A systematic survey of conserved histidines in the core subunits of Photosystem I by site-directed mutagenesis reveals the likely axial ligands of P700

The EMBO Journal
K ReddingJ D Rochaix

Abstract

The Photosystem I complex catalyses the transfer of an electron from lumenal plastocyanin to stromal ferredoxin, using the energy of an absorbed photon. The initial photochemical event is the transfer of an electron from the excited state of P700, a pair of chlorophylls, to a monomer chlorophyll serving as the primary electron acceptor. We have performed a systematic survey of conserved histidines in the last six transmembrane segments of the related polytopic membrane proteins PsaA and PsaB in the green alga Chlamydomonas reinhardtii. These histidines, which are present in analogous positions in both proteins, were changed to glutamine or leucine by site-directed mutagenesis. Double mutants in which both histidines had been changed to glutamine were screened for changes in the characteristics of P700 using electron paramagnetic resonance, Fourier transform infrared and visible spectroscopy. Only mutations in the histidines of helix 10 (PsaA-His676 and PsaB-His656) resulted in changes in spectroscopic properties of P700, leading us to conclude that these histidines are most likely the axial ligands to the P700 chlorophylls.

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Citations

Jan 5, 2008·Photosynthesis Research·Galina GulisKevin E Redding
May 13, 2010·Photosynthesis Research·Aaron M CollinsRobert E Blankenship
Aug 18, 2000·Biochimie·Y Choquet, O Vallon
Mar 14, 2000·Current Opinion in Plant Biology·A R Grossman
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Oct 10, 2012·Proceedings of the National Academy of Sciences of the United States of America·Mia TerashimaMichael Hippler
Dec 6, 2011·Plant & Cell Physiology·Shin-ichiro OzawaYuichiro Takahashi
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