The electron transfer pathway upon H2oxidation by the NiFe bidirectional hydrogenase of Synechocystis sp. PCC 6803 in the light shares components with the photosynthetic electron transfer chain in thylakoid membranes

Ipsita Dutta, Willem Vermaas

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

In anaerobic conditions the NiFe hydrogenase in the cyanobacterium Synechocystis sp. PCC 6803 catalyzes transient H2production upon a darkness-to-light transition, followed by a rapid H2uptake. We measured H2uptake in Synechocystis mutants lacking photosystem I, photosystem II or terminal oxidases and in the wild-type strain with and without active cytochrome b6f. Rapid light-induced H2uptake was dependent on cytochrome b6f and the presence of photosystem I. We propose light-dependent electron transport from H2to plastoquinone, probably via NAD(P)H dehydrogenase, and on to cytochrome b6f and photosystem I. In darkness H2uptake is ∼10-fold slower than in the light and is independent of thylakoid redox components. The plastoquinone redox state may be key in determining the ultimate H2redox partner. H2uptake and production in darkness likely use the same redox partners. NADH and NADPH, but not reduced ferredoxin, were confirmed as hydrogenase redox donors in vitro.

Original languageEnglish (US)
Pages (from-to)11949-11959
Number of pages11
JournalInternational Journal of Hydrogen Energy
Volume41
Issue number28
DOIs
StatePublished - Jul 27 2016

Fingerprint

darkness
cytochromes
electron transfer
membranes
Membranes
Electrons
Proteins
dehydrogenases
oxidase
Oxidation-Reduction
electrons
Oxidoreductases

Keywords

  • Bidirectional hydrogenase
  • Cyanobacteria
  • Electron transport
  • Hydrogen uptake
  • Photosynthesis
  • Synechocystis

ASJC Scopus subject areas

  • Renewable Energy, Sustainability and the Environment
  • Fuel Technology
  • Condensed Matter Physics
  • Energy Engineering and Power Technology

Cite this

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abstract = "In anaerobic conditions the NiFe hydrogenase in the cyanobacterium Synechocystis sp. PCC 6803 catalyzes transient H2production upon a darkness-to-light transition, followed by a rapid H2uptake. We measured H2uptake in Synechocystis mutants lacking photosystem I, photosystem II or terminal oxidases and in the wild-type strain with and without active cytochrome b6f. Rapid light-induced H2uptake was dependent on cytochrome b6f and the presence of photosystem I. We propose light-dependent electron transport from H2to plastoquinone, probably via NAD(P)H dehydrogenase, and on to cytochrome b6f and photosystem I. In darkness H2uptake is ∼10-fold slower than in the light and is independent of thylakoid redox components. The plastoquinone redox state may be key in determining the ultimate H2redox partner. H2uptake and production in darkness likely use the same redox partners. NADH and NADPH, but not reduced ferredoxin, were confirmed as hydrogenase redox donors in vitro.",
keywords = "Bidirectional hydrogenase, Cyanobacteria, Electron transport, Hydrogen uptake, Photosynthesis, Synechocystis",
author = "Ipsita Dutta and Willem Vermaas",
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AU - Vermaas, Willem

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N2 - In anaerobic conditions the NiFe hydrogenase in the cyanobacterium Synechocystis sp. PCC 6803 catalyzes transient H2production upon a darkness-to-light transition, followed by a rapid H2uptake. We measured H2uptake in Synechocystis mutants lacking photosystem I, photosystem II or terminal oxidases and in the wild-type strain with and without active cytochrome b6f. Rapid light-induced H2uptake was dependent on cytochrome b6f and the presence of photosystem I. We propose light-dependent electron transport from H2to plastoquinone, probably via NAD(P)H dehydrogenase, and on to cytochrome b6f and photosystem I. In darkness H2uptake is ∼10-fold slower than in the light and is independent of thylakoid redox components. The plastoquinone redox state may be key in determining the ultimate H2redox partner. H2uptake and production in darkness likely use the same redox partners. NADH and NADPH, but not reduced ferredoxin, were confirmed as hydrogenase redox donors in vitro.

AB - In anaerobic conditions the NiFe hydrogenase in the cyanobacterium Synechocystis sp. PCC 6803 catalyzes transient H2production upon a darkness-to-light transition, followed by a rapid H2uptake. We measured H2uptake in Synechocystis mutants lacking photosystem I, photosystem II or terminal oxidases and in the wild-type strain with and without active cytochrome b6f. Rapid light-induced H2uptake was dependent on cytochrome b6f and the presence of photosystem I. We propose light-dependent electron transport from H2to plastoquinone, probably via NAD(P)H dehydrogenase, and on to cytochrome b6f and photosystem I. In darkness H2uptake is ∼10-fold slower than in the light and is independent of thylakoid redox components. The plastoquinone redox state may be key in determining the ultimate H2redox partner. H2uptake and production in darkness likely use the same redox partners. NADH and NADPH, but not reduced ferredoxin, were confirmed as hydrogenase redox donors in vitro.

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