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Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I

Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5715780

Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I

About this item

Full title

Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2017-11, Vol.114 (48), p.12737-12742

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Respiratory complex I (NADH:ubiquinone oxidoreductase), one of the largest membrane-bound enzymes in mammalian cells, powers ATP synthesis by using the energy from electron transfer from NADH to ubiquinone-10 to drive protons across the energy-transducing mitochondrial inner membrane. Ubiquinone-10 is extremely hydrophobic, but in complex I the bin...

Alternative Titles

Full title

Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5715780

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5715780

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1714074114

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