What question did this study set out to answer?

To determine the structural and functional role of the 2Fe-2S cluster-binding HoxE subunit in the cyanobacterial reversible hydrogenase of Synechocystis PCC6803.

August 17, 2011FEBS Journal

Role of HoxE subunit in Synechocystis PCC6803 hydrogenase

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Authors

EAEmeline Aubert‐Jousset MCMélissa Cano GGGeneviève Guedeney

Discussion

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Overview

Gene deletion study reveals HoxE mediates pyridine nucleotide-dependent hydrogen catalysis in Synechocystis PCC6803, indicating distinct pathways for catalytic activation and electron transfer.

Key Points

To determine the structural and functional role of the 2Fe-2S cluster-binding HoxE subunit in the cyanobacterial reversible hydrogenase of Synechocystis PCC6803.
Generated a targeted hoxE subunit deletion strain in Synechocystis PCC6803.
Assayed hydrogen production, hydrogen uptake, NiFe active site reductive activation, and electron transfer-independent H/D exchange using pyridine nucleotides (NADH, NADPH, NAD+, NADP+) and artificial electron carriers.
In the intact enzyme, NADPH preferentially mediated reductive NiFe activation, whereas NADH served as the more efficient electron donor for hydrogen production and NAD+ as the preferred acceptor for hydrogen oxidation.
Deletion of hoxE eliminated NADH- and NAD+-dependent hydrogen production and consumption without impairing catalytic activity supported by artificial electron donors or acceptors.
HoxE-deficient enzyme retained the ability to activate H/D exchange via NADPH, while NADH-mediated activation of this reaction was completely abolished.

Cite This Study

Aubert‐Jousset et al. (2011) studied this question.

synapsesocial.com/papers/6a8c019790fae8fd47e9a2b7 https://doi.org/10.1111/j.1742-4658.2011.08308.x

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August 17, 2011FEBS Journal

Role of HoxE subunit in Synechocystis PCC6803 hydrogenase

View Full Paper

Ask AI

Bookmark

Authors

EAEmeline Aubert‐Jousset MCMélissa Cano GGGeneviève Guedeney

Discussion

Member takes

Overview

Gene deletion study reveals HoxE mediates pyridine nucleotide-dependent hydrogen catalysis in Synechocystis PCC6803, indicating distinct pathways for catalytic activation and electron transfer.

Key Points

To determine the structural and functional role of the 2Fe-2S cluster-binding HoxE subunit in the cyanobacterial reversible hydrogenase of Synechocystis PCC6803.
Generated a targeted hoxE subunit deletion strain in Synechocystis PCC6803.
Assayed hydrogen production, hydrogen uptake, NiFe active site reductive activation, and electron transfer-independent H/D exchange using pyridine nucleotides (NADH, NADPH, NAD+, NADP+) and artificial electron carriers.
In the intact enzyme, NADPH preferentially mediated reductive NiFe activation, whereas NADH served as the more efficient electron donor for hydrogen production and NAD+ as the preferred acceptor for hydrogen oxidation.
Deletion of hoxE eliminated NADH- and NAD+-dependent hydrogen production and consumption without impairing catalytic activity supported by artificial electron donors or acceptors.
HoxE-deficient enzyme retained the ability to activate H/D exchange via NADPH, while NADH-mediated activation of this reaction was completely abolished.

Cite This Study

Aubert‐Jousset et al. (2011) studied this question.

synapsesocial.com/papers/6a8c019790fae8fd47e9a2b7 https://doi.org/10.1111/j.1742-4658.2011.08308.x

View Full Paper

Ask AI

Bookmark