Ruhr Universität Bochum, Fakultät für Biologie und Biotechnologie, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, ND2/170, 44780 Bochum, Germany.
Eur J Cell Biol. 2010 Dec;89(12):998-1004. doi: 10.1016/j.ejcb.2010.06.018. Epub 2010 Aug 8.
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.
单细胞绿藻莱茵衣藻至少有六种植物型铁氧还蛋白（FDX）。除了众所周知的光合作用铁氧还蛋白 PetF 外，还鉴定出了同工型 Fdx2-Fdx6。FDX 基因在各种环境条件下（如氧气、铜、铁和铵的可用性）差异表达。最近，对厌氧诱导的 Fdx5 以及参与亚硝酸盐还原的 Fdx2 进行了更详细的研究。此外，还表明，PetF 是 C. reinhardtii 中中心且最丰富的 FDX，是氢化酶 HydA1 的合适伴侣。使用 PetF 和 HydA1 的突变变体，可以鉴定出两者相互作用所必需的氨基酸残基。这些发现将有助于为实现 C. reinhardtii 的优化光生物技术制氢来定制 PetF，这也可能得益于对氧如何攻击 HydA1 的活性位点金属簇的机制的新见解。本文综述了在理解 C. reinhardtii 中铁氧还蛋白和氢化酶的功能方面的最新进展。
