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Bacteriorhodopsin is a 26 KD protein with all-transretinal attached. Light induced isomerization of this protein drives H+ translocation. Light is converted directly into a H+ motive force.
Bacteriorhodopsin is a 26 KD protein with all-transretinal attached. Light induced isomerization of this protein drives H+ translocation. Light is converted directly into a H+ motive force.
Bacteriorhodopsin is a 26 KD protein with all-transretinal attached. Light induced isomerization of this protein drives H+ translocation. Light is converted directly into a H+ motive force.
Resides in hypertonic environments (shallow waters of San
Francisco bay) Diatomic oxygen is plentiful = OXPHOS Diatomic oxygen unavailable = LIGHT HARVESTING Achieved by Bacteriorhodopsin, a 26 KD protein with all-transretinal attached
LIGHT IS CONVERTED DIRECTLY INTO A H+ MOTIVE FORCE
hv
H+
H+
+++++++
F0F1 ATPase
--------ATP
Retinal is bound to Lysine
H+ pumping
Photocycle
The energy trapping conformational
transition occurs within one ps Deprotonation and reprotonation steps are characterized by intermediates which contain distinct absorption spectra One full turn of the cycle occurs within a ms Hence each step has a characteristic colour Every sec, 50 protons are exported One question remainshow does the light induced isomerization of this protein drive H+ translocation
Bacteriorhodopsin is a Dynamic, Transmembrane
Protein Several transmem spanning helices 3 Tyr hold the BR in place
Retinal sits at the junction separating the two
half channels
Notice the Bacteriorhodopsin is surronded
by Asp and Arg
Aspartate and Arginine are involved in the translocation