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Molecular interference of Cd2+ with Photosystem II

Författare:
Publiceringsår: 2004
Språk: Engelska
Sidor: 19-31
Publikation/Tidskrift/Serie: Biochimica et Biophysica Acta (BBA) - Bioenergetics
Volym: 1659
Nummer: 1
Dokumenttyp: Artikel
Förlag: Elsevier B.V.

Sammanfattning

Many heavy metals inhibit electron transfer reactions in Photosystem II (PSII). Cd2+ is known to exchange, with high affinity in a slow reaction, for the Ca2+ cofactor in the Ca/Mn cluster that constitutes the oxygen-evolving center. This results in inhibition of photosynthetic oxygen evolution. There are also indications that Cd2+ binds to other sites in PSII, potentially to proton channels in analogy to heavy metal binding in photosynthetic reaction centers from purple bacteria. In search for the effects of Cd2+-binding to those sites, we have studied how Cd2+ affects electron transfer reactions in PSII after short incubation times and in sites, which interact with Cd2+ with low affinity. Overall electron transfer and partial electron transfer were studied by a combination of EPR spectroscopy of individual redox components, flash-induced variable fluorescence and steady state oxygen evolution measurements. Several effects of Cd2+ were observed: (i) the amplitude of the flash-induced variable fluorescence was lost indicating that electron transfer from Y-Z to P-680(+) was inhibited; (ii) Q(A)(-) to Q(B) electron transfer was slowed down; (iii) the S-2 state multiline EPR signal was not observable; (iv) steady state oxygen evolution was inhibited in both a high-affinity and a low-affinity site; (v) the spectral shape of the EPR signal from Q(A)(-)Fe(2+) was modified but its amplitude was not sensitive to the presence of Cd2+. In addition, the presence of both Ca2+ and DCMU abolished Cd2+-induced effects partially and in different sites. The number of sites for Cd2+ binding and the possible nature of these sites are discussed. (C) 2004 Elsevier B.V. All rights reserved.

Disputation

Nyckelord

  • Chemistry

Övriga

Published
Yes
  • ISSN: 0005-2728

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