178 related articles for article (PubMed ID: 19161296)
1. Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from Rhodobacter sphaeroides.
Iwata T; Paddock ML; Okamura MY; Kandori H
Biochemistry; 2009 Feb; 48(6):1220-9. PubMed ID: 19161296
[TBL] [Abstract][Full Text] [Related]
2. Coupling of electron transfer to proton uptake at the Q(B) site of the bacterial reaction center: a perspective from FTIR difference spectroscopy.
Nabedryk E; Breton J
Biochim Biophys Acta; 2008 Oct; 1777(10):1229-48. PubMed ID: 18671937
[TBL] [Abstract][Full Text] [Related]
3. Fourier transform infrared evidence of proton uptake by glutamate L212 upon reduction of the secondary quinone QB in the photosynthetic reaction center from Rhodobacter capsulatus.
Nabedryk E; Breton J; Joshi HM; Hanson DK
Biochemistry; 2000 Nov; 39(47):14654-63. PubMed ID: 11087422
[TBL] [Abstract][Full Text] [Related]
4. Monitoring the pH dependence of IR carboxylic acid signals upon Q(B)- formation in the Glu-L212 --> Asp/Asp-L213 --> Glu swap mutant reaction center from Rhodobacter sphaeroides.
Nabedryk E; Paddock ML; Okamura MY; Breton J
Biochemistry; 2007 Feb; 46(5):1176-82. PubMed ID: 17260947
[TBL] [Abstract][Full Text] [Related]
5. An isotope-edited FTIR investigation of the role of Ser-L223 in binding quinone (QB) and semiquinone (QB-) in the reaction center from Rhodobacter sphaeroides.
Nabedryk E; Paddock ML; Okamura MY; Breton J
Biochemistry; 2005 Nov; 44(44):14519-27. PubMed ID: 16262252
[TBL] [Abstract][Full Text] [Related]
6. Simultaneous replacement of Asp-L210 and Asp-M17 with Asn increases proton uptake by Glu-L212 upon first electron transfer to QB in reaction centers from Rhodobacter sphaeroides.
Nabedryk E; Breton J; Okamura MY; Paddock ML
Biochemistry; 2001 Nov; 40(46):13826-32. PubMed ID: 11705371
[TBL] [Abstract][Full Text] [Related]
7. Fourier transforms infrared difference spectroscopy of secondary quinone acceptor photoreduction in proton transfer mutants of Rhodobacter sphaeroides.
Nabedryk E; Breton J; Hienerwadel R; Fogel C; Mäntele W; Paddock ML; Okamura MY
Biochemistry; 1995 Nov; 34(45):14722-32. PubMed ID: 7578080
[TBL] [Abstract][Full Text] [Related]
8. Redox potential of quinones in photosynthetic reaction centers from Rhodobacter sphaeroides: dependence on protonation of Glu-L212 and Asp-L213.
Ishikita H; Morra G; Knapp EW
Biochemistry; 2003 Apr; 42(13):3882-92. PubMed ID: 12667079
[TBL] [Abstract][Full Text] [Related]
9. Electrostatic influence of QA reduction on the IR vibrational mode of the 10a-ester C==O of HA demonstrated by mutations at residues Glu L104 and Trp L100 in reaction centers from Rhodobacter sphaeroides.
Breton J; Nabedryk E; Allen JP; Williams JC
Biochemistry; 1997 Apr; 36(15):4515-25. PubMed ID: 9109660
[TBL] [Abstract][Full Text] [Related]
10. Proton uptake by carboxylic acid groups upon photoreduction of the secondary quinone (QB) in bacterial reaction centers from Rhodobacter sphaeroides: FTIR studies on the effects of replacing Glu H173.
Nabedryk E; Breton J; Okamura MY; Paddock ML
Biochemistry; 1998 Oct; 37(41):14457-62. PubMed ID: 9772172
[TBL] [Abstract][Full Text] [Related]
11. Identification of a novel protonation pattern for carboxylic acids upon Q(B) photoreduction in Rhodobacter sphaeroides reaction center mutants at Asp-L213 and Glu-L212 sites.
Nabedryk E; Breton J; Okamura MY; Paddock ML
Biochemistry; 2004 Jun; 43(23):7236-43. PubMed ID: 15182169
[TBL] [Abstract][Full Text] [Related]
12. Quinone (Q(B)) binding site and protein stuctural changes in photosynthetic reaction center mutants at Pro-L209 revealed by vibrational spectroscopy.
Nabedryk E; Breton J; Sebban P; Baciou L
Biochemistry; 2003 May; 42(19):5819-27. PubMed ID: 12741840
[TBL] [Abstract][Full Text] [Related]
13. Reduction and protonation of the secondary quinone acceptor of Rhodobacter sphaeroides photosynthetic reaction center: kinetic model based on a comparison of wild-type chromatophores with mutants carrying Arg-->Ile substitution at sites 207 and 217 in the L-subunit.
Cherepanov DA; Bibikov SI; Bibikova MV; Bloch DA; Drachev LA; Gopta OA; Oesterhelt D; Semenov AY; Mulkidjanian AY
Biochim Biophys Acta; 2000 Jul; 1459(1):10-34. PubMed ID: 10924896
[TBL] [Abstract][Full Text] [Related]
14. Protonation of Glu L212 following QB- formation in the photosynthetic reaction center of Rhodobacter sphaeroides: evidence from time-resolved infrared spectroscopy.
Hienerwadel R; Grzybek S; Fogel C; Kreutz W; Okamura MY; Paddock ML; Breton J; Nabedryk E; Mäntele W
Biochemistry; 1995 Mar; 34(9):2832-43. PubMed ID: 7893696
[TBL] [Abstract][Full Text] [Related]
15. Binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: binding of chainless symmetrical quinones to the QA site of Rhodobacter sphaeroides.
Breton J; Burie JR; Boullais C; Berger G; Nabedryk E
Biochemistry; 1994 Oct; 33(41):12405-15. PubMed ID: 7918463
[TBL] [Abstract][Full Text] [Related]
16. Rapid-scan Fourier transform infrared spectroscopy shows coupling of GLu-L212 protonation and electron transfer to Q(B) in Rhodobacter sphaeroides reaction centers.
Mezzetti A; Nabedryk E; Breton J; Okamura MY; Paddock ML; Giacometti G; Leibl W
Biochim Biophys Acta; 2002 Feb; 1553(3):320-30. PubMed ID: 11997141
[TBL] [Abstract][Full Text] [Related]
17. Vibrational spectroscopy favors a unique QB binding site at the proximal position in wild-type reaction centers and in the Pro-L209 --> Tyr mutant from Rhodobacter sphaeroides.
Breton J; Boullais C; Mioskowski C; Sebban P; Baciou L; Nabedryk E
Biochemistry; 2002 Oct; 41(43):12921-7. PubMed ID: 12390017
[TBL] [Abstract][Full Text] [Related]
18. The unusually strong hydrogen bond between the carbonyl of Q(A) and His M219 in the Rhodobacter sphaeroides reaction center is not essential for efficient electron transfer from Q(A)(-) to Q(B).
Breton J; Lavergne J; Wakeham MC; Nabedryk E; Jones MR
Biochemistry; 2007 Jun; 46(22):6468-76. PubMed ID: 17497939
[TBL] [Abstract][Full Text] [Related]
19. Effects of dehydration on light-induced conformational changes in bacterial photosynthetic reaction centers probed by optical and differential FTIR spectroscopy.
Malferrari M; Mezzetti A; Francia F; Venturoli G
Biochim Biophys Acta; 2013 Mar; 1827(3):328-39. PubMed ID: 23103449
[TBL] [Abstract][Full Text] [Related]
20. Time-resolved infrared spectroscopy of electron transfer in bacterial photosynthetic reaction centers: dynamics of binding and interaction upon QA and QB reduction.
Hienerwadel R; Thibodeau D; Lenz F; Nabedryk E; Breton J; Kreutz W; Mäntele W
Biochemistry; 1992 Jun; 31(25):5799-808. PubMed ID: 1610825
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]