In bacterial reaction centers protons can diffuse to the secondary quinone by alternative pathways.
The mechanisms of proton conduction to the reduced secondary quinone in bacterial reaction centers were studied in wild-type and genetically modified reaction centers from Rhodobacter capsulatus. In the L212-213AA double mutant (L212Glu----Ala, L213Asp----Ala), reaction center function is severely altered. However, a photocompetent revertant of this strain which carries a third 'compensating' mutation, M231Arg----Leu, at about 15 A from the secondary quinone, displays the normal proton binding function of the reaction center. Furthermore, the apparent pK values of group(s) involved in the stabilization of the semiquinone anion are restored by that mutation. We conclude that L212Glu and L213Asp are not obligatory residues for proton donation to QB in Rb. capsulatus. We suggest that protons can be delivered to the QB site from the cytoplasm via a network of proton channels activated by compensatory mutations, possibly involving water molecules bound in the interior of the reaction center.
Hanson
D K
DK
Biological and Medical Research Division Argonne National Laboratory, IL.
Baciou
L
L
Tiede
D M
DM
Nance
S L
SL
Schiffer
M
M
Sebban
P
P
D001665:Binding Sites; D009154:Mutation; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D011522:Protons; D011809:Quinones / Q000378:metabolism*; D016354:Rhodobacter capsulatus / Q000235:genetics; D012242:Rhodobacter sphaeroides / Q000235:genetics
D045322:Photosynthetic Reaction Center Complex Proteins; D011522:Protons; D011809:Quinones