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Biochemical evidenc...
Biochemical evidence of both copper chelation and oxygenase activity at the histidine brace
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- Brander, Søren (author)
- Köpenhamns universitet,University of Copenhagen
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- Horvath, Istvan, 1979 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Ipsen, Johan (author)
- Köpenhamns universitet,University of Copenhagen
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- Peciulyte, Ausra, 1986 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Olsson, Lisbeth, 1963 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Hernández-Rollán, Cristina (author)
- Danmarks Tekniske Universitet,Technical University of Denmark
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- Nørholm, Morten H.H. (author)
- Danmarks Tekniske Universitet,Technical University of Denmark
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- Mossin, Susanne (author)
- Danmarks Tekniske Universitet,Technical University of Denmark
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- Leggio, Leila Lo (author)
- Köpenhamns universitet,University of Copenhagen
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- Probst, Corinna (author)
- Duke University
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- Thiele, Dennis J. (author)
- Duke University
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- Salomon Johansen, Katja, 1969 (author)
- Chalmers tekniska högskola,Chalmers University of Technology,Köpenhamns universitet,University of Copenhagen
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(creator_code:org_t)
- 2020-10-01
- 2020
- English.
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In: Scientific Reports. - : Springer Science and Business Media LLC. - 2045-2322 .- 2045-2322. ; 10:1
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Abstract
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- Lytic polysaccharide monooxygenase (LPMO) and copper binding protein CopC share a similar mononuclear copper site. This site is defined by an N-terminal histidine and a second internal histidine side chain in a configuration called the histidine brace. To understand better the determinants of reactivity, the biochemical and structural properties of a well-described cellulose-specific LPMO from Thermoascus aurantiacus (TaAA9A) is compared with that of CopC from Pseudomonas fluorescens (PfCopC) and with the LPMO-like protein Bim1 from Cryptococcus neoformans. PfCopC is not reduced by ascorbate but is a very strong Cu(II) chelator due to residues that interacts with the N-terminus. This first biochemical characterization of Bim1 shows that it is not redox active, but very sensitive to H2O2, which accelerates the release of Cu ions from the protein. TaAA9A oxidizes ascorbate at a rate similar to free copper but through a mechanism that produce fewer reactive oxygen species. These three biologically relevant examples emphasize the diversity in how the proteinaceous environment control reactivity of Cu with O2.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
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- art (subject category)
- ref (subject category)
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- By the author/editor
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Brander, Søren
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Horvath, Istvan, ...
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Ipsen, Johan
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Peciulyte, Ausra ...
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Olsson, Lisbeth, ...
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Hernández-Rollán ...
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show more...
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Nørholm, Morten ...
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Mossin, Susanne
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Leggio, Leila Lo
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Probst, Corinna
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Thiele, Dennis J ...
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Salomon Johansen ...
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biophysics
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Structural Biolo ...
- Articles in the publication
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Scientific Repor ...
- By the university
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Chalmers University of Technology