Structure of the cytochrome aa 3 -600 heme-copper menaquinol oxidase bound to inhibitor HQNO shows T...
Structure of the cytochrome aa 3 -600 heme-copper menaquinol oxidase bound to inhibitor HQNO shows TM0 is part of the quinol binding site
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Author / Creator
Xu, Jingjing , Ding, Ziqiao , Liu, Bing , Yi, Sophia M. , Li, Jiao , Zhang, Zhengguang , Liu, Yuchen , Li, Jin , Liu, Liu , Zhou, Aiwu , Gennis, Robert B. and Zhu, Jiapeng
Publisher
United States
Journal title
Language
English
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Publisher
United States
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Contents
Virtually all proton-pumping terminal respiratory oxygen reductases are members of the heme-copper oxidoreductase superfamily. Most of these enzymes use reduced cytochrome
c
as a source of electrons, but a group of enzymes have evolved to directly oxidize membrane-bound quinols, usually menaquinol or ubiquinol. All of the quinol oxidases have...
Alternative Titles
Full title
Structure of the cytochrome aa 3 -600 heme-copper menaquinol oxidase bound to inhibitor HQNO shows TM0 is part of the quinol binding site
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Record Identifier
TN_cdi_proquest_miscellaneous_2331613264
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_2331613264
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1915013117
