Cyanobacterial hydrogenases: diversity, regulation and applications

Authors

  • Paula Tamagnini,

    1. IBMC – Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal
    2. Departmento de Botânica, Faculdade de Ciências, Universidade do Porto, Porto, Portugal
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  • Elsa Leitão,

    1. IBMC – Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal
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  • Paulo Oliveira,

    1. Department of Photochemistry and Molecular Science, The Ångström Laboratories, Uppsala University, Uppsala, Sweden
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  • Daniela Ferreira,

    1. IBMC – Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal
    2. Departmento de Botânica, Faculdade de Ciências, Universidade do Porto, Porto, Portugal
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  • Filipe Pinto,

    1. IBMC – Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal
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  • David James Harris,

    1. CIBIO/UP, Centro de Investigação em Biodiversidade e Recursos Genéticos, Universidade do Porto, Vairão, Portugal
    2. Departamento de Zoologia e Antropologia, Faculdade de Ciências da Universidade do Porto, Porto, Portugal
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  • Thorsten Heidorn,

    1. Department of Photochemistry and Molecular Science, The Ångström Laboratories, Uppsala University, Uppsala, Sweden
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  • Peter Lindblad

    1. Department of Photochemistry and Molecular Science, The Ångström Laboratories, Uppsala University, Uppsala, Sweden
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  • Editor: Annick Wilmotte

Correspondence: Paula Tamagnini, IBMC – Instituto de Biologia Molecular e Celular, Rua do Campo Alegre, 823. 4150-180 Porto, Portugal. Tel.: +351 2260 74900; fax: +351 2260 99157; e-mail: pmtamagn@ibmc.up.pt

Abstract

Cyanobacteria may possess two distinct nickel-iron (NiFe)-hydrogenases: an uptake enzyme found in N2-fixing strains, and a bidirectional one present in both non-N2-fixing and N2-fixing strains. The uptake hydrogenase (encoded by hupSL) catalyzes the consumption of the H2 produced during N2 fixation, while the bidirectional enzyme (hoxEFUYH) probably plays a role in fermentation and/or acts as an electron valve during photosynthesis. hupSL constitute a transcriptional unit, and are essentially transcribed under N2-fixing conditions. The bidirectional hydrogenase consists of a hydrogenase and a diaphorase part, and the corresponding five hox genes are not always clustered or cotranscribed. The biosynthesis/maturation of NiFe-hydrogenases is highly complex, requiring several core proteins. In cyanobacteria, the genes that are thought to affect hydrogenases pleiotropically (hyp), as well as the genes presumably encoding the hydrogenase-specific endopeptidases (hupW and hoxW) have been identified and characterized. Furthermore, NtcA and LexA have been implicated in the transcriptional regulation of the uptake and the bidirectional enzyme respectively. Recently, the phylogenetic origin of cyanobacterial and algal hydrogenases was analyzed, and it was proposed that the current distribution in cyanobacteria reflects a differential loss of genes according to their ecological needs or constraints. In addition, the possibilities and challenges of cyanobacterial-based H2 production are addressed.

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