Subunit CydX ofEscherichia colicytochromebdubiquinol oxidase is essential for assembly and stability of the di-heme active site

The Escherichia coli CydX Protein Is a Member of the CydAB Cytochrome bd Oxidase Complex and Is Required for Cytochrome bd Oxidase Activity

(2013) C. E. VanOrsdel et al.   JOURNAL OF BACTERIOLOGY

The small protein CydX is required for function of cytochrome bd oxidase in Brucella abortus

(2012) Yao-Hui Sun et al.   Frontiers in Cellular and Infection Microbiology

Heme/heme redox interaction and resolution of individual optical absorption spectra of the hemes in cytochrome bd from Escherichia coli

(2009) Dmitry A. Bloch et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS

Electron transfer and energy transduction in the terminal part of the respiratory chain — Lessons from bacterial model systems

(2009) Oliver-Matthias H. Richter et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS

Probing the haem d-binding site in cytochrome bd quinol oxidase by site-directed mutagenesis

(2009) T. Mogi   JOURNAL OF BIOCHEMISTRY

Looking for the minimum common denominator in haem–copper oxygen reductases: Towards a unified catalytic mechanism

(2008) Manuela M. Pereira et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS

Cytochrome c oxidase: exciting progress and remaining mysteries

(2008) Peter Brzezinski et al.   JOURNAL OF BIOENERGETICS AND BIOMEMBRANES