Structural Dynamics of Lytic Polysaccharide Monooxygenase
during Catalysis

J 2020

Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis

FILANDR, Frantisek; Daniel KAVAN; Daniel KRACHER; Christophe V F P LAURENT; Roland LUDWIG et al.

Základní údaje

Originální název

Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis

Autoři

FILANDR, Frantisek; Daniel KAVAN; Daniel KRACHER; Christophe V F P LAURENT; Roland LUDWIG; Petr MAN a Petr HALADA

Vydání

Biomolecules, Basel, Switzerland, MDPI AG, 2020, 2218-273X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Švýcarsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.879

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:90043/20:00139205

Organizační jednotka

CIISB

Klíčová slova anglicky

lytic polysaccharide monooxygenase; lignocellulose degradation; hydrogen; deuterium exchange mass spectrometry; oxidative amino acid modification; peptide bond cleavage; reactive oxygen species

Štítky

ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 3. 2025 17:16, Mgr. Eva Dubská

Anotace

V originále

Lytic polysaccharide monooxygenases (LPMOs) are industrially important oxidoreductases employed in lignocellulose saccharification. Using advanced time-resolved mass spectrometric techniques, we elucidated the structural determinants for substrate-mediated stabilization of the fungal LPMO9C from Neurospora crassa during catalysis. LPMOs require a reduction in the active-site copper for catalytic activity. We show that copper reduction in NcLPMO9C leads to structural rearrangements and compaction around the active site. However, longer exposure to the reducing agent ascorbic acid also initiated an uncoupling reaction of the bound oxygen species, leading to oxidative damage, partial unfolding, and even fragmentation of NcLPMO9C. Interestingly, no changes in the hydrogen/deuterium exchange rate were detected upon incubation of oxidized or reduced LPMO with crystalline cellulose, indicating that the LPMO-substrate interactions are mainly side-chain mediated and neither affect intraprotein hydrogen bonding nor induce significant shielding of the protein surface. On the other hand, we observed a protective effect of the substrate, which slowed down the autooxidative damage induced by the uncoupling reaction. These observations further complement the picture of structural changes during LPMO catalysis.

Návaznosti

90043, velká výzkumná infrastruktura

Název: CIISB

Citovat

FILANDR, Frantisek; Daniel KAVAN; Daniel KRACHER; Christophe V F P LAURENT; Roland LUDWIG; Petr MAN a Petr HALADA. Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis. Biomolecules. Basel, Switzerland: MDPI AG, 2020, roč. 10, č. 2, s. 1-18. ISSN 2218-273X. Dostupné z: https://doi.org/10.3390/biom10020242.

@article{2487290,
   author = {Filandr, Frantisek and Kavan, Daniel and Kracher, Daniel and Laurent, Christophe V F P and Ludwig, Roland and Man, Petr and Halada, Petr},
   article_location = {Basel, Switzerland},
   article_number = {2},
   doi = {https://doi.org/10.3390/biom10020242},
   keywords = {lytic polysaccharide monooxygenase; lignocellulose degradation; hydrogen; deuterium exchange mass spectrometry; oxidative amino acid modification; peptide bond cleavage; reactive oxygen species},
   language = {eng},
   issn = {2218-273X},
   journal = {Biomolecules},
   title = {Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis},
   url = {https://www.mdpi.com/2218-273X/10/2/242},
   volume = {10},
   year = {2020}
}

TY  - JOUR
ID  - 2487290
AU  - Filandr, Frantisek - Kavan, Daniel - Kracher, Daniel - Laurent, Christophe V F P - Ludwig, Roland - Man, Petr - Halada, Petr
PY  - 2020
TI  - Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis
JF  - Biomolecules
VL  - 10
IS  - 2
SP  - 1-18
EP  - 1-18
PB  - MDPI AG
SN  - 2218273X
KW  - lytic polysaccharide monooxygenase
KW  - lignocellulose degradation
KW  - hydrogen
KW  - deuterium exchange mass spectrometry
KW  - oxidative amino acid modification
KW  - peptide bond cleavage
KW  - reactive oxygen species
UR  - https://www.mdpi.com/2218-273X/10/2/242
N2  - Lytic polysaccharide monooxygenases (LPMOs) are industrially important oxidoreductases employed in lignocellulose saccharification. Using advanced time-resolved mass spectrometric techniques, we elucidated the structural determinants for substrate-mediated stabilization of the fungal LPMO9C from Neurospora crassa during catalysis. LPMOs require a reduction in the active-site copper for catalytic activity. We show that copper reduction in NcLPMO9C leads to structural rearrangements and compaction around the active site. However, longer exposure to the reducing agent ascorbic acid also initiated an uncoupling reaction of the bound oxygen species, leading to oxidative damage, partial unfolding, and even fragmentation of NcLPMO9C. Interestingly, no changes in the hydrogen/deuterium exchange rate were detected upon incubation of oxidized or reduced LPMO with crystalline cellulose, indicating that the LPMO-substrate interactions are mainly side-chain mediated and neither affect intraprotein hydrogen bonding nor induce significant shielding of the protein surface. On the other hand, we observed a protective effect of the substrate, which slowed down the autooxidative damage induced by the uncoupling reaction. These observations further complement the picture of structural changes during LPMO catalysis.
ER  -

FILANDR, Frantisek; Daniel KAVAN; Daniel KRACHER; Christophe V F P LAURENT; Roland LUDWIG; Petr MAN a Petr HALADA. Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis. \textit{Biomolecules}. Basel, Switzerland: MDPI AG, 2020, roč.~10, č.~2, s.~1-18. ISSN~2218-273X. Dostupné z: https://doi.org/10.3390/biom10020242.

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