Multiple ferredoxin isoforms in Chlamydomonas reinhardtii - Their role under stress conditions and biotechnological implications.
Summary of "Multiple ferredoxin isoforms in Chlamydomonas reinhardtii - Their role under stress conditions and biotechnological implications."
The unicellular green alga Chlamydomonas reinhardtii has at least six plant-type ferredoxins (FDX). Besides the long-known photosynthetic ferredoxin PetF the isoforms Fdx2-Fdx6 have been identified. The FDX genes are differentially expressed under various environmental conditions such as the availability of oxygen, copper, iron and ammonium. Recently, the anaerobically induced Fdx5 as well as Fdx2, which is involved in nitrite reduction were characterized in more detail. Moreover, it was shown that PetF, the central and most abundant FDX of C. reinhardtii, is a suitable partner of the hydrogenase HydA1. Using mutant variants of both PetF and HydA1, amino acid residues essential for the interaction of both proteins could be identified. These findings will help to tailor PetF for achieving an optimized photobiotechnological hydrogen production in C. reinhardtii, which might also benefit from new insights into the mechanism of how oxygen attacks the active site metal cluster of HydA1. This review gives an update on recent advances in understanding the function of ferredoxins and the hydrogenase in C. reinhardtii.
Ruhr Universität Bochum, Fakultät für Biologie und Biotechnologie, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, ND2/170, 44780 Bochum, Germany.
This article was published in the following journal.
Name: European journal of cell biology
- PubMed Source: http://www.ncbi.nlm.nih.gov/pubmed/20696493
- DOI: http://dx.doi.org/10.1016/j.ejcb.2010.06.018
Medical and Biotech [MESH] Definitions
An organism considered both a protozoon (Dorland, 27th ed) and an alga (Bold & Wynne, Introduction to the Algae, 2d ed, p84). Delicate, hairlike appendages arise from the flagellar surface in these organisms.
Sulfite Reductase (ferredoxin)
A FERREDOXIN-dependent oxidoreductase that is primarily found in PLANTS where it plays an important role in the assimilation of SULFUR atoms for the production of CYSTEINE and METHIONINE.
Transmembrane proteins belonging to the tumor necrosis factor superfamily that play an essential role in the normal development of several ectodermally derived organs. Several isoforms of the ectodysplasins exist due to multiple ALTERNATIVE SPLICING of the MRNA for the protein. The isoforms ectodysplasin A1 and ectodysplasin A2 are considered biologically active and each bind distinct ECTODYSPLASIN RECEPTORS. Genetic mutations that result in loss of function of ectodysplasin result in ECTODERMAL DYSPLASIA 1, ANHIDROTIC.
A tumor necrosis factor receptor subtype found in a variety of tissues and on activated LYMPHOCYTES. It has specificity for FAS LIGAND and plays a role in regulation of peripheral immune responses and APOPTOSIS. Multiple isoforms of the protein exist due to multiple ALTERNATIVE SPLICING. The activated receptor signals via a conserved death domain that associates with specific TNF RECEPTOR-ASSOCIATED FACTORS in the CYTOPLASM.
An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 126.96.36.199 was formerly listed as EC 188.8.131.52 and EC 184.108.40.206.
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