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Hydrogenase(s) in Synechocystis

Tools for Photohydrogen Production?

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Book cover BioHydrogen

Abstract

From the unicellular non-N2-fixing cyanobacterium Synechocystis sp. PCC 6803, we isolated and characterized a hox gene cluster encoding the large and small subunit of a NAD(P)+-reducing NiFe hydrogenase (reversible hydrogenase) and at least three additional polypeptides. Until now, only 11 of the 14 polypeptides of the NADH-dehydrogenase were found in Synechocystis. By sequence homologies, we suggested that the missing subunits of the peripheral part of the dehydrogenase, containing most of the FeS clusters, are encoded by three ORFs of this gene cluster. Since there are no other homologs of these subunits in the entire sequence of Synechocystis (which is now available on the Internet), joint use of these polypeptides as the diaphorase moiety of the complex I and the reversible hydrogenase seems obvious. Complex I of cyanobacteria is located at the interface of the photosynthetic and respiratory electron transport in the thylakoid membrane. Our working hypothesis is that the reversible hydrogenase could be an important controlling device of the redox conditions in the different membranes. It could, for example, function as an electron valve under high light intensities at the photosynthetic membrane. To prove this hypothesis, deletion mutants of the corresponding hox genes were generated. Besides confirming the suggested function of HoxH as the large subunit of the reversible hydrogenase, we confirmed parts of the presented idea tested so far about the physiological role of the reversible hydrogenase in Synechocystis in relation to fermentation, respiration, and photosynthesis.

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© 1998 Plenum Press, New York

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Appel, J., Phunpruch, S., Schulz, R. (1998). Hydrogenase(s) in Synechocystis . In: Zaborsky, O.R., Benemann, J.R., Matsunaga, T., Miyake, J., San Pietro, A. (eds) BioHydrogen. Springer, Boston, MA. https://doi.org/10.1007/978-0-585-35132-2_25

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  • DOI: https://doi.org/10.1007/978-0-585-35132-2_25

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-0-306-46057-9

  • Online ISBN: 978-0-585-35132-2

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