Redox reactions play important roles in almost all biological processes, including
photosynthesis and respiration, which are two essential energy processes that sustain all life …

Cytochrome c is the specific and efficient electron transfer mediator between the two last
redox complexes of the mitochondrial respiratory chain. Its interaction with both partner …

The electrochemical midpoint potentials (E m's) of 13 cytochromes, in globin (c, c 2, c 551, c
553), four-helix bundle (c ', b 562), αβ roll (b5), and β sandwich (f) motifs, with E m's …

A novel laser-based mass spectrometry method termed LILBID (laser-induced liquid bead
ion desorption) is applied to analyze large integral membrane protein complexes and their …

This review focuses on the terminal part of the respiratory chain where, macroscopically
speaking, electron transfer (ET) switches from the two-electron donor, ubiquinol, to the …

In Paracoccus denitrificans, electrons pass from the membrane-bound cytochrome bc 1
complex to the periplasmic nitrite reductase, cytochrome cd 1. The periplasmic protein …

The structural analysis of the redox complex between the soluble cytochrome c 552 and the
membrane-integral cytochrome ba 3 oxidase of Thermus thermophilus is complicated by the …

Cytochrome-c oxidase is the terminal enzyme in the respiratory chains of mitochondria and
many bacteria and catalyzes the formation of water by reduction of dioxygen. The first step in …

Introducing site‐directed mutations in surface‐exposed residues of subunit II of the heme
aa3 cytochrome c oxidase of Paracoccus denitrificans, we analyze the kinetic parameters of …

In many biochemical processes, proteins need to bind partners amidst a sea of other
molecules. Generally, partner selection is achieved by formation of a single-orientation …