Time-resolved X-, K-, and W-band EPR of the radical pair state P700 •+A1 •- of photosystem I in comparison with P865 •+QA •- in bacterial reaction centers

A. Van Der Est, T. Prisner, R. Bittl, Petra Fromme, W. Lubitz, K. Möbius, D. Stehlik

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Abstract

The spin-polarized EPR spectra at 95 GHz (W-band), 24 GHz (K-band), and 9 GHz (X-band) of the radical pair P700 •+A1 •- in highly purified photosystem I particles are presented. The spectra are analyzed to obtain both the magnetic parameters of the radical pair as well as the relative orientation of the two species. From the analysis, the g-tensor of A1 •- is found to be gxx = 2.0062, gyy = 2.0051, and gzz = 2.0022, and it is shown that A1 is oriented such that the carbonyl bonds are parallel to the vector joining the centers of P700 •+ and A1 •-. The anisotropy of the g-tensor is considerably larger than that obtained for chemically reduced phylloquinone in frozen 2-propanol solution. Possible reasons for this difference and their implications for the A1 binding site are discussed. The relative orientation of P700 •+ and A1•- is compared with earlier estimates obtained using less accurate g-values for A1 •1. A comparison with the spectra of P865 •+QA •- in bacterial reaction centers (bRCs) of Rhodobacter sphaeroides R-26 in which the nonheme iron has been replaced by zinc (Zn-bRCs) allows the structural and magnetic properties of the charge-separated state in the two systems to be compared. From the similarity of the two W-band spectra in the region around the free electron g-value it is clear that the dipolar vector, Zd, between P•+ and QA •-/A1 •- has a similar orientation relative to P700 in PS I and P865 in bRCs. This is compatible with the similar overall structural arrangement of P700 and P865. In contrast, the low-field parts of the two spectra are very different as a result of differences in the orientation of A1 and QA with respect to zd.

Original languageEnglish
Pages (from-to)1437-1443
Number of pages7
JournalJournal of Physical Chemistry B
Volume101
Issue number8
Publication statusPublished - Feb 20 1997

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Photosystem I Protein Complex
Tensors
Paramagnetic resonance
Vitamin K 1
2-Propanol
Propanol
Binding sites
Joining
Zinc
Structural properties
Magnetic properties
Anisotropy
Iron
Binding Sites
phylloquinone
Electrons
tensors
extremely high frequencies
superhigh frequencies
free electrons

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Engineering(all)

Cite this

Time-resolved X-, K-, and W-band EPR of the radical pair state P700 •+A1 •- of photosystem I in comparison with P865 •+QA •- in bacterial reaction centers. / Van Der Est, A.; Prisner, T.; Bittl, R.; Fromme, Petra; Lubitz, W.; Möbius, K.; Stehlik, D.

In: Journal of Physical Chemistry B, Vol. 101, No. 8, 20.02.1997, p. 1437-1443.

Research output: Contribution to journalArticle

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abstract = "The spin-polarized EPR spectra at 95 GHz (W-band), 24 GHz (K-band), and 9 GHz (X-band) of the radical pair P700 •+A1 •- in highly purified photosystem I particles are presented. The spectra are analyzed to obtain both the magnetic parameters of the radical pair as well as the relative orientation of the two species. From the analysis, the g-tensor of A1 •- is found to be gxx = 2.0062, gyy = 2.0051, and gzz = 2.0022, and it is shown that A1 is oriented such that the carbonyl bonds are parallel to the vector joining the centers of P700 •+ and A1 •-. The anisotropy of the g-tensor is considerably larger than that obtained for chemically reduced phylloquinone in frozen 2-propanol solution. Possible reasons for this difference and their implications for the A1 binding site are discussed. The relative orientation of P700 •+ and A1•- is compared with earlier estimates obtained using less accurate g-values for A1 •1. A comparison with the spectra of P865 •+QA •- in bacterial reaction centers (bRCs) of Rhodobacter sphaeroides R-26 in which the nonheme iron has been replaced by zinc (Zn-bRCs) allows the structural and magnetic properties of the charge-separated state in the two systems to be compared. From the similarity of the two W-band spectra in the region around the free electron g-value it is clear that the dipolar vector, Zd, between P•+ and QA •-/A1 •- has a similar orientation relative to P700 in PS I and P865 in bRCs. This is compatible with the similar overall structural arrangement of P700 and P865. In contrast, the low-field parts of the two spectra are very different as a result of differences in the orientation of A1 and QA with respect to zd.",
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T1 - Time-resolved X-, K-, and W-band EPR of the radical pair state P700 •+A1 •- of photosystem I in comparison with P865 •+QA •- in bacterial reaction centers

AU - Van Der Est, A.

AU - Prisner, T.

AU - Bittl, R.

AU - Fromme, Petra

AU - Lubitz, W.

AU - Möbius, K.

AU - Stehlik, D.

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N2 - The spin-polarized EPR spectra at 95 GHz (W-band), 24 GHz (K-band), and 9 GHz (X-band) of the radical pair P700 •+A1 •- in highly purified photosystem I particles are presented. The spectra are analyzed to obtain both the magnetic parameters of the radical pair as well as the relative orientation of the two species. From the analysis, the g-tensor of A1 •- is found to be gxx = 2.0062, gyy = 2.0051, and gzz = 2.0022, and it is shown that A1 is oriented such that the carbonyl bonds are parallel to the vector joining the centers of P700 •+ and A1 •-. The anisotropy of the g-tensor is considerably larger than that obtained for chemically reduced phylloquinone in frozen 2-propanol solution. Possible reasons for this difference and their implications for the A1 binding site are discussed. The relative orientation of P700 •+ and A1•- is compared with earlier estimates obtained using less accurate g-values for A1 •1. A comparison with the spectra of P865 •+QA •- in bacterial reaction centers (bRCs) of Rhodobacter sphaeroides R-26 in which the nonheme iron has been replaced by zinc (Zn-bRCs) allows the structural and magnetic properties of the charge-separated state in the two systems to be compared. From the similarity of the two W-band spectra in the region around the free electron g-value it is clear that the dipolar vector, Zd, between P•+ and QA •-/A1 •- has a similar orientation relative to P700 in PS I and P865 in bRCs. This is compatible with the similar overall structural arrangement of P700 and P865. In contrast, the low-field parts of the two spectra are very different as a result of differences in the orientation of A1 and QA with respect to zd.

AB - The spin-polarized EPR spectra at 95 GHz (W-band), 24 GHz (K-band), and 9 GHz (X-band) of the radical pair P700 •+A1 •- in highly purified photosystem I particles are presented. The spectra are analyzed to obtain both the magnetic parameters of the radical pair as well as the relative orientation of the two species. From the analysis, the g-tensor of A1 •- is found to be gxx = 2.0062, gyy = 2.0051, and gzz = 2.0022, and it is shown that A1 is oriented such that the carbonyl bonds are parallel to the vector joining the centers of P700 •+ and A1 •-. The anisotropy of the g-tensor is considerably larger than that obtained for chemically reduced phylloquinone in frozen 2-propanol solution. Possible reasons for this difference and their implications for the A1 binding site are discussed. The relative orientation of P700 •+ and A1•- is compared with earlier estimates obtained using less accurate g-values for A1 •1. A comparison with the spectra of P865 •+QA •- in bacterial reaction centers (bRCs) of Rhodobacter sphaeroides R-26 in which the nonheme iron has been replaced by zinc (Zn-bRCs) allows the structural and magnetic properties of the charge-separated state in the two systems to be compared. From the similarity of the two W-band spectra in the region around the free electron g-value it is clear that the dipolar vector, Zd, between P•+ and QA •-/A1 •- has a similar orientation relative to P700 in PS I and P865 in bRCs. This is compatible with the similar overall structural arrangement of P700 and P865. In contrast, the low-field parts of the two spectra are very different as a result of differences in the orientation of A1 and QA with respect to zd.

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