PMID: 8950373Nov 12, 1996Paper

Construction and characterization of a photosystem II D1 mutant (arginine-269-glycine) of Chlamydomonas reinhardtii

Biochimica Et Biophysica Acta
R S Hutchison Govindjee

Abstract

Numerous lines of evidence indicate that bicarbonate anion regulates electron and proton transfer processes in the photosystem II (PSII) complex of chloroplasts and cyanobacteria. On the reducing side of PSII, the addition of bicarbonate to bicarbonate-depleted (or formate-treated) membranes accelerates, especially, QA(-)-->QB(-) electron transfer kinetics. The site(s) at which bicarbonate binds is unknown. It is evident, however, from several spectroscopic studies that the bicarbonate binding site on the reducing side of PSII includes the non-heme iron located between the QA and QB sites. Since small anions may displace bicarbonate (Good, N.E. (1963) Plant Physiol. 38, 298-304) [1], it is apparent that the bicarbonate binding site is electrostatic in nature, presumably also involving positively charged amino acid residues. Previously, it had been predicted that residue arginine 269 of the PSII D1 protein may participate in bicarbonate binding. To test this hypothesis, we have generated a non-conservative mutation in the psbA gene of Chlamydomonas reinhardtii which converts residue R269 to a glycine (R269G). The R269G mutant was unable to grow photosynthetically or evolve oxygen. This phenotype is associated with a lack of the ...Continue Reading

References

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Citations

Oct 12, 2013·Photosynthesis Research·Julian J Eaton-Rye
Nov 18, 2006·Cell Structure and Function·Taisuke KayamoriTakenori Yamada
Oct 24, 1998·Biochimica Et Biophysica Acta·M HipplerJ D Rochaix
Apr 24, 2012·Biochimica Et Biophysica Acta·Dmitriy Shevela Govindjee
Oct 16, 2007·Biochimica Et Biophysica Acta·Hiroshi IshikitaErnst-Walter Knapp
Dec 15, 2000·Biochimica Et Biophysica Acta·V V Klimov, S V Baranov
Mar 29, 2014·Photosynthesis Research·Alexandra Dubini, Maria L Ghirardi

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