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C Abresch

Showing results (21-30 of 34) with videos related to

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Biochemistry|June 26, 2007
ENDOR spectroscopy reveals light induced movement of the H-bond from Ser-L223 upon forming the semiquinone (Q(B)(-)(*)) in reaction centers from Rhodobacter sphaeroidesM L Paddock, M Flores, R Isaacson, et al.
Biochimica Et Biophysica Acta|August 7, 1985
Electron nuclear double resonance of semiquinones in reaction centers of Rhodopseudomonas sphaeroidesW Lubitz, E C Abresch, R J Debus, et al.
Structure (London, England : 1993)|April 6, 2004
X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathwaysQiang Xu, Herbert L Axelrod, Edward C Abresch, et al.
Journal of Molecular Biology|June 8, 2002
X-ray structure determination of the cytochrome c2: reaction center electron transfer complex from Rhodobacter sphaeroidesHerbert L Axelrod, Edward C Abresch, Melvin Y Okamura, et al.
Biochemistry|November 23, 2006
Trapped conformational states of semiquinone (D+*QB-*) formed by B-branch electron transfer at low temperature in Rhodobacter sphaeroides reaction centersM L Paddock, M Flores, R Isaacson, et al.
Photosynthesis Research|September 21, 2005
Characterization of a highly purified, fully active, crystallizable RC-LH1-PufX core complex from Rhodobacter sphaeroidesE C Abresch, H L A Axelrod, J T Beatty, et al.
Biochemistry|May 4, 2005
Quinone (QB) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structureM L Paddock, C Chang, Q Xu, et al.
The Journal of Physical Chemistry. B|November 25, 2010
Electron-nuclear and electron-electron double resonance spectroscopies show that the primary quinone acceptor QA in reaction centers from photosynthetic bacteria Rhodobacter sphaeroides remains in the same orientation upon light-induced reductionMarco Flores, Anton Savitsky, Mark L Paddock, et al.
Journal of the American Chemical Society|September 4, 2010
Engineering the redox potential over a wide range within a new class of FeS proteinsJohn A Zuris, Danny A Halim, Andrea R Conlan, et al.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|July 4, 2009
The novel 2Fe-2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domainAndrea R Conlan, Mark L Paddock, Herbert L Axelrod, et al.
Pageof 4

Showing results (21-30 of 34) with videos related to

Sort By:
Pageof 4
Biochemistry|June 26, 2007
ENDOR spectroscopy reveals light induced movement of the H-bond from Ser-L223 upon forming the semiquinone (Q(B)(-)(*)) in reaction centers from Rhodobacter sphaeroidesM L Paddock, M Flores, R Isaacson, et al.
Biochimica Et Biophysica Acta|August 7, 1985
Electron nuclear double resonance of semiquinones in reaction centers of Rhodopseudomonas sphaeroidesW Lubitz, E C Abresch, R J Debus, et al.
Structure (London, England : 1993)|April 6, 2004
X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathwaysQiang Xu, Herbert L Axelrod, Edward C Abresch, et al.
Journal of Molecular Biology|June 8, 2002
X-ray structure determination of the cytochrome c2: reaction center electron transfer complex from Rhodobacter sphaeroidesHerbert L Axelrod, Edward C Abresch, Melvin Y Okamura, et al.
Biochemistry|November 23, 2006
Trapped conformational states of semiquinone (D+*QB-*) formed by B-branch electron transfer at low temperature in Rhodobacter sphaeroides reaction centersM L Paddock, M Flores, R Isaacson, et al.
Photosynthesis Research|September 21, 2005
Characterization of a highly purified, fully active, crystallizable RC-LH1-PufX core complex from Rhodobacter sphaeroidesE C Abresch, H L A Axelrod, J T Beatty, et al.
Biochemistry|May 4, 2005
Quinone (QB) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structureM L Paddock, C Chang, Q Xu, et al.
The Journal of Physical Chemistry. B|November 25, 2010
Electron-nuclear and electron-electron double resonance spectroscopies show that the primary quinone acceptor QA in reaction centers from photosynthetic bacteria Rhodobacter sphaeroides remains in the same orientation upon light-induced reductionMarco Flores, Anton Savitsky, Mark L Paddock, et al.
Journal of the American Chemical Society|September 4, 2010
Engineering the redox potential over a wide range within a new class of FeS proteinsJohn A Zuris, Danny A Halim, Andrea R Conlan, et al.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|July 4, 2009
The novel 2Fe-2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domainAndrea R Conlan, Mark L Paddock, Herbert L Axelrod, et al.
Pageof 4