PMID: 9183022May 1, 1997Paper

Electron transfer between spinach plastocyanin mutants and photosystem 1

European Journal of Biochemistry
K SigfridssonO Hansson

Abstract

Two distinct regions of plastocyanin, one hydrophobic and one acidic, are generally thought to be involved in the electron-transfer reactions with its physiological partners, cytochrome f and photosystem 1. To probe the importance of the hydrophobic patch in the reaction with photosystem 1, seven mutant plastocyanin proteins have been constructed with the following mutations: Gly7Ala, Gly8Asp, Ser11Asp, Ser11Gly, Pro36Gly, Ser85Thr and Gln88Asn. The electron-transfer reaction was investigated by transient flash-photolysis absorption spectroscopy. All proteins remained active in photosystem 1 reduction, showing a biphasic reaction. However, the substitution in position 36 resulted in a drastic decrease in efficiency, suggesting that this residue is involved in a specific contact with photosystem 1. Measurements over a wide range of plastocyanin concentration, ionic strength and pH, showed different properties for the two kinetic phases. A mechanism involving a rate-limiting conformational change accounts well for the observations. Electron transfer from plastocyanin to photosystem 1 would thus require a conversion from an inactive to an active conformation of the complex. Both hydrophobic and electrostatic interactions are impor...Continue Reading

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Citations

Oct 29, 1998·Protein Science : a Publication of the Protein Society·Y XueS Young
Jul 17, 1998·Current Opinion in Chemical Biology·B G Malmström, J Leckner
Sep 7, 2000·Protein Science : a Publication of the Protein Society·F De RienzoR C Wade
Jul 22, 2008·Biophysical Journal·Shana L Bender, Bridgette A Barry
May 1, 2008·Biochimica Et Biophysica Acta·Hanna Jansson, Orjan Hansson
Jun 7, 2013·Metallomics : Integrated Biometal Science·Inmaculada Yruela
Jan 10, 2002·Biochemistry·Christopher DennisonTakamitsu Kohzuma

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