PMID: 708722Oct 11, 1978Paper

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

Biochimica Et Biophysica Acta
J H GolbeckB KOK

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 P700+ 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 in equilibrium 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.

References

Jan 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·R Malkin, A J Bearden
May 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·T Hiyama, B Ke

Citations

Jan 1, 1986·Photosynthesis Research·P Setif, P Mathis
Dec 1, 1985·Photosynthesis Research·A W Rutherford, Peter Heathcote
Oct 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H A FrankK Sauer
Jan 1, 1987·Biochimica Et Biophysica Acta·J H Golbeck
Feb 1, 1980·Archives of Biochemistry and Biophysics·T Hiyama, D C Fork
Apr 2, 1980·Biochimica Et Biophysica Acta·B Bouges-Bocquet

Related Concepts

Cytochromes
Sodium Dithionite
Respiratory Chain
Iron-Sulfur Proteins
Metalloproteins
Oxidation-Reduction
Dark Reactions of Photosynthesis
Spectrophotometry

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