Hydrogenases bidirectional

O. Schmitz, G. Boison, R. Hilscher, B. Hundeshagen, W. Zimmer, F. Lottspeich, H. Bothe (1995) Molecular biological analysis of a bidirectional hydrogenase from cyanobacteria. European Journal of Biochemistry, 233 266-276... 

Cyanobacteria may possess several enzymes directly involved in H2 metabolism nitrogenase(s) catalyzing the production of H2 concomitantly with the reduction of nitrogen to ammonia, an uptake hydrogenase, catalyzing the consumption of H2 produced by the nitrogenase, and a bidirectional hydrogenase, which has the capacity to both take up and produce H2 [3, 5],... 

C Thermococcus litoralis hydrogenase D Bidirectional hydrogenase from Cyanobacteria... 

Figure 10.3 Z-scheme of oxygenic photosynthesis in green algae and cyanobacteria, showing links to hydrogenase. Q (plastoquinone) and X (an iron-sulfur cluster) are electron acceptors from photosystems II and I, respectively.The two hydrogenases shown are the NADP-dependent bidirectional hydrogenase and a ferredoxin-dependent enzyme.

Cyanobacteria also contain a reversible/bidirectional hydrogenase, which is soluble and has the capacity to both take up and produce H2 (Bothe et al. 1991 Flores and Herrero 1994 Appel and Schulz 1998 Hansel and Lindblad 1998). The latter enzyme was called bidirectional hydrogenase until the respective structural genes were sequenced and characterized by Schmitz et al. (1995). It has been the subject of some interest as another possible means to produce H2 photosynthetically. 

Appel, J., Phunpruch., S., Steinmuller, K. and Schulz, R. (2000) The bidirectional hydrogenase of Synechocystis sp PCC 6803 works as an electron valve during photosynthesis. Arch. Microbiol., 173, 333-8. 

Boison, G., Schmitz, O., Mikheeva, L., Shestakov, S. and Bothe, H. (1996) Cloning, molecular analysis and insertional mutagenesis of the bidirectional hydrogenase genes from the cyanobacterium Anacystis nidulans. FEES Lett., 394, 153-8. 

We continue our attempts to gain some control over the construction of D. vulgaris bidirectional hydrogenase in E. coli not only to come to an understanding of the biosynthesis of complex Fe/S enzymes, but also to bring the candidacy of this protein for biotechnological applications within the realm of possibility. 

Based on the homology of the cyanobacterial bidirectional hydrogenase with the NAD+-reducing hydrogenase from R. eutropha and the detection of NAD+-reducing activity from H2 oxidation (described in Section 3.2), cyanobacterial H2... 

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