Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode

Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: Heme d binds CO with high affinity

(2011) V. B. Borisov   BIOCHEMISTRY-MOSCOW

Heme–heme and heme–ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy

(2010) Fabrice Rappaport et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS

Compensations for Diminished Terminal Oxidase Activity inEscherichia coli

(2010) Mark Shepherd et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Elevated Proton Leak of the Intermediate OH in Cytochrome c Oxidase

(2009) Dmitry A. Bloch et al.   BIOPHYSICAL JOURNAL

Respiration of Escherichia coli Can Be Fully Uncoupled via the Nonelectrogenic Terminal Cytochrome bd-II Oxidase

(2009) M. Bekker et al.   JOURNAL OF BACTERIOLOGY

Strong Excitonic Interactions in the Oxygen-Reducing Site ofbd-Type Oxidase:  The Fe-to-Fe Distance between Hemesdandb595is 10 ņ

(2008) Alexander M. Arutyunyan et al.   BIOCHEMISTRY

Glutamate 107 in Subunit I of CytochromebdfromEscherichia coliIs Part of a Transmembrane Intraprotein Pathway Conducting Protons from the Cytoplasm to the Hemeb595/HemedActive Site†

(2008) Vitaliy B. Borisov et al.   BIOCHEMISTRY