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Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase
by
Wimmer, Reinhard
, Sandgren, Mats
, Felice, Alfons K. G.
, Røhr, Åsmund K.
, Sørlie, Morten
, Preims, Marita
, Aachmann, Finn Lillelund
, Dimarogona, Maria
, Courtade, Gaston
, Ludwig, Roland
, Vaaje-Kolstad, Gustav
, Eijsink, Vincent G. H.
in
Analytical Chemistry
/ Analytisk kemi
/ Binding Sites
/ Biochemistry
/ Biochemistry and Molecular Biology
/ Biofysik
/ Biokemi och molekylärbiologi
/ Biological Sciences
/ Biologiska vetenskaper
/ Biophysics
/ Carbohydrate Dehydrogenases - chemistry
/ Carbohydrate Dehydrogenases - genetics
/ Copper - chemistry
/ Fungal Proteins - chemistry
/ Fungal Proteins - genetics
/ Fysik
/ Mixed Function Oxygenases - chemistry
/ Mixed Function Oxygenases - genetics
/ Natural Sciences
/ Naturvetenskap
/ Neurospora crassa - enzymology
/ Neurospora crassa - genetics
/ Nuclear Magnetic Resonance, Biomolecular
/ Physical Sciences
/ Structural Biology
/ Strukturbiologi
/ Substrate Specificity
2016
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Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase
by
Wimmer, Reinhard
, Sandgren, Mats
, Felice, Alfons K. G.
, Røhr, Åsmund K.
, Sørlie, Morten
, Preims, Marita
, Aachmann, Finn Lillelund
, Dimarogona, Maria
, Courtade, Gaston
, Ludwig, Roland
, Vaaje-Kolstad, Gustav
, Eijsink, Vincent G. H.
in
Analytical Chemistry
/ Analytisk kemi
/ Binding Sites
/ Biochemistry
/ Biochemistry and Molecular Biology
/ Biofysik
/ Biokemi och molekylärbiologi
/ Biological Sciences
/ Biologiska vetenskaper
/ Biophysics
/ Carbohydrate Dehydrogenases - chemistry
/ Carbohydrate Dehydrogenases - genetics
/ Copper - chemistry
/ Fungal Proteins - chemistry
/ Fungal Proteins - genetics
/ Fysik
/ Mixed Function Oxygenases - chemistry
/ Mixed Function Oxygenases - genetics
/ Natural Sciences
/ Naturvetenskap
/ Neurospora crassa - enzymology
/ Neurospora crassa - genetics
/ Nuclear Magnetic Resonance, Biomolecular
/ Physical Sciences
/ Structural Biology
/ Strukturbiologi
/ Substrate Specificity
2016
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Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase
by
Wimmer, Reinhard
, Sandgren, Mats
, Felice, Alfons K. G.
, Røhr, Åsmund K.
, Sørlie, Morten
, Preims, Marita
, Aachmann, Finn Lillelund
, Dimarogona, Maria
, Courtade, Gaston
, Ludwig, Roland
, Vaaje-Kolstad, Gustav
, Eijsink, Vincent G. H.
in
Analytical Chemistry
/ Analytisk kemi
/ Binding Sites
/ Biochemistry
/ Biochemistry and Molecular Biology
/ Biofysik
/ Biokemi och molekylärbiologi
/ Biological Sciences
/ Biologiska vetenskaper
/ Biophysics
/ Carbohydrate Dehydrogenases - chemistry
/ Carbohydrate Dehydrogenases - genetics
/ Copper - chemistry
/ Fungal Proteins - chemistry
/ Fungal Proteins - genetics
/ Fysik
/ Mixed Function Oxygenases - chemistry
/ Mixed Function Oxygenases - genetics
/ Natural Sciences
/ Naturvetenskap
/ Neurospora crassa - enzymology
/ Neurospora crassa - genetics
/ Nuclear Magnetic Resonance, Biomolecular
/ Physical Sciences
/ Structural Biology
/ Strukturbiologi
/ Substrate Specificity
2016
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Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase
Journal Article
Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase
2016
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Overview
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze oxidative cleavage of glycosidic bonds using molecular oxygen and an external electron donor. We have used NMR and isothermal titration calorimetry (ITC) to study the interactions of a broad-specificity fungal LPMO, NcLPMO9C, with various substrates and with cellobiose dehydrogenase (CDH), a known natural supplier of electrons. The NMR studies revealed interactions with cellohexaose that center around the copper site. NMR studies with xyloglucans, i.e., branched β-glucans, showed an extended binding surface compared with cellohexaose, whereas ITC experiments showed slightly higher affinity and a different thermodynamic signature of binding. The ITC data also showed that although the copper ion alone hardly contributes to affinity, substrate binding is enhanced for metal-loaded enzymes that are supplied with cyanide, a mimic of O₂⁻. Studies with CDH and its isolated heme b cytochrome domain unambiguously showed that the cytochrome domain of CDH interacts with the copper site of the LPMO and that substrate binding precludes interaction with CDH. Apart from providing insights into enzyme–substrate interactions in LPMOs, the present observations shed new light on possible mechanisms for electron supply during LPMO action.
Publisher
National Academy of Sciences
Subject
/ Biochemistry and Molecular Biology
/ Biofysik
/ Biokemi och molekylärbiologi
/ Carbohydrate Dehydrogenases - chemistry
/ Carbohydrate Dehydrogenases - genetics
/ Fysik
/ Mixed Function Oxygenases - chemistry
/ Mixed Function Oxygenases - genetics
/ Neurospora crassa - enzymology
/ Neurospora crassa - genetics
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