Correlation between multiple hydrogen bonding and alteration of the oxidation potential of the bacteriochlorophyll dimer of reaction centers from Rhodobacter sphaeroides

T. A. Mattioli, X. Lin, James Paul Allen, J. C. Williams

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Abstract

The electronic absorption and vibrational Raman spectra of mutant reaction centers from Rhodobacter sphaeroides beating multiple site-specific mutations near the primary electron donor (P), a bacteriochlorophyll dimer, are reported. These mutations bear double and triple combinations of single- point mutations that alter the H-bonding interactions between histidine residues and the C2- and C9-conjugated carbonyl groups of the primary donor [Mattioli, T. A., Williams, J. C., Allen, J. P., and Robert, B. (1994) Biochemistry 33, 1636-1643] and change the donor redox midpoint potential from 410 to 765 mV compared to 505 mV for wild type [Lin, X. Murchison, H. A., Nagarajan, V., Parson, W. W., Williams, J. C., and Allen, J. P. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 10265-10269]. Near-infrared Fourier transform Raman spectroscopy was used to determine the changes in H-bonding interactions of the primary donor in these multiple mutants. The Fourier transform Raman spectra of the mutants exhibit the predicted changes in hydrogen bond interactions of the P carbonyl groups with the protein, and they are consistent with the designed mutations. Moreover, the Raman data verify that the H-bonds formed or broken in the multiple mutants are similar in strength to those observed in the corresponding single mutants. A correlation was observed between the change in P/P·+ redox midpoint potential and the total change in H-bonding interaction energy (from -207 to 364 meV relative to wild type) as gauged by the estimated enthalpy of each H- bond formed or broken on the four conjugated carbonyls of the primary donor. Only minor changes were observed in the optical spectra of the mutant reaction centers, indicating that the addition of H-bonds from histidines has little effect in destabilizing the first electronic excited state of the dimer relative to the ground state. However a blue shift in the dimer absorption band at ca. 890 nm at 20 K was associated with the removal of the H-bond to the C2 acetyl carbonyl group via His L168. A red shift of the oxidized dimer band at ca. 1250 nm was associated with the formation of each H-bond to the C9 keto carbonyl groups.

Original languageEnglish
Pages (from-to)6142-6152
Number of pages11
JournalBiochemistry
Volume34
Issue number18
Publication statusPublished - 1995

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Bacteriochlorophylls
Rhodobacter sphaeroides
Hydrogen Bonding
Dimers
Hydrogen bonds
Fourier Analysis
Histidine
Oxidation
Mutation
Oxidation-Reduction
Raman scattering
Fourier transforms
Raman Spectrum Analysis
Point Mutation
Biochemistry
Hydrogen
Excited states
Electrons
Ground state
Raman spectroscopy

ASJC Scopus subject areas

  • Biochemistry

Cite this

Correlation between multiple hydrogen bonding and alteration of the oxidation potential of the bacteriochlorophyll dimer of reaction centers from Rhodobacter sphaeroides. / Mattioli, T. A.; Lin, X.; Allen, James Paul; Williams, J. C.

In: Biochemistry, Vol. 34, No. 18, 1995, p. 6142-6152.

Research output: Contribution to journalArticle

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title = "Correlation between multiple hydrogen bonding and alteration of the oxidation potential of the bacteriochlorophyll dimer of reaction centers from Rhodobacter sphaeroides",
abstract = "The electronic absorption and vibrational Raman spectra of mutant reaction centers from Rhodobacter sphaeroides beating multiple site-specific mutations near the primary electron donor (P), a bacteriochlorophyll dimer, are reported. These mutations bear double and triple combinations of single- point mutations that alter the H-bonding interactions between histidine residues and the C2- and C9-conjugated carbonyl groups of the primary donor [Mattioli, T. A., Williams, J. C., Allen, J. P., and Robert, B. (1994) Biochemistry 33, 1636-1643] and change the donor redox midpoint potential from 410 to 765 mV compared to 505 mV for wild type [Lin, X. Murchison, H. A., Nagarajan, V., Parson, W. W., Williams, J. C., and Allen, J. P. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 10265-10269]. Near-infrared Fourier transform Raman spectroscopy was used to determine the changes in H-bonding interactions of the primary donor in these multiple mutants. The Fourier transform Raman spectra of the mutants exhibit the predicted changes in hydrogen bond interactions of the P carbonyl groups with the protein, and they are consistent with the designed mutations. Moreover, the Raman data verify that the H-bonds formed or broken in the multiple mutants are similar in strength to those observed in the corresponding single mutants. A correlation was observed between the change in P/P·+ redox midpoint potential and the total change in H-bonding interaction energy (from -207 to 364 meV relative to wild type) as gauged by the estimated enthalpy of each H- bond formed or broken on the four conjugated carbonyls of the primary donor. Only minor changes were observed in the optical spectra of the mutant reaction centers, indicating that the addition of H-bonds from histidines has little effect in destabilizing the first electronic excited state of the dimer relative to the ground state. However a blue shift in the dimer absorption band at ca. 890 nm at 20 K was associated with the removal of the H-bond to the C2 acetyl carbonyl group via His L168. A red shift of the oxidized dimer band at ca. 1250 nm was associated with the formation of each H-bond to the C9 keto carbonyl groups.",
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T1 - Correlation between multiple hydrogen bonding and alteration of the oxidation potential of the bacteriochlorophyll dimer of reaction centers from Rhodobacter sphaeroides

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AU - Allen, James Paul

AU - Williams, J. C.

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N2 - The electronic absorption and vibrational Raman spectra of mutant reaction centers from Rhodobacter sphaeroides beating multiple site-specific mutations near the primary electron donor (P), a bacteriochlorophyll dimer, are reported. These mutations bear double and triple combinations of single- point mutations that alter the H-bonding interactions between histidine residues and the C2- and C9-conjugated carbonyl groups of the primary donor [Mattioli, T. A., Williams, J. C., Allen, J. P., and Robert, B. (1994) Biochemistry 33, 1636-1643] and change the donor redox midpoint potential from 410 to 765 mV compared to 505 mV for wild type [Lin, X. Murchison, H. A., Nagarajan, V., Parson, W. W., Williams, J. C., and Allen, J. P. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 10265-10269]. Near-infrared Fourier transform Raman spectroscopy was used to determine the changes in H-bonding interactions of the primary donor in these multiple mutants. The Fourier transform Raman spectra of the mutants exhibit the predicted changes in hydrogen bond interactions of the P carbonyl groups with the protein, and they are consistent with the designed mutations. Moreover, the Raman data verify that the H-bonds formed or broken in the multiple mutants are similar in strength to those observed in the corresponding single mutants. A correlation was observed between the change in P/P·+ redox midpoint potential and the total change in H-bonding interaction energy (from -207 to 364 meV relative to wild type) as gauged by the estimated enthalpy of each H- bond formed or broken on the four conjugated carbonyls of the primary donor. Only minor changes were observed in the optical spectra of the mutant reaction centers, indicating that the addition of H-bonds from histidines has little effect in destabilizing the first electronic excited state of the dimer relative to the ground state. However a blue shift in the dimer absorption band at ca. 890 nm at 20 K was associated with the removal of the H-bond to the C2 acetyl carbonyl group via His L168. A red shift of the oxidized dimer band at ca. 1250 nm was associated with the formation of each H-bond to the C9 keto carbonyl groups.

AB - The electronic absorption and vibrational Raman spectra of mutant reaction centers from Rhodobacter sphaeroides beating multiple site-specific mutations near the primary electron donor (P), a bacteriochlorophyll dimer, are reported. These mutations bear double and triple combinations of single- point mutations that alter the H-bonding interactions between histidine residues and the C2- and C9-conjugated carbonyl groups of the primary donor [Mattioli, T. A., Williams, J. C., Allen, J. P., and Robert, B. (1994) Biochemistry 33, 1636-1643] and change the donor redox midpoint potential from 410 to 765 mV compared to 505 mV for wild type [Lin, X. Murchison, H. A., Nagarajan, V., Parson, W. W., Williams, J. C., and Allen, J. P. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 10265-10269]. Near-infrared Fourier transform Raman spectroscopy was used to determine the changes in H-bonding interactions of the primary donor in these multiple mutants. The Fourier transform Raman spectra of the mutants exhibit the predicted changes in hydrogen bond interactions of the P carbonyl groups with the protein, and they are consistent with the designed mutations. Moreover, the Raman data verify that the H-bonds formed or broken in the multiple mutants are similar in strength to those observed in the corresponding single mutants. A correlation was observed between the change in P/P·+ redox midpoint potential and the total change in H-bonding interaction energy (from -207 to 364 meV relative to wild type) as gauged by the estimated enthalpy of each H- bond formed or broken on the four conjugated carbonyls of the primary donor. Only minor changes were observed in the optical spectra of the mutant reaction centers, indicating that the addition of H-bonds from histidines has little effect in destabilizing the first electronic excited state of the dimer relative to the ground state. However a blue shift in the dimer absorption band at ca. 890 nm at 20 K was associated with the removal of the H-bond to the C2 acetyl carbonyl group via His L168. A red shift of the oxidized dimer band at ca. 1250 nm was associated with the formation of each H-bond to the C9 keto carbonyl groups.

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