Resolving domain positions of cellobiose dehydrogenase by small angle X-ray scattering.
cellobiose dehydrogenase
conformational changes
interdomain electron transfer
multistate modelling
small angle X-ray scattering
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
10 2023
10 2023
Historique:
revised:
16
05
2023
received:
02
03
2023
accepted:
06
06
2023
pmc-release:
01
10
2024
medline:
23
10
2023
pubmed:
8
6
2023
entrez:
8
6
2023
Statut:
ppublish
Résumé
The interdomain electron transfer (IET) between the catalytic flavodehydrogenase domain and the electron-transferring cytochrome domain of cellobiose dehydrogenase (CDH) plays an essential role in biocatalysis, biosensors and biofuel cells, as well as in its natural function as an auxiliary enzyme of lytic polysaccharide monooxygenase. We investigated the mobility of the cytochrome and dehydrogenase domains of CDH, which is hypothesised to limit IET in solution by small angle X-ray scattering (SAXS). CDH from Myriococcum thermophilum (syn. Crassicarpon hotsonii, syn. Thermothelomyces myriococcoides) was probed by SAXS to study the CDH mobility at different pH and in the presence of divalent cations. By comparison of the experimental SAXS data, using pair-distance distribution functions and Kratky plots, we show an increase in CDH mobility at higher pH, indicating alterations of domain mobility. To further visualise CDH movement in solution, we performed SAXS-based multistate modelling. Glycan structures present on CDH partially masked the resulting SAXS shapes, we diminished these effects by deglycosylation and studied the effect of glycoforms by modelling. The modelling shows that with increasing pH, the cytochrome domain adopts a more flexible state with significant separation from the dehydrogenase domain. On the contrary, the presence of calcium ions decreases the mobility of the cytochrome domain. Experimental SAXS data, multistate modelling and previously reported kinetic data show how pH and divalent ions impact the closed state necessary for the IET governed by the movement of the CDH cytochrome domain.
Identifiants
pubmed: 37287434
doi: 10.1111/febs.16885
pmc: PMC10592539
mid: NIHMS1907296
doi:
Substances chimiques
cellobiose-quinone oxidoreductase
EC 1.1.99.18
Cytochromes
0
Carbohydrate Dehydrogenases
EC 1.1.-
Polysaccharides
0
Ions
0
Cellobiose
16462-44-5
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
4726-4743Subventions
Organisme : NCI NIH HHS
ID : P01 CA092584
Pays : United States
Organisme : NIGMS NIH HHS
ID : P30 GM124169
Pays : United States
Informations de copyright
© 2023 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
Références
Appl Environ Microbiol. 2012 Sep;78(17):6161-71
pubmed: 22729546
Methods Mol Biol. 2018;1764:449-473
pubmed: 29605933
Carbohydr Res. 2017 Aug 7;448:200-204
pubmed: 28291519
Q Rev Biophys. 2007 Aug;40(3):191-285
pubmed: 18078545
Biophys J. 2013 Aug 20;105(4):962-74
pubmed: 23972848
FEBS J. 2020 Mar;287(5):897-908
pubmed: 31532909
Biotechnol Biofuels. 2013 Mar 21;6(1):41
pubmed: 23514094
Curr Protein Pept Sci. 2006 Jun;7(3):255-80
pubmed: 16787264
ACS Catal. 2021 Jan 15;11(2):517-532
pubmed: 33489432
Proc Natl Acad Sci U S A. 2009 Dec 29;106(52):22157-62
pubmed: 20018766
Chem Rev. 2018 Sep 12;118(17):8005-8024
pubmed: 30091597
Eur Biophys J. 2012 Oct;41(10):789-99
pubmed: 22639100
Enzymes. 2020;47:457-489
pubmed: 32951832
Nature. 1999 Nov 4;402(6757):47-52
pubmed: 10573417
Biochim Biophys Acta. 2000 Jul 14;1480(1-2):83-91
pubmed: 11004557
Proc Natl Acad Sci U S A. 2011 Sep 13;108(37):15079-84
pubmed: 21876164
Biochim Biophys Acta. 1996 Mar 7;1293(1):161-9
pubmed: 8652622
J Comput Chem. 2004 Oct;25(13):1605-12
pubmed: 15264254
Nat Commun. 2015 Jul 07;6:7542
pubmed: 26151670
Methods Enzymol. 2022;677:191-219
pubmed: 36410949
J Appl Crystallogr. 2017 Sep 05;50(Pt 5):1545-1553
pubmed: 29021737
Biotechnol Genet Eng Rev. 2012;28:147-75
pubmed: 22616486
J Appl Crystallogr. 2013 Feb 1;46(Pt 1):1-13
pubmed: 23396808
Biochim Biophys Acta Gen Subj. 2018 Apr;1862(4):1031-1039
pubmed: 29374564
Anal Chem. 2020 Feb 4;92(3):2620-2627
pubmed: 31916434
J Struct Biol. 2010 Oct;172(1):128-41
pubmed: 20558299
J Comput Chem. 2008 Aug;29(11):1859-65
pubmed: 18351591
FEBS J. 2015 Aug;282(16):3136-48
pubmed: 25913436
Gen Physiol Biophys. 2009 Jun;28(2):174-89
pubmed: 19592714
J Am Chem Soc. 2012 Jan 18;134(2):890-2
pubmed: 22188218
J Mol Biol. 2002 Jan 18;315(3):421-34
pubmed: 11786022
FEBS Lett. 1992 May 4;302(1):77-80
pubmed: 1587358
Biochim Biophys Acta Gen Subj. 2017 Feb;1861(2):157-167
pubmed: 27851982
Appl Environ Microbiol. 2001 Apr;67(4):1766-74
pubmed: 11282631
Curr Opin Chem Biol. 2015 Dec;29:108-19
pubmed: 26583519
Nucleic Acids Res. 2018 Jul 2;46(W1):W296-W303
pubmed: 29788355
Nat Methods. 2009 Aug;6(8):606-12
pubmed: 19620974
J Biol Chem. 2014 Dec 26;289(52):35929-38
pubmed: 25361767
Nature. 2013 Apr 25;496(7446):477-81
pubmed: 23619693
Chem Sci. 2017 Sep 1;8(9):6561-6565
pubmed: 28989682
Biochemistry. 2010 Apr 20;49(15):3305-16
pubmed: 20230050
Science. 2007 Feb 9;315(5813):804-7
pubmed: 17289988
Nucleic Acids Res. 2016 Jul 8;44(W1):W424-9
pubmed: 27151198
Appl Environ Microbiol. 2011 Mar;77(5):1804-15
pubmed: 21216904