org/10.1007/s11120-005-5106-z
https://doi.org/10.1007/s11120-005-5106-z
Autor:
E. C. Abresch, Q. Xu, C. Chang, George Feher, Herbert L. Axelrod, Mark L. Paddock, Melvin Y. Okamura
Publikováno v:
Biochemistry. 44:6920-6928
The photosynthetic reaction center (RC) from purple bacteria converts light into chemical energy. Although the RC shows two nearly structurally symmetric branches, A and B, light-induced electron transfer in the native RC occurs almost exclusively al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc1fbee222585a9424889984de858627
https://doi.org/10.1021/bi047559m
https://doi.org/10.1021/bi047559m
Autor:
Qiang Xu, George Feher, Melvin Y. Okamura, E. C. Abresch, Herbert L. Axelrod, Mark L. Paddock
Publikováno v:
Structure. 12:703-715
In the photosynthetic reaction center (RC) from Rhodobacter sphaeroides , the reduction of a bound quinone molecule Q B is coupled with proton uptake. When Asp-L213 is replaced by Asn, proton transfer is inhibited. Proton transfer was restored by two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0a1422ca8d89712daacad6a93e460ab
https://doi.org/10.1016/j.str.2004.03.001
https://doi.org/10.1016/j.str.2004.03.001
Publikováno v:
Biophysical Journal. 83:2440-2456
The spin-lattice relaxation times (T(1)) for the reduced quinone acceptors Q(A)(-.) and Q(B)(-.), and the intermediate pheophytin acceptor phi(-.), were measured in native photosynthetic reaction centers (RC) containing a high spin Fe(2+) (S = 2) and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::79efa992f9c7bc1969c964aec8d4b3b3
https://doi.org/10.1016/s0006-3495(02)75256-9
https://doi.org/10.1016/s0006-3495(02)75256-9
Autor:
E. C. Abresch, Melvin Y. Okamura, Douglas C. Rees, Herbert L. Axelrod, Andrew P. Yeh, George Feher
Publikováno v:
Journal of Molecular Biology. 319:501-515
In the photosynthetic bacterium Rhodobacter sphaeroides, a water soluble cytochrome c2 (cyt c2) is the electron donor to the reaction center (RC), the membrane-bound pigment-protein complex that is the site of the primary light-induced electron trans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfba429986aff89ce37a12f837a75fc8
https://doi.org/10.1016/s0022-2836(02)00168-7
https://doi.org/10.1016/s0022-2836(02)00168-7
Publikováno v:
Biochemistry. 40:6893-6902
The reaction center (RC) from Rhodobacter sphaeroides uses light energy to reduce and protonate a quinone molecule, Q(B) (the secondary quinone electron acceptor), to form quinol, Q(B)H2. Asp-L210 and Asp-M17 have been proposed to be components of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d0e5ebbf6398e51d6b41a66426e2c24
https://doi.org/10.1021/bi010280a
https://doi.org/10.1021/bi010280a