A Comparison of the Manganese Center Responsible for Photosynthetic Water Oxidation in O2‐Evolving Core Particles and Photosystem II Enriched Membranes: EPR of the S2 State

M. Sivaraia, G Charles Dismukes

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Abstract

We have characterized the electron donors to Photosystem II (PS II) in an O2‐evolving reaction center core preparation from spinach (Ghanotakis, D.F.; Yocum, C.F. FEBS Lett., 1986, 197: 244–248) using EPR spectroscopy of the manganese center involved in water oxidation and of the tyrosine donor responsible for signal II. Both the 16‐line and the 19‐line form of the S2 multiline EPR signal can be observed in the core particles under conditions similar to those which produce these signals in PS II membranes. Consequently, the structure of the coupled cluster of three or four Mn ions remains intact in the core particles. The Kok parameters which characterize the number of reaction centers capable of advancing by 0, 1, or 2 equivalents in response to a short laser pulse are found to be the same in PS II membranes and in the core particles. Also, there is no evidence for partially inactivated centers which reach the S2 or S3 states, but which do not advance to O2 release. Thus the new class of highly resolved O2‐evolving particles appears to be well suited for biophysical studies directed at the mechanism of water oxidation.

Original languageEnglish
Pages (from-to)103-108
Number of pages6
JournalIsrael Journal of Chemistry
Volume28
Issue number2-3
DOIs
Publication statusPublished - Jan 1 1988

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Photosystem II Protein Complex
Manganese
Paramagnetic resonance
Membranes
Oxidation
Water
Tyrosine
Laser pulses
Spectroscopy
Ions
Electrons

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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title = "A Comparison of the Manganese Center Responsible for Photosynthetic Water Oxidation in O2‐Evolving Core Particles and Photosystem II Enriched Membranes: EPR of the S2 State",
abstract = "We have characterized the electron donors to Photosystem II (PS II) in an O2‐evolving reaction center core preparation from spinach (Ghanotakis, D.F.; Yocum, C.F. FEBS Lett., 1986, 197: 244–248) using EPR spectroscopy of the manganese center involved in water oxidation and of the tyrosine donor responsible for signal II. Both the 16‐line and the 19‐line form of the S2 multiline EPR signal can be observed in the core particles under conditions similar to those which produce these signals in PS II membranes. Consequently, the structure of the coupled cluster of three or four Mn ions remains intact in the core particles. The Kok parameters which characterize the number of reaction centers capable of advancing by 0, 1, or 2 equivalents in response to a short laser pulse are found to be the same in PS II membranes and in the core particles. Also, there is no evidence for partially inactivated centers which reach the S2 or S3 states, but which do not advance to O2 release. Thus the new class of highly resolved O2‐evolving particles appears to be well suited for biophysical studies directed at the mechanism of water oxidation.",
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AU - Dismukes, G Charles

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N2 - We have characterized the electron donors to Photosystem II (PS II) in an O2‐evolving reaction center core preparation from spinach (Ghanotakis, D.F.; Yocum, C.F. FEBS Lett., 1986, 197: 244–248) using EPR spectroscopy of the manganese center involved in water oxidation and of the tyrosine donor responsible for signal II. Both the 16‐line and the 19‐line form of the S2 multiline EPR signal can be observed in the core particles under conditions similar to those which produce these signals in PS II membranes. Consequently, the structure of the coupled cluster of three or four Mn ions remains intact in the core particles. The Kok parameters which characterize the number of reaction centers capable of advancing by 0, 1, or 2 equivalents in response to a short laser pulse are found to be the same in PS II membranes and in the core particles. Also, there is no evidence for partially inactivated centers which reach the S2 or S3 states, but which do not advance to O2 release. Thus the new class of highly resolved O2‐evolving particles appears to be well suited for biophysical studies directed at the mechanism of water oxidation.

AB - We have characterized the electron donors to Photosystem II (PS II) in an O2‐evolving reaction center core preparation from spinach (Ghanotakis, D.F.; Yocum, C.F. FEBS Lett., 1986, 197: 244–248) using EPR spectroscopy of the manganese center involved in water oxidation and of the tyrosine donor responsible for signal II. Both the 16‐line and the 19‐line form of the S2 multiline EPR signal can be observed in the core particles under conditions similar to those which produce these signals in PS II membranes. Consequently, the structure of the coupled cluster of three or four Mn ions remains intact in the core particles. The Kok parameters which characterize the number of reaction centers capable of advancing by 0, 1, or 2 equivalents in response to a short laser pulse are found to be the same in PS II membranes and in the core particles. Also, there is no evidence for partially inactivated centers which reach the S2 or S3 states, but which do not advance to O2 release. Thus the new class of highly resolved O2‐evolving particles appears to be well suited for biophysical studies directed at the mechanism of water oxidation.

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