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Catalase HPII from Escherichia coli Exhibits Enhanced Resistance to Denaturation
Abstract
Catalase HPII from Escherichia coli is a homotetramer of 753 residue subunits. The multimer displays a number of unusual structural features, including interwoven subunits and a covalent bond between Tyr415 and His392, that would contribute to its rigidity and stability. As the temperature of a solution of HPII in 50 mM potassium phosphate buffer (pH 7) is raised from 50 to 92 degrees C, the enzyme begins to lose activity at 78 degrees C and 50% inactivation has occurred at 83 degrees C. The inactivation is accompanied by absorbance changes at 280 and 407 nm and by changes in the CD spectrum consistent with small changes in secondary structure. The subunits in the dimer structure remain associated at 95 degrees C and show a significant level of dissociation only at 100 degrees C. The exceptional stability of the dimer association is consistent with the interwoven nature of the subunits and provides an explanation for the resistance to inactivation of the enzyme. For comparison, catalase-peroxidase HPI of E. coli and bovine liver catalase are 50% inactivated at 53 and 56 degrees C, respectively. In 5.6 M urea, HPII exhibits a coincidence of inactivation, CD spectral change, and dissociation of the dimer structure with a midpoint of 65 degrees C. The inactive mutant variants of HPII which fold poorly during synthesis and which lack the Tyr-His covalent bond undergo spectral changes in the 78 to 84 degrees C range, revealing that the extra covalent linkage is not important in the enhanced resistance to denaturation and that problems in the folding pathway do not affect the ultimate stability of the folded structure.
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“Bacterial clade II catalases exhibit greater resistance to denaturing conditions, such as high temperature or 7 M urea than metazoan clade III catalases40 and, thus, tardigrade clade II catalase might be active even in hyperosmotic conditions during dehydration/rehydration and contribute to desiccation tolerance.”
From Extremotolerant tardigrade genome and improved radiotolerance of human cultured cells by tardigrade-unique protein (2016) · cites this paper as [40]
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Metadata
- Authors
- Switala, J., O'Neil, J. O., & Loewen, P. C.
- Affiliations
- University of Manitoba (CA)
- Corresponding author
- Loewen, Peter C.
- ORCID
- Loewen, Peter C.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1999-03-01
- Volume
- 38
- Issue
- 13
- Pages
- 3895-3901
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2035837541
- Cited by
- 49
- References
- 7
- Citations by year
- 2026: 1 · 2024: 1 · 2022: 1 · 2019: 2 · 2018: 1 · 2016: 2 · 2015: 2 · 2014: 3 · 2013: 2 · 2012: 3
- FWCI
- 0.57
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- Escherichia coli, thermal denaturation, protein stability, homotetramer, urea denaturation, bovine liver catalase, protein folding, mutants, secondary structure changes
- MeSH terms
- Catalase, Circular Dichroism, Enzyme Activation, Enzyme Stability, Escherichia coli, Hot Temperature, Models, Molecular, Protein Denaturation, Sodium Dodecyl Sulfate, Urea, Mutagenesis, Site-Directed, Guanidine
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