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Results: 1-14 |
Results: 14
EPR study of the semiquinone biradical Q(A)(center dot-)Q(B)(center dot-) in photosynthetic reaction centers of Rhodobacter sphaeroides at 326 GHz: Determination of the exchange interaction J(o)
Authors: Calvo, R Isaacson, RA Paddock, ML Abresch, EC Okamura, MY Maniero, AL Brunel, LC Feher, G
Citation: R. Calvo et al., EPR study of the semiquinone biradical Q(A)(center dot-)Q(B)(center dot-) in photosynthetic reaction centers of Rhodobacter sphaeroides at 326 GHz: Determination of the exchange interaction J(o), J PHYS CH B, 105(19), 2001, pp. 4053-4057
Identification of the proton pathway in bacterial reaction centers: Decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors
Authors: Adelroth, P Paddock, ML Tehrani, A Beatty, JT Feher, G Okamura, MY
Citation: P. Adelroth et al., Identification of the proton pathway in bacterial reaction centers: Decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors, BIOCHEM, 40(48), 2001, pp. 14538-14546
Simultaneous replacement of Asp-L210 and Asp-M17 with Asn increases protonuptake by Glu-L212 upon first electron transfer to Q(B) in reaction centers from Rhodobacter sphaeroides
Authors: Nabedryk, E Breton, J Okamura, MY Paddock, ML
Citation: E. Nabedryk et al., Simultaneous replacement of Asp-L210 and Asp-M17 with Asn increases protonuptake by Glu-L212 upon first electron transfer to Q(B) in reaction centers from Rhodobacter sphaeroides, BIOCHEM, 40(46), 2001, pp. 13826-13832
Interaction between cytochrome c(2) and the photosynthetic reaction centerfrom Rhodobacter sphaeroides: Effects of charge-modifying mutations on binding and electron transfer
Authors: Tetreault, M Rongey, SH Feher, G Okamura, MY
Citation: M. Tetreault et al., Interaction between cytochrome c(2) and the photosynthetic reaction centerfrom Rhodobacter sphaeroides: Effects of charge-modifying mutations on binding and electron transfer, BIOCHEM, 40(29), 2001, pp. 8452-8462
Identification of the proton pathway in bacterial reaction centers: Cooperation between Asp-M17 and Asp-L210 facilitates proton transfer to the secondary quinone (Q(B))
Authors: Paddock, ML Adelroth, P Chang, C Abresch, EC Feher, G Okamura, MY
Citation: Ml. Paddock et al., Identification of the proton pathway in bacterial reaction centers: Cooperation between Asp-M17 and Asp-L210 facilitates proton transfer to the secondary quinone (Q(B)), BIOCHEM, 40(23), 2001, pp. 6893-6902
Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers (vol 97, pg 1542, 2000)
Authors: Axelrod, HL Abresch, EC Paddock, ML Okamura, MY Feher, G
Citation: Hl. Axelrod et al., Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers (vol 97, pg 1542, 2000), P NAS US, 97(8), 2000, pp. 4410-4410
Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers
Authors: Axelrod, HL Abresch, EC Paddock, ML Okamura, MY Feher, G
Citation: Hl. Axelrod et al., Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers, P NAS US, 97(4), 2000, pp. 1542-1547
Identification of the proton pathway in bacterial reaction centers: Replacement of Asp-M17 and Asp-L210 with Asn reduces the proton transfer rate in the presence of Cd2+
Authors: Paddock, ML Feher, G Okamura, MY
Citation: Ml. Paddock et al., Identification of the proton pathway in bacterial reaction centers: Replacement of Asp-M17 and Asp-L210 with Asn reduces the proton transfer rate in the presence of Cd2+, P NAS US, 97(4), 2000, pp. 1548-1553
Identification of the proton pathway in bacterial reaction centers: Both protons associated with reduction of Q(B) to Q(B)H(2) share a common entry point
Authors: Adelroth, P Paddock, ML Sagle, LB Feher, G Okamura, MY
Citation: P. Adelroth et al., Identification of the proton pathway in bacterial reaction centers: Both protons associated with reduction of Q(B) to Q(B)H(2) share a common entry point, P NAS US, 97(24), 2000, pp. 13086-13091
Proton and electron transfer in bacterial reaction centers
Authors: Okamura, MY Paddock, ML Graige, MS Feher, G
Citation: My. Okamura et al., Proton and electron transfer in bacterial reaction centers, BBA-BIOENER, 1458(1), 2000, pp. 148-163
EPR study of the molecular and electronic structure of the semiquinone biradical Q(A)(-center dot) Q(B)(-center dot) in photosynthetic reaction centers from Rhodobacter sphaeroides
Authors: Calvo, R Abresch, EC Bittl, R Feher, G Hofbauer, W Isaacson, RA Lubitz, W Okamura, MY Paddock, ML
Citation: R. Calvo et al., EPR study of the molecular and electronic structure of the semiquinone biradical Q(A)(-center dot) Q(B)(-center dot) in photosynthetic reaction centers from Rhodobacter sphaeroides, J AM CHEM S, 122(30), 2000, pp. 7327-7341
The primary and secondary acceptors in bacterial photosynthesis: II. The structure of the Fe2+-Q(-) complex
Authors: Feher, G Okamura, MY
Citation: G. Feher et My. Okamura, The primary and secondary acceptors in bacterial photosynthesis: II. The structure of the Fe2+-Q(-) complex, APPL MAGN R, 16(1), 1999, pp. 63-100
Identification of the proton pathway in bacterial reaction centers: Inhibition of proton transfer by binding of Zn2+ or Cd2+
Authors: Paddock, ML Graige, MS Feher, G Okamura, MY
Citation: Ml. Paddock et al., Identification of the proton pathway in bacterial reaction centers: Inhibition of proton transfer by binding of Zn2+ or Cd2+, P NAS US, 96(11), 1999, pp. 6183-6188
Observation of the protonated semiquinone intermediate in isolated reaction centers from Rhodobacter sphaeroides: Implications for the mechanism of electron and proton transfer in proteins
Authors: Graige, MS Paddock, ML Feher, G Okamura, MY
Citation: Ms. Graige et al., Observation of the protonated semiquinone intermediate in isolated reaction centers from Rhodobacter sphaeroides: Implications for the mechanism of electron and proton transfer in proteins, BIOCHEM, 38(35), 1999, pp. 11465-11473
Risultati: 1-14 |