Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions.

James Paul Allen, G. Feher, T. O. Yeates, H. Komiya, D. C. Rees

Research output: Contribution to journalArticle

292 Citations (Scopus)

Abstract

The three-dimensional structure of the reaction center (RC) from Rhodobacter sphaeroides has been determined by x-ray diffraction to a resolution of 2.8 A with an R value of 24%. The interactions of the protein with the primary quinone, QA, secondary quinone, QB, and the nonheme iron are described and compared to those of RCs from Rhodopseudomonas viridis. Structural differences between the QA and QB environments that contribute to the function of the quinones (the electron transfer from QA- to QB and the charge recombination of QA-, QB- with the primary donor) are delineated. The protein residues that may be involved in the protonation of QB are identified. A pathway for the doubly reduced QB to dissociate from the RC is proposed. The interactions between QB and the residues that have been changed in herbicide-resistant mutants are described. The environment of the nonheme iron is compared to the environments of metal ions in other proteins.

Original languageEnglish
Pages (from-to)8487-8491
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number22
Publication statusPublished - Nov 1988

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Rhodobacter sphaeroides
Quinones
Iron
Rhodopseudomonas
Proteins
Herbicides
Genetic Recombination
Metals
X-Rays
Electrons
Ions
benzoquinone

ASJC Scopus subject areas

  • General
  • Genetics

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Structure of the reaction center from Rhodobacter sphaeroides R-26 : protein-cofactor (quinones and Fe2+) interactions. / Allen, James Paul; Feher, G.; Yeates, T. O.; Komiya, H.; Rees, D. C.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, No. 22, 11.1988, p. 8487-8491.

Research output: Contribution to journalArticle

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