Improved O2-tolerance in variants of a H2-evolving [NiFe]-hydrogenase fromKlebsiella oxytocaHP1
| Autor: | Qing-Xi Chen, Li-Ping Bai, Xiao-Bing Wu, Gang-Feng Huang, Lijing Jiang, Minnan Long, Ke Liu |
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| Rok vydání: | 2015 |
| Předmět: |
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Molecular Hydrogenase Protein Conformation Stereochemistry Protein subunit O2-tolerance Biophysics medicine.disease_cause Biochemistry Active center H2-evolving hydrogenase Structural Biology Gas channel Genetics medicine Anaerobiosis Amino acid residue Molecular Biology Mutation Dose-Response Relationship Drug biology Chemistry Klebsiella oxytoca Biocatalysts Cell Biology Partial pressure Hydrogen-Ion Concentration Enzymes Immobilized biology.organism_classification Oxygen Protein Subunits Biocatalysis Klebsiella oxytoca HP1 Heterochromatin protein 1 Hydrogen |
| Zdroj: | FEBS Letters. 589:910-918 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2015.02.027 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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