Abstract:
:Cytochrome c oxidase is a membrane-bound redox-driven proton pump that harbors two proton-transfer pathways, D and K, which are used at different stages of the reaction cycle. Here, we address the question if a D pathway with a modified energy landscape for proton transfer could take over the role of the K pathway when the latter is blocked by a mutation. Our data indicate that structural alterations near the entrance of the D pathway modulate energy barriers that influence proton transfer to the proton-loading site. The data also suggest that during reduction of the catalytic site, its protonation has to occur via the K pathway and that this proton transfer to the catalytic site cannot take place through the D pathway.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Vilhjálmsdóttir J,Albertsson I,Blomberg MRA,Ädelroth P,Brzezinski Pdoi
10.1002/1873-3468.13679subject
Has Abstractpub_date
2020-03-01 00:00:00pages
813-822issue
5eissn
0014-5793issn
1873-3468journal_volume
594pub_type
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