A novel, anaerobically induced ferredoxin in Chlamydomonas reinhardtii

Jacobs, Jessica; Pudollek, Susanne; Hemschemeier, Anja; Happe, Thomas

doi:10.1016/j.febslet.2008.12.018

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Volume 583, Issue 2 , Pages 325-329, 22 January 2009

A novel, anaerobically induced ferredoxin in Chlamydomonas reinhardtii

Edited by Stuart Ferguson

Jessica Jacobs
- Ruhr Universität Bochum, Fakultät für Biologie und Biotechnologie, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, ND2/169, Universitätsstrasse 150, 44780 Bochum, Germany
Susanne Pudollek
- Freie Universität Berlin, Fachbereich Physik, Arnimallee 14, 14195 Berlin, Germany
Anja Hemschemeier
- Ruhr Universität Bochum, Fakultät für Biologie und Biotechnologie, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, ND2/169, Universitätsstrasse 150, 44780 Bochum, Germany
Thomas Happe
- Ruhr Universität Bochum, Fakultät für Biologie und Biotechnologie, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, ND2/169, Universitätsstrasse 150, 44780 Bochum, Germany
- Corresponding author. Fax: +49 234 3214322.

Received 21 October 2008; received in revised form 4 December 2008; accepted 6 December 2008. published online 18 December 2008.

Abstract

We have found the transcript of one of at least six ferredoxin encoding genes of the green alga Chlamydomonas reinhardtii, FDX5, strongly accumulating in anaerobiosis, indicating a vital role of the encoded protein in the anaerobic metabolism of the cells. According to absorption and electron paramagnetic resonance spectroscopy, Fdx5 is a plant-type [2Fe2S]-ferredoxin with a redox potential similar to that of the ferredoxin PetF. However, although Fdx5 seems to be located in the chloroplast, it is not able to photoreduce nicotinamide adenine dinucleotide phosphate (NADP⁺) via ferredoxin-NADP-reductase, nor to be an electron donor to the plastidic [FeFe]-hydrogenase HydA1. Thus, Fdx5 seems to have a special role in a yet to be identified anaerobic pathway.

Abbreviations: aa(s), amino acid(s), Aox, alternative oxidase, bps, basepairs, F, forward, Fnr, ferredoxin-NADPH-oxidoreductase, NADP, nicotinamide adenine dinucleotide phosphate, orf, open reading frame, Pfl, pyruvate formate lyase, PSII, PSI, photosystem II, photosytem I, qPCR, quantitative RealTime PCR, Rubisco LS, large subunit of Rubisco, Rubisco, ribulosebisphosphate carboxylase/oxygenase, SAM, S-adenosylmethionine.