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High Resolution Structure of the ba3 Cytochrome c Oxidase from Thermus thermophilus in a Lipidic Env...

High Resolution Structure of the ba3 Cytochrome c Oxidase from Thermus thermophilus in a Lipidic Env...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1306361295

High Resolution Structure of the ba3 Cytochrome c Oxidase from Thermus thermophilus in a Lipidic Environment

About this item

Full title

High Resolution Structure of the ba3 Cytochrome c Oxidase from Thermus thermophilus in a Lipidic Environment

Publisher

United States: Public Library of Science

Journal title

PloS one, 2011-07, Vol.6 (7), p.e22348-e22348

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

The fundamental chemistry underpinning aerobic life on Earth involves reduction of dioxygen to water with concomitant proton translocation. This process is catalyzed by members of the heme-copper oxidase (HCO) superfamily. Despite the availability of crystal structures for all types of HCO, the mode of action for this enzyme is not understood at th...

Alternative Titles

Full title

High Resolution Structure of the ba3 Cytochrome c Oxidase from Thermus thermophilus in a Lipidic Environment

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1306361295

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1306361295

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0022348

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