Improved O2-tolerance in variants of a H2-evolving [NiFe]-hydrogenase from Klebsiella oxytoca HP1

FEBS Letters
Gang-Feng HuangQing-Xi Chen

Abstract

In this study, we investigated the mechanism of O2 tolerance of Klebsiella oxytoca HP1 H2-evolving hydrogenase 3 (KHyd3) by mutational analysis and three-dimensional structure modeling. Results revealed that certain surface amino acid residues of KHyd3 large subunit, in particular those at the outer entrance of the gas channel, have a visible effect on its oxygen tolerance. Additionally, solution pH, immobilization and O2 partial pressure also affect KHyd3 O2-tolerance to some extent. We propose that the extent of KHyd3 O2-tolerance is determined by a balance between the rate of O2 access to the active center through gas channels and the deoxidation rate of the oxidized active center. Based on our findings, two higher O2-tolerant KHyd3 mutations G300E and G300M were developed.

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Citations

Sep 12, 2015·FEBS Letters·Jennifer S McDowallFrank Sargent
Jan 31, 2020·Microbiology and Molecular Biology Reviews : MMBR·Stéphane L BenoitChris Greening
Oct 15, 2020·Chemical Reviews·Hui ChenShelley D Minteer

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