The [NiFe]-hydrogenase of the cyanobacterium synechocystis sp. PCC 6803 works bidirectionally with a bias to H2 production

Chelsea L. McIntosh, Frauke Germer, Rüdiger Schulz, Jens Appel, Anne Katherine Jones

Research output: Contribution to journalArticle

56 Citations (Scopus)

Abstract

Protein film electrochemistry (PFE) was utilized to characterize the catalytic activity and oxidative inactivation of a bidirectional [NiFe]-hydrogenase (HoxEFUYH) from the cyanobacterium Synechocystis sp. PCC 6803. PFE provides precise control of the redox potential of the adsorbed enzyme so that its activity can be monitored under changing experimental conditions as current. The properties of HoxEFUYH are different from those of both the standard uptake and the "oxygen-tolerant" [NiFe]-hydrogenases. First, HoxEFUYH is biased toward proton reduction as opposed to hydrogen oxidation. Second, despite being expressed under aerobic conditions in vivo, HoxEFUYH is clearly not oxygen-tolerant. Aerobic inactivation of catalytic hydrogen oxidation by HoxEFUYH is total and nearly instantaneous, producing two inactive states. However, unlike the Ni-A and Ni-B inactive states of standard [NiFe]-hydrogenases, both of these states are quickly (

Original languageEnglish
Pages (from-to)11308-11319
Number of pages12
JournalJournal of the American Chemical Society
Volume133
Issue number29
DOIs
Publication statusPublished - Jul 27 2011

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Synechocystis
Cyanobacteria
Electrochemistry
Proteins
Oxidation
Hydrogen
Oxygen
Catalyst activity
Protons
Enzymes
Oxidation-Reduction
nickel-iron hydrogenase

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

The [NiFe]-hydrogenase of the cyanobacterium synechocystis sp. PCC 6803 works bidirectionally with a bias to H2 production. / McIntosh, Chelsea L.; Germer, Frauke; Schulz, Rüdiger; Appel, Jens; Jones, Anne Katherine.

In: Journal of the American Chemical Society, Vol. 133, No. 29, 27.07.2011, p. 11308-11319.

Research output: Contribution to journalArticle

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