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Curr Microbiol. 2000 Jun;40(6):356-61.

Diversity of cyanobacterial hydrogenases, a molecular approach.

Author information

1
Department of Physiological Botany, EBC, Uppsala University, Villav├Ągen 6, S-752 36 Uppsala, Sweden. pmtamgn@gaia.ibmc.up.pt

Abstract

In an effort to elucidate the diversity of cyanobacterial hydrogenases, we used a molecular approach. Filamentous strains from a broad range of sources were screened for the presence of hup (uptake hydrogenase), xisC (rearrangement within hupL), and hox (bidirectional hydrogenase) genes. As expected, an uptake hydrogenase seems to be present in all N(2)-fixing cyanobacteria. On the other hand, no evidence was found for the presence of a conventional bidirectional enzyme in several strains. Similarly, the presence of xisC is not a characteristic shared by all the heterocyst-forming cyanobacteria. Although tempting, it is not possible to establish a correlation between the presence/absence of the bidirectional hydrogenase and the occurrence of xisC. The natural molecular variation of hydrogenases in cyanobacteria is certainly a field to explore, both to understand the physiological functions of the respective enzymes and to identify a genetic background to be used when constructing a strain for photobiological H(2) production in a bioreactor.

PMID:
10827276
DOI:
10.1007/s002840010070
[Indexed for MEDLINE]

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