James N Blaza

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Kinetic evidence against partitioning of the ubiquinone pool and the catalytic relevance of respiratory-chain supercomplexes.

James N Blaza, Riccardo Serreli, Andrew Jones, Khairunnisa Mohammed, Judy Hirst
Proceedings of the National Academy of Sciences…
2014

In mitochondria, four respiratory-chain complexes drive oxidative phosphorylation by sustaining a proton-motive force across the inner membrane that is used to synthesize ATP. The question of how the… (More)

The Enigma of the Respiratory Chain Supercomplex.

Dusanka Milenkovic, James N Blaza, Nils-Göran Larsson, Judy Hirst
Cell metabolism
2017

Respiratory chain dysfunction plays an important role in human disease and aging. It is now well established that the individual respiratory complexes can be organized into supercomplexes, and… (More)

An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump

Zhao Wang, Guizhen Fan, +6 authors Dijun Du
eLife
2017

Bacterial efflux pumps confer multidrug resistance by transporting diverse antibiotics from the cell. In Gram-negative bacteria, some of these pumps form multi-protein assemblies that span the cell… (More)

Respiratory Complex I in Bos taurus and Paracoccus denitrificans Pumps Four Protons across the Membrane for Every NADH Oxidized*

Andrew Jones, James N Blaza, Febin Varghese, Judy Hirst
The Journal of biological chemistry
2017

Respiratory complex I couples electron transfer between NADH and ubiquinone to proton translocation across an energy-transducing membrane to support the proton-motive force that drives ATP synthesis.… (More)

Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump

Anthony W. Fitzpatrick, Salomé Llabrés, +9 authors Dijun Du
Nature Microbiology
2017

The MacA–MacB–TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence… (More)

Structure of the Deactive State of Mammalian Respiratory Complex I

James N Blaza, K. Vinothkumar, Judy Hirst
Structure
2018

Complex I (NADH:ubiquinone oxidoreductase) is central to energy metabolism in mammalian mitochondria. It couples NADH oxidation by ubiquinone to proton transport across the energy-conserving inner… (More)

Deleting the IF1-like ζ subunit from Paracoccus denitrificans ATP synthase is not sufficient to activate ATP hydrolysis

Febin Varghese, James N Blaza, Andrew Jones, Owen D Jarman, Judy Hirst
Open biology
2018

In oxidative phosphorylation, ATP synthases interconvert two forms of free energy: they are driven by the proton-motive force across an energy-transducing membrane to synthesize ATP and displace the… (More)

The mechanism of catalysis by type-II NADH:quinone oxidoreductases

James N Blaza, Hannah R. Bridges, +5 authors Judy Hirst
Scientific reports
2017

Type II NADH:quinone oxidoreductase (NDH-2) is central to the respiratory chains of many organisms. It is not present in mammals so may be exploited as an antimicrobial drug target or used as a… (More)

A Self‐Assembled Respiratory Chain that Catalyzes NADH Oxidation by Ubiquinone‐10 Cycling between Complex I and the Alternative Oxidase

Andrew Jones, James N Blaza, Hannah R. Bridges, Benjamin May, Anthony L. Moore, Judy Hirst
Angewandte Chemie
2016

Complex I is a crucial respiratory enzyme that conserves the energy from NADH oxidation by ubiquinone-10 (Q10) in proton transport across a membrane. Studies of its energy transduction mechanism are… (More)

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