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Volumn 106, Issue 2, 2002, Pages 495-503

Probing M-branch electron transfer and cofactor environment in the bacterial photosynthetic reaction center by addition of a hydrogen bond to the M-side bacteriopheophytin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL REACTION CENTERS;

EID: 0037123068     PISSN: 10895647     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp012768r     Document Type: Article
Times cited : (35)

References (89)
  • 18
    • 0011203505 scopus 로고    scopus 로고
    • note
    • L with such water molecules will not contribute since such bonding is not commensurate with the vibrational data on wt RCs or the G(M201)D mutant (at least when P is neutral).
  • 22
    • 0000885678 scopus 로고
    • Scheer, H., Ed.; CRC Press: Boca Raton, FL
    • (b) Lutz, M.; Mantele, W. In Chlorophylls; Scheer, H., Ed.; CRC Press: Boca Raton, FL, 1991; pp 855-902.
    • (1991) Chlorophylls , pp. 855-902
    • Lutz, M.1    Mantele, W.2
  • 29
    • 0011169565 scopus 로고    scopus 로고
    • note
    • L as a result of the "beta" or "H" mutation L(M214)H in Rb. sphaeroides.
  • 51
    • 0011250502 scopus 로고    scopus 로고
    • note
    • Because the data extend to only 3.8 ns and this at best is about four 1/e times of the slower component, the error in the associated time constant for the longer-lived component in the anion region and P-bleaching decay is much larger than indicated by simple best fits (1.0 ± 0.4 ns and 1.2 ± 0.4 ns, respectively). For example, in the anion region, holding the slow component fixed at 1.5, 2.0, 2.5, or 3.0 ns gives visually good fits to the gion data in Figure 6, with the value of the faster time constant only marginally changed. The use of time constants longer than about 4 ns for the slow component gives poorer fits and unreasonable spectra at the asymptote of the decay. These considerations suggest that the time constant of the slower component is likely in the 1-4 ns range. This behavior parallels that previously observed for the DH and KDH mutants.
  • 52
    • 0011198741 scopus 로고    scopus 로고
    • note
    • - formation (Figure 2B).
  • 53
    • 0011214760 scopus 로고    scopus 로고
    • note
    • (a) The amplitude spectra in Figure 7 were generated from fits in which the value of the longer component was held fixed at 2.5 ns. Varying this time constant between 1.0 and 3.5 ns does not appreciably affect the derived spectra.
  • 54
    • 0011227950 scopus 로고    scopus 로고
    • note
    • +.
  • 55
    • 0011237168 scopus 로고    scopus 로고
    • note
    • -1; not shown).
  • 56
    • 0011175408 scopus 로고    scopus 로고
    • note
    • Y excited states of the chromophores (via origin shifts and/or dephasing times of certain modes). These particular excited-state properties are outside the scope of this paper. Inspection of the RR data shown in Figures 8 and 9 clearly shows that the RR intensities of the V(M131)D versus wild-type RCs are different at a given excitation wavelength. This observation is similar to that made in previous RR studies of genetically modified RCs. These studies have shown that the RR intensities of the cofactors can be significantly affected by altering protein residues in the vicinity of a particular cofactor, even in cases when the genetic modification does not affect the ground-state absorption features or vibrational frequencies of the cofactor to any appreciable extent.
  • 58
    • 0011211375 scopus 로고    scopus 로고
    • note
    • - occurs in the Rb. sphaeroides DH mutant but with a yield of only ∼7%, half that found in the Rb. capsulatus DH mutant.
  • 59
    • 0011228114 scopus 로고    scopus 로고
    • note
    • M has been replaced by a BPh, an Rb. capsulatus mutant involving alterations/ swapping of large sections of the L and M polypeptides, and Rb. capsulatus wild-type RCs at low temperature at high excitation intensities.
  • 63
    • 0021805950 scopus 로고
    • - has been produced in steady-state photochemical trapping experiments: Robert, B.; Tiede, D.M.; Lutz, M. FEBS Lett. 1985, 183, 326-330. Kellogg, E.C.; Kolaczkowski, S.; Wasiewlewski, M.R.; Tiede, D.M. Photosynth. Res. 1989, 22, 47-59. Gray, K.A.; Wachtveitl, J.; Oesterhelt, D. Eur. J. Biochem. 1992, 207, 723-731.
    • (1985) FEBS Lett. , vol.183 , pp. 326-330
    • Robert, B.1    Tiede, D.M.2    Lutz, M.3
  • 64
    • 0002839430 scopus 로고
    • - has been produced in steady-state photochemical trapping experiments: Robert, B.; Tiede, D.M.; Lutz, M. FEBS Lett. 1985, 183, 326-330. Kellogg, E.C.; Kolaczkowski, S.; Wasiewlewski, M.R.; Tiede, D.M. Photosynth. Res. 1989, 22, 47-59. Gray, K.A.; Wachtveitl, J.; Oesterhelt, D. Eur. J. Biochem. 1992, 207, 723-731.
    • (1989) Photosynth. Res. , vol.22 , pp. 47-59
    • Kellogg, E.C.1    Kolaczkowski, S.2    Wasiewlewski, M.R.3    Tiede, D.M.4
  • 65
    • 0026769095 scopus 로고
    • - has been produced in steady-state photochemical trapping experiments: Robert, B.; Tiede, D.M.; Lutz, M. FEBS Lett. 1985, 183, 326-330. Kellogg, E.C.; Kolaczkowski, S.; Wasiewlewski, M.R.; Tiede, D.M. Photosynth. Res. 1989, 22, 47-59. Gray, K.A.; Wachtveitl, J.; Oesterhelt, D. Eur. J. Biochem. 1992, 207, 723-731.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 723-731
    • Gray, K.A.1    Wachtveitl, J.2    Oesterhelt, D.3
  • 66
    • 0011250504 scopus 로고    scopus 로고
    • note
    • Calculations on hydrogen bonding to the ring V keto group of a BPh and experimental results on manipulation of hydrogen bonds to P indicate that these hydrogen bonds generally shift the redox properties of the cofactors by 50-80 mV.
  • 85
    • 0011175816 scopus 로고    scopus 로고
    • note
    • L in the Chloroflexus aurantiacus RC and the Rb. capsulatus E(L104)Q mutant, but that the hydrogen bond to Gln is not as strong as that to Glu in wild-type Rb. capsulatus (and Rb. sphaeroides).
  • 87
    • 0002312013 scopus 로고
    • Dolphin, D., Ed.; Academic Press: New York
    • Gouterman, M. In The Porphyrins; Dolphin, D., Ed.; Academic Press: New York, 1978; Vol III, pp 1-165.
    • (1978) Porphyrins , vol.3 , pp. 1-165
    • Gouterman, M.1


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