Interdomain electron transfer in cellobiose dehydrogenase is governed by surface electrostatics

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00467728" target="_blank" >RIV/61388971:_____/17:00467728 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/17:10363733

Result on the web

<a href="http://dx.doi.org/10.1016/j.bbagen.2016.11.016" target="_blank" >http://dx.doi.org/10.1016/j.bbagen.2016.11.016</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbagen.2016.11.016" target="_blank" >10.1016/j.bbagen.2016.11.016</a>

Result language

angličtina

Original language name

Interdomain electron transfer in cellobiose dehydrogenase is governed by surface electrostatics

Original language description

Background Cellobiose dehydrogenase (CDH) is a fungal extracellular oxidoreductase which fuels lytic polysaccharide monooxygenase with electrons during cellulose degradation. Interdomain electron transfer between the flavin and cytochrome domain in CDH, preceding the electron flow to lytic polysaccharide monooxygenase, is known to be pH dependent, but the exact mechanism of this regulation has not been experimentally proven so far. Methods To investigate the structural aspects underlying the domain interaction in CDH, hydrogen/deuterium exchange (HDX-MS) with improved proteolytic setup (combination of nepenthesin-1 with rhizopuspepsin), native mass spectrometry with ion mobility and electrostatics calculations were used. Results HDX-MS revealed pH-dependent changes in solvent accessibility and hydrogen bonding at the interdomain interface. Electrostatics calculations identified these differences to result from charge neutralization by protonation and together with ion mobility pointed at higher electrostatic repulsion between CDH domains at neutral pH. In addition, we uncovered extensive O-glycosylation in the linker region and identified the long-unknown exact cleavage point in papain-mediated domain separation. Conclusions Transition of CDH between its inactive (open) and interdomain electron transfer-capable (closed) state is shown to be governed by changes in the protein surface electrostatics at the domain interface. Our study confirms that the interdomain electrostatic repulsion is the key factor modulating the functioning of CDH. General significance The results presented in this paper provide experimental evidence for the role of charge repulsion in the interdomain electron transfer in cellobiose dehydrogenases, which is relevant for exploiting their biotechnological potential in biosensors and biofuel cells

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochimica et Biophysica Acta. General Subjects

ISSN

0304-4165

e-ISSN

—

Volume of the periodical

1861

Issue of the periodical within the volume

2

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

157-167

UT code for WoS article

000392680200016

EID of the result in the Scopus database

2-s2.0-84997282785