Comparison of M-side electron transfer in Rb. sphaeroides and Rb. capsulatus reaction centers

Journal of Physical Chemistry B

Volumn 106, Issue 7, 2002, Pages 1799-1808

  Kirmaier, Christine ^a   Laible, Philip D ^b   Czarnecki, Kazimierz ^c   Hata, Aaron N ^b   Hanson, Deborah K ^b   Bocian, David F ^c   Holten, Dewey ^a  

^a WASHINGTON UNIVERSITY   (United States)

^b ARGONNE NATIONAL LABORATORY   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON TRANSFER; RESONANCE RAMAN STUDIES;

ABSORPTION; FREE ENERGY; GROUND STATE; PROTEINS; QUANTUM THEORY; REDUCTION; RESONANCE;

REACTION KINETICS;

EID: 0037149090     PISSN: 10895647     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp013264w     Document Type: Article

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40. -) Similarly, electron transfer to QA is slowed because of the larger distance involved.
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43. L with such water molecules should not contribute significantly because such bonding is not commensurate with the vibrational data on wt RCs or the G(M201)D mutant (at least when P is neutral). (b) Fyfe, P.K.; Ridge, J.P.; McAuley, K.E.; Cogdell, R.J.; Isaacs, N.W.; Jones, M.R Biochemistry 2000, 39, 5953-5960. (c) Lutz, M.; Robert, B. In Biological Applications or Raman Spectroscopy; Spiro, T.G., Ed.; Wiley: New York, 1988; Vol 3, pp 347-411. (d) Lutz, M.; Mantele, W. In Chlorophylls; Scheer, H., Ed.; CRC Press: Boca Raton, FL, 1991; pp 855-902. (e) Lutz, M. Biospectroscopy 1995, 1, 313-327. (f) Palanniappan, V.; Bocian, D.F. J. Am. Chem. Soc. 1995, 117, 3647-3648.
44. L with such water molecules should not contribute significantly because such bonding is not commensurate with the vibrational data on wt RCs or the G(M201)D mutant (at least when P is neutral). (b) Fyfe, P.K.; Ridge, J.P.; McAuley, K.E.; Cogdell, R.J.; Isaacs, N.W.; Jones, M.R Biochemistry 2000, 39, 5953-5960. (c) Lutz, M.; Robert, B. In Biological Applications or Raman Spectroscopy; Spiro, T.G., Ed.; Wiley: New York, 1988; Vol 3, pp 347-411. (d) Lutz, M.; Mantele, W. In Chlorophylls; Scheer, H., Ed.; CRC Press: Boca Raton, FL, 1991; pp 855-902. (e) Lutz, M. Biospectroscopy 1995, 1, 313-327. (f) Palanniappan, V.; Bocian, D.F. J. Am. Chem. Soc. 1995, 117, 3647-3648.
45. L with such water molecules should not contribute significantly because such bonding is not commensurate with the vibrational data on wt RCs or the G(M201)D mutant (at least when P is neutral). (b) Fyfe, P.K.; Ridge, J.P.; McAuley, K.E.; Cogdell, R.J.; Isaacs, N.W.; Jones, M.R Biochemistry 2000, 39, 5953-5960. (c) Lutz, M.; Robert, B. In Biological Applications or Raman Spectroscopy; Spiro, T.G., Ed.; Wiley: New York, 1988; Vol 3, pp 347-411. (d) Lutz, M.; Mantele, W. In Chlorophylls; Scheer, H., Ed.; CRC Press: Boca Raton, FL, 1991; pp 855-902. (e) Lutz, M. Biospectroscopy 1995, 1, 313-327. (f) Palanniappan, V.; Bocian, D.F. J. Am. Chem. Soc. 1995, 117, 3647-3648.
46. L with such water molecules should not contribute significantly because such bonding is not commensurate with the vibrational data on wt RCs or the G(M201)D mutant (at least when P is neutral). (b) Fyfe, P.K.; Ridge, J.P.; McAuley, K.E.; Cogdell, R.J.; Isaacs, N.W.; Jones, M.R Biochemistry 2000, 39, 5953-5960. (c) Lutz, M.; Robert, B. In Biological Applications or Raman Spectroscopy; Spiro, T.G., Ed.; Wiley: New York, 1988; Vol 3, pp 347-411. (d) Lutz, M.; Mantele, W. In Chlorophylls; Scheer, H., Ed.; CRC Press: Boca Raton, FL, 1991; pp 855-902. (e) Lutz, M. Biospectroscopy 1995, 1, 313-327. (f) Palanniappan, V.; Bocian, D.F. J. Am. Chem. Soc. 1995, 117, 3647-3648.
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77. - formation in Rb. sphaeroides than Rb. capsulatus.
78. - and thus its contribution at 3 ns, as noted previously for other mutants.
79. 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 anion region 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.
80. (a) The amplitude spectra in Figure 6 (insets) 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.
81. +.
82. Fajer, J., Borg, D.C.; Forman, A., Dolphin, D.; Felton, R.H. J. Am. Chem. Soc. 1973, 95, 42 739.
83. L/β (see ref 9b).
84. L/β (see ref 9b).
85. L/β (see ref 9b).
86. -). Such delayed P* stimulated emission was also found previously for the analogous Rb. capsulatus DH mutant at 77 K (lifetime 470 ± 80) ps.
87. -1; not shown).
88. -1 bands by a small amount.
89. An effective rate constant for electron transfer to each branch is used in the simple kinetic model because one- and two-step mechanisms are operative in parallel to an extent depending on the branch and the RC.
90. - drops below P* as a result of genetic manipulation of the RC.
91. (a) Kirmaier, C.; Holten, D. Proc. Natl. Acad. Sci. U.S.A. 1990, 97, 3522-3556.
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93. The absorption band of P can be shifted from ∼830 to ∼850 nm (corresponding to an ∼0.03 eV difference in the P* energy) by altering a series of nearby amino acid residues, with no measurable change in the rate constant for electron transfer to the L branch; Eastman, J.E.; Taguchi, A.K.W.; Lin, S.; Jackson, J.A.; Woodbury, N.W. Biochemistry 2000, 39, 14787-14789.