Log in to save to my catalogue

Cryo-EM structures of Escherichia coli cytochrome bo 3 reveal bound phospholipids and ubiquinone-8 i...

Cryo-EM structures of Escherichia coli cytochrome bo 3 reveal bound phospholipids and ubiquinone-8 i...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_2563420060

Cryo-EM structures of Escherichia coli cytochrome bo 3 reveal bound phospholipids and ubiquinone-8 in a dynamic substrate binding site

About this item

Full title

Cryo-EM structures of Escherichia coli cytochrome bo 3 reveal bound phospholipids and ubiquinone-8 in a dynamic substrate binding site

Publisher

United States

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2021-08, Vol.118 (34)

Language

English

Formats

Publication information

Publisher

United States

More information

Scope and Contents

Contents

Quinol oxidases that are members of the heme–copper superfamily of respiratory oxygen reductases have evolved from cytochrome
c
oxidases. They directly oxidize quinol and reduce oxygen to water. Here, we describe two high-resolution cryogenic electron microscopy structures of the proton-pumping cytochrome
bo
3
ubiquinol oxidase in st...

Alternative Titles

Full title

Cryo-EM structures of Escherichia coli cytochrome bo 3 reveal bound phospholipids and ubiquinone-8 in a dynamic substrate binding site

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_2563420060

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_2563420060

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.2106750118

How to access this item