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Identification of an uptake hydrogenase for hydrogen-dependent dissimilatory azoreduction by Shewanella decolorationis S12

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Abstract

Shewanella decolorationis S12, a representative dissimilatory azo-reducing bacterium of Shewanella genus, can grow by coupling the oxidation of hydrogen to the reduction of azo compounds as the sole electron acceptor, indicating that an uptake hydrogenase is an important component for electron transfer for azoreduction. For searching to the uptake hydrogenase in the genome of S. decolorationis, two operons, hyd and hya, were cloned and sequenced, which encode periplasmically oriented Fe-only hydrogenase and a Ni–Fe hydrogenase, respectively, according to the homologous comparison with other bacterial hydrogenases. In order to assess the roles of these two enzymes in hydrogen-dependent azoreduction and growth, hyd- and hya-deficient mutants were generated by gene replacement. Hya was found to be required for hydrogen-dependent reduction of azo compound by resting cell suspensions and to be essential for growth with hydrogen as electron donor and azo compound as electron acceptor. Hyd, in contrast, was not. These findings suggest that Hya is an essential respiratory hydrogenase of dissimilatory azoreduction in S. decolorationis.

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Acknowledgments

The author gratefully acknowledges the support of Young People Innovation Foundation of South China Sea Institute of Oceanology, CAS (07SC011009) and National Natural Science Foundation (30670020).

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Authors and Affiliations

  1. Key Laboratory of Tropical Marine Environment Dynamics (LED), South China Sea Institute of Oceanography, Chinese Academy of Sciences, Guangzhou, 510301, People’s Republic of China

    Yi-Guo Hong

  2. Guangdong Institute of Microbiology, Guangzhou, 510070, People’s Republic of China

    Jun Guo & Guo-Ping Sun

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  1. Yi-Guo Hong
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  2. Jun Guo
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  3. Guo-Ping Sun
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Correspondence to Guo-Ping Sun.

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Fig. S1.

Nucleic acid sequence of Fe hydrogenase from S. decolorationnis S12. The coding regions of the genes for the 46-kDa hydrogenase (169-1401) and the 13.5-kDa protein (1414-1734) are indicated by means of translocation using the single-letter amino acid code. The Cys residues have been circled. Two possible ribosome binding sites, as well as a promoter, are indicated (−35, −10). (DOC 29.5 KB)

Fig. S2.

Nucleic acid sequence of Ni–Fe hydrogenase from S. decolorationnis S12. The coding regions of the genes for the small subunit (136-1272), large subunit (1276-2976), cytochrome b subunit (2998-3675) are indicated by means of translocation using the single-letter amino acid code. The Cys and His residues have been circled. Three possible ribosome binding sites, as well as a promoter, are indicated (−35, −10). (DOC 42.0 KB)

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Hong, YG., Guo, J. & Sun, GP. Identification of an uptake hydrogenase for hydrogen-dependent dissimilatory azoreduction by Shewanella decolorationis S12. Appl Microbiol Biotechnol 80, 517–524 (2008). https://doi.org/10.1007/s00253-008-1597-9

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