The electron transfer rate from BPhA to QA in reaction centers of Rhodobacter sphaeroides R-26: Influence of the H-subunit, the QA and Fe2+ cofactors, and the isoprene tail of QA

Johannes Schelvis, B. L. Liu, T. J. Aartsma, A. J. Hoff

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Abstract

The secondary electron transfer from reduced bacteriopheophytin (BPhA) to the first acceptor quinone (QA) in variously modified reaction centers from Rhodobacter sphaeroides was studied by transient absorption spectroscopy and compared with native reaction centers. In intact reaction centers, neither substitution of the native QA, ubiquinone-10(UQ10), with menaquinone (MK), nor shortening of the isoprene tail of ubiquinone (UQ) down to 4 and that of MK down to 2 isoprene units changed the rate of electron transfer to QA. However, in Fe2+-depleted reaction centers the electron transfer rate decreased by a factor of 5 upon MK-reconstitution and by a factor of 20-50 upon non-native UQ-reconstitution. In the latter particles, the electron transfer rate decreased with decreasing tail length of UQ, suggesting that the displacement of UQ within the QA pocket as proposed in previous work (Liu B.-L., Van Kan P.J.M. and Hoff A.J. (1991) FEBS Lett. 289, 23-28), is tail-length-dependent.

Original languageEnglish
Pages (from-to)229-236
Number of pages8
JournalBBA - Bioenergetics
Volume1102
Issue number2
DOIs
StatePublished - 25 Sep 1992

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Rhodobacter sphaeroides
Ubiquinone
Electrons
Vitamin K 2
Absorption spectroscopy
Spectrum Analysis
Substitution reactions
isoprene

Keywords

  • (Rb. sphaeroides)
  • Electron transfer
  • Isoprene tail
  • Menaquinone
  • Reaction center
  • Ubiquinone

Cite this

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title = "The electron transfer rate from BPhA to QA in reaction centers of Rhodobacter sphaeroides R-26: Influence of the H-subunit, the QA and Fe2+ cofactors, and the isoprene tail of QA",
abstract = "The secondary electron transfer from reduced bacteriopheophytin (BPhA) to the first acceptor quinone (QA) in variously modified reaction centers from Rhodobacter sphaeroides was studied by transient absorption spectroscopy and compared with native reaction centers. In intact reaction centers, neither substitution of the native QA, ubiquinone-10(UQ10), with menaquinone (MK), nor shortening of the isoprene tail of ubiquinone (UQ) down to 4 and that of MK down to 2 isoprene units changed the rate of electron transfer to QA. However, in Fe2+-depleted reaction centers the electron transfer rate decreased by a factor of 5 upon MK-reconstitution and by a factor of 20-50 upon non-native UQ-reconstitution. In the latter particles, the electron transfer rate decreased with decreasing tail length of UQ, suggesting that the displacement of UQ within the QA pocket as proposed in previous work (Liu B.-L., Van Kan P.J.M. and Hoff A.J. (1991) FEBS Lett. 289, 23-28), is tail-length-dependent.",
keywords = "(Rb. sphaeroides), Electron transfer, Isoprene tail, Menaquinone, Reaction center, Ubiquinone",
author = "Johannes Schelvis and Liu, {B. L.} and Aartsma, {T. J.} and Hoff, {A. J.}",
year = "1992",
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T1 - The electron transfer rate from BPhA to QA in reaction centers of Rhodobacter sphaeroides R-26

T2 - Influence of the H-subunit, the QA and Fe2+ cofactors, and the isoprene tail of QA

AU - Schelvis, Johannes

AU - Liu, B. L.

AU - Aartsma, T. J.

AU - Hoff, A. J.

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N2 - The secondary electron transfer from reduced bacteriopheophytin (BPhA) to the first acceptor quinone (QA) in variously modified reaction centers from Rhodobacter sphaeroides was studied by transient absorption spectroscopy and compared with native reaction centers. In intact reaction centers, neither substitution of the native QA, ubiquinone-10(UQ10), with menaquinone (MK), nor shortening of the isoprene tail of ubiquinone (UQ) down to 4 and that of MK down to 2 isoprene units changed the rate of electron transfer to QA. However, in Fe2+-depleted reaction centers the electron transfer rate decreased by a factor of 5 upon MK-reconstitution and by a factor of 20-50 upon non-native UQ-reconstitution. In the latter particles, the electron transfer rate decreased with decreasing tail length of UQ, suggesting that the displacement of UQ within the QA pocket as proposed in previous work (Liu B.-L., Van Kan P.J.M. and Hoff A.J. (1991) FEBS Lett. 289, 23-28), is tail-length-dependent.

AB - The secondary electron transfer from reduced bacteriopheophytin (BPhA) to the first acceptor quinone (QA) in variously modified reaction centers from Rhodobacter sphaeroides was studied by transient absorption spectroscopy and compared with native reaction centers. In intact reaction centers, neither substitution of the native QA, ubiquinone-10(UQ10), with menaquinone (MK), nor shortening of the isoprene tail of ubiquinone (UQ) down to 4 and that of MK down to 2 isoprene units changed the rate of electron transfer to QA. However, in Fe2+-depleted reaction centers the electron transfer rate decreased by a factor of 5 upon MK-reconstitution and by a factor of 20-50 upon non-native UQ-reconstitution. In the latter particles, the electron transfer rate decreased with decreasing tail length of UQ, suggesting that the displacement of UQ within the QA pocket as proposed in previous work (Liu B.-L., Van Kan P.J.M. and Hoff A.J. (1991) FEBS Lett. 289, 23-28), is tail-length-dependent.

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