Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10869965 | FEBS Letters | 2015 | 9 Pages |
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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Authors
Gang-Feng Huang, Xiao-Bing Wu, Li-Ping Bai, Ke Liu, Li-Jing Jiang, Min-Nan Long, Qing-Xi Chen,