Alteration of the axial met ligand to electron acceptor A0 in photosystem I

An investigation of electron transfer at different temperatures by multifrequency time-resolved and CW EPR

Art van der Est, Sara Chirico, Irina Karyagina, Rachel Cohen, Gaozhong Shen, John H. Golbeck

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The ambient temperature and low-temperature electron transfer properties of Photosystem I (PS I) from the M688NPsaA and M668NPsaB mutant strains of the cyanobacterium Synechocystis sp. PCC 6803 are studied using transient electron paramagnetic resonance (EPR) and continuous-wave (CW) EPR. The two mutations are expected to alter the midpoint potentials of, and the reorganization energies around, the primary electron chlorophyll acceptors A0A and A0B, which should lead to a change in the yield and/or rate of electron transfer to the phylloquinone acceptors A1A and A1B, respectively. At ambient temperature it is known that both quinone acceptors are active in electron transfer. At low temperature there are at least two fractions that undergo either reversible or irreversible electron transfer. The EPR data of the two PS I variants are used to investigate the relationship between these low-temperature fractions and the ambient temperature electron transfer pathway. The results show that mutation in the PsaA-branch increases the rate of A- iA to FX electron transfer at ambient temperature, while the corresponding mutation in the PsaB-branch has no effect on the electron transfer rate observable by transient EPR. An analysis of the complete time/field datasets from both variants suggests that the yield of electron transfer in the branch carrying the mutation is reduced. The mutations have no effect on the low-temperature CW EPR spectra of the iron-sulfur clusters if the samples are frozen under illumination but they both cause a decrease in the yield of reduced FA and FB if the samples are frozen in the dark and then illuminated. The PsaA-branch mutation greatly reduces the intensity and changes the polarization pattern of the radical pair P+ 700A.- iA to FX. Possible causes of the changes in the polarization pattern are discussed and it is suggested that the mutations introduce structural heterogeneity in the vicinity of the A0 binding site. No clear correlation between the yield of electron transfer in a particular branch and the yield of stable charge separation is found.

Original languageEnglish (US)
Pages (from-to)103-121
Number of pages19
JournalApplied Magnetic Resonance
Volume37
Issue number1
DOIs
StatePublished - Jan 1 2010

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continuous radiation
electron paramagnetic resonance
electron transfer
mutations
ligands
ambient temperature
electrons
temperature
phylloquinone
causes
quinones
chlorophylls
polarization
polarization (charge separation)
sulfur
illumination
iron

All Science Journal Classification (ASJC) codes

  • Atomic and Molecular Physics, and Optics

Cite this

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title = "Alteration of the axial met ligand to electron acceptor A0 in photosystem I: An investigation of electron transfer at different temperatures by multifrequency time-resolved and CW EPR",
abstract = "The ambient temperature and low-temperature electron transfer properties of Photosystem I (PS I) from the M688NPsaA and M668NPsaB mutant strains of the cyanobacterium Synechocystis sp. PCC 6803 are studied using transient electron paramagnetic resonance (EPR) and continuous-wave (CW) EPR. The two mutations are expected to alter the midpoint potentials of, and the reorganization energies around, the primary electron chlorophyll acceptors A0A and A0B, which should lead to a change in the yield and/or rate of electron transfer to the phylloquinone acceptors A1A and A1B, respectively. At ambient temperature it is known that both quinone acceptors are active in electron transfer. At low temperature there are at least two fractions that undergo either reversible or irreversible electron transfer. The EPR data of the two PS I variants are used to investigate the relationship between these low-temperature fractions and the ambient temperature electron transfer pathway. The results show that mutation in the PsaA-branch increases the rate of A- iA to FX electron transfer at ambient temperature, while the corresponding mutation in the PsaB-branch has no effect on the electron transfer rate observable by transient EPR. An analysis of the complete time/field datasets from both variants suggests that the yield of electron transfer in the branch carrying the mutation is reduced. The mutations have no effect on the low-temperature CW EPR spectra of the iron-sulfur clusters if the samples are frozen under illumination but they both cause a decrease in the yield of reduced FA and FB if the samples are frozen in the dark and then illuminated. The PsaA-branch mutation greatly reduces the intensity and changes the polarization pattern of the radical pair P+ 700A.- iA to FX. Possible causes of the changes in the polarization pattern are discussed and it is suggested that the mutations introduce structural heterogeneity in the vicinity of the A0 binding site. No clear correlation between the yield of electron transfer in a particular branch and the yield of stable charge separation is found.",
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Alteration of the axial met ligand to electron acceptor A0 in photosystem I : An investigation of electron transfer at different temperatures by multifrequency time-resolved and CW EPR. / van der Est, Art; Chirico, Sara; Karyagina, Irina; Cohen, Rachel; Shen, Gaozhong; Golbeck, John H.

In: Applied Magnetic Resonance, Vol. 37, No. 1, 01.01.2010, p. 103-121.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Alteration of the axial met ligand to electron acceptor A0 in photosystem I

T2 - An investigation of electron transfer at different temperatures by multifrequency time-resolved and CW EPR

AU - van der Est, Art

AU - Chirico, Sara

AU - Karyagina, Irina

AU - Cohen, Rachel

AU - Shen, Gaozhong

AU - Golbeck, John H.

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AB - The ambient temperature and low-temperature electron transfer properties of Photosystem I (PS I) from the M688NPsaA and M668NPsaB mutant strains of the cyanobacterium Synechocystis sp. PCC 6803 are studied using transient electron paramagnetic resonance (EPR) and continuous-wave (CW) EPR. The two mutations are expected to alter the midpoint potentials of, and the reorganization energies around, the primary electron chlorophyll acceptors A0A and A0B, which should lead to a change in the yield and/or rate of electron transfer to the phylloquinone acceptors A1A and A1B, respectively. At ambient temperature it is known that both quinone acceptors are active in electron transfer. At low temperature there are at least two fractions that undergo either reversible or irreversible electron transfer. The EPR data of the two PS I variants are used to investigate the relationship between these low-temperature fractions and the ambient temperature electron transfer pathway. The results show that mutation in the PsaA-branch increases the rate of A- iA to FX electron transfer at ambient temperature, while the corresponding mutation in the PsaB-branch has no effect on the electron transfer rate observable by transient EPR. An analysis of the complete time/field datasets from both variants suggests that the yield of electron transfer in the branch carrying the mutation is reduced. The mutations have no effect on the low-temperature CW EPR spectra of the iron-sulfur clusters if the samples are frozen under illumination but they both cause a decrease in the yield of reduced FA and FB if the samples are frozen in the dark and then illuminated. The PsaA-branch mutation greatly reduces the intensity and changes the polarization pattern of the radical pair P+ 700A.- iA to FX. Possible causes of the changes in the polarization pattern are discussed and it is suggested that the mutations introduce structural heterogeneity in the vicinity of the A0 binding site. No clear correlation between the yield of electron transfer in a particular branch and the yield of stable charge separation is found.

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