Cytochrome cd1 nitrite reductase from Paracoccus pantotrophus is a dimer; within each
monomer there is a largely alpha-helical domain that contains the c-type cytochrome centre …

Cytochrome c oxidase is a member of the haem copper oxidase superfamily (HCO). HCOs
function as the terminal enzymes in the respiratory chain of mitochondria and aerobic …

Cytochrome c552 is the terminal component of the formate‐dependent nitrite reduction
pathway of Escherichia coli. In addition to four 'typical'haem‐binding motifs, CXXCH …

Oxidized horse cytochrome c (cyt c) has been shown to oligomerize by domain swapping its
C-terminal helix successively. We show that the structural and thermodynamic properties of …

A soluble and fully functional 10.5 kDa fragment of the 18.2 kDa membrane-bound
cytochrome c 552 from Paracoccus denitrificans has been heterologously expressed and …

Nitrous oxide (N 2 O) is a greenhouse gas, the third most significant contributor to global
warming. As a key process for N 2 O elimination from the biosphere, N 2 O reductases …

In this report, we describe direct spectroscopic evidence supporting the presence of a µ-oxo
bridged dinuclear active site in the bacterial enzyme nitric oxide reductase (NOR). As part of …

The gene encoding cytochrome cnitrite reductase (NrfA) from Desulfovibrio
desulfuricansATCC 27774 was sequenced and the crystal structure of the enzyme was …

The crystal structure of the fully oxidized di-heme peroxidase from Nitrosomonas europaea
has been solved to a resolution of 1.80 Å and compared to the closely related enzyme from …

Cytochrome c553 is a photosynthetic electron transport protein found in algae and
cyanobacteria. We have purified cytochromes c553 from five cyanobacteria and studied the …