-
Je něco špatně v tomto záznamu ?
Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis
F. Filandr, D. Kavan, D. Kracher, CVFP. Laurent, R. Ludwig, P. Man, P. Halada
Jazyk angličtina Země Švýcarsko
Typ dokumentu časopisecké články, práce podpořená grantem
Grantová podpora
16-34818L
Grantová Agentura České Republiky - International
I 2385-N28
Austrian Science Fund - International
W1224
Austrian Science Fund - International
J-4154
Austrian Science Fund - International
LQ1604
Ministry of Education, Youth and Science - International
CZ.1.05/1.1.00/02.0109
European Regional Development Fund - International
LM2015043
Ministry of Education, Youth and Science - International
SVV260427/2019
Univerzita Karlova v Praze - International
PubMed Central od 2011
Europe PubMed Central od 2011
ProQuest Central od 2011-01-01
Open Access Digital Library od 2011-01-01
Open Access Digital Library od 2011-01-01
Health & Medicine (ProQuest) od 2011-01-01
ROAD: Directory of Open Access Scholarly Resources od 2011
Odkazy
PubMed
32033404
DOI
10.3390/biom10020242
Knihovny.cz E-zdroje
- MeSH
- celulosa chemie MeSH
- fungální proteiny chemie MeSH
- hmotnostní spektrometrie s elektrosprejovou ionizací MeSH
- hmotnostní spektrometrie MeSH
- katalytická doména MeSH
- katalýza MeSH
- koncentrace vodíkových iontů MeSH
- konformace proteinů MeSH
- kyslík chemie MeSH
- lignin chemie MeSH
- měď chemie MeSH
- Neurospora crassa enzymologie MeSH
- oxidační stres MeSH
- oxidoreduktasy chemie MeSH
- oxygenasy se smíšenou funkcí chemie MeSH
- polysacharidy chemie MeSH
- reaktivní formy kyslíku chemie MeSH
- substrátová specifita MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
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 Neurosporacrassa 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.
- 000
- 00000naa a2200000 a 4500
- 001
- bmc21012868
- 003
- CZ-PrNML
- 005
- 20210507101639.0
- 007
- ta
- 008
- 210420s2020 sz f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.3390/biom10020242 $2 doi
- 035 __
- $a (PubMed)32033404
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a sz
- 100 1_
- $a Filandr, Frantisek $u Institute of Microbiology of the CAS, Division BioCeV, Prumyslova 595, 252 50 Vestec, Czech Republic $u Department of Biochemistry, Faculty of Science, Charles University, Hlavova 2030/8, 128 43 Prague 2, Czech Republic
- 245 10
- $a Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis / $c F. Filandr, D. Kavan, D. Kracher, CVFP. Laurent, R. Ludwig, P. Man, P. Halada
- 520 9_
- $a 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 Neurosporacrassa 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.
- 650 _2
- $a katalýza $7 D002384
- 650 _2
- $a katalytická doména $7 D020134
- 650 _2
- $a celulosa $x chemie $7 D002482
- 650 _2
- $a měď $x chemie $7 D003300
- 650 _2
- $a fungální proteiny $x chemie $7 D005656
- 650 _2
- $a koncentrace vodíkových iontů $7 D006863
- 650 _2
- $a lignin $x chemie $7 D008031
- 650 _2
- $a hmotnostní spektrometrie $7 D013058
- 650 _2
- $a oxygenasy se smíšenou funkcí $x chemie $7 D006899
- 650 _2
- $a Neurospora crassa $x enzymologie $7 D009492
- 650 _2
- $a oxidační stres $7 D018384
- 650 _2
- $a oxidoreduktasy $x chemie $7 D010088
- 650 _2
- $a kyslík $x chemie $7 D010100
- 650 _2
- $a polysacharidy $x chemie $7 D011134
- 650 _2
- $a vazba proteinů $7 D011485
- 650 _2
- $a konformace proteinů $7 D011487
- 650 _2
- $a reaktivní formy kyslíku $x chemie $7 D017382
- 650 _2
- $a hmotnostní spektrometrie s elektrosprejovou ionizací $7 D021241
- 650 _2
- $a substrátová specifita $7 D013379
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Kavan, Daniel $u Institute of Microbiology of the CAS, Division BioCeV, Prumyslova 595, 252 50 Vestec, Czech Republic
- 700 1_
- $a Kracher, Daniel $u Biocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria
- 700 1_
- $a Laurent, Christophe V F P $u Biocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria
- 700 1_
- $a Ludwig, Roland $u Biocatalysis and Biosensing Research Group, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria
- 700 1_
- $a Man, Petr $u Institute of Microbiology of the CAS, Division BioCeV, Prumyslova 595, 252 50 Vestec, Czech Republic
- 700 1_
- $a Halada, Petr $u Institute of Microbiology of the CAS, Division BioCeV, Prumyslova 595, 252 50 Vestec, Czech Republic
- 773 0_
- $w MED00188737 $t Biomolecules $x 2218-273X $g Roč. 10, č. 2 (2020)
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/32033404 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y p $z 0
- 990 __
- $a 20210420 $b ABA008
- 991 __
- $a 20210507101639 $b ABA008
- 999 __
- $a ok $b bmc $g 1651110 $s 1133247
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2020 $b 10 $c 2 $e 20200205 $i 2218-273X $m Biomolecules $n Biomolecules $x MED00188737
- GRA __
- $a 16-34818L $p Grantová Agentura České Republiky $2 International
- GRA __
- $a I 2385-N28 $p Austrian Science Fund $2 International
- GRA __
- $a W1224 $p Austrian Science Fund $2 International
- GRA __
- $a J-4154 $p Austrian Science Fund $2 International
- GRA __
- $a LQ1604 $p Ministry of Education, Youth and Science $2 International
- GRA __
- $a CZ.1.05/1.1.00/02.0109 $p European Regional Development Fund $2 International
- GRA __
- $a LM2015043 $p Ministry of Education, Youth and Science $2 International
- GRA __
- $a SVV260427/2019 $p Univerzita Karlova v Praze $2 International
- LZP __
- $a Pubmed-20210420