Evidence that the intermediate electron acceptor, A2, in Photosystem I is a bound iron-sulfur protein

John H. Golbeck, B. R. Velthuys, B. Kok

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

Absorption changes accompanying the formation of light-induced P-700+ were investigated in a highly enriched Photosystem I preparation where an intermediate electron acceptor preceding P-430 could be detected. In an enriched Photosystem I particle, light-induced reversible absorption changes observed at 700 nm in the presence of dithionite resembled those previously seen at 703 nm and 820 nm [9], thus indicating the presence of a backreaction between P-700+ and A- 2. After this same Photosystem I particle was treated to denature the bound iron-sulfur centers, the photochemical changes that could be attributed to P-700 A2 were completely lost. These results provide evidence that the intermediate electron acceptor, A2, is a bound iron-sulfur protein. Additional studies in the 400-500 nm region with Photosystem I particles prepared by sonication indicate that the spectrum of A2 is different from that of P-430.

Original languageEnglish (US)
Pages (from-to)226-230
Number of pages5
JournalBBA - Bioenergetics
Volume504
Issue number1
DOIs
StatePublished - Oct 11 1978

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Medicine(all)

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