isolated reduced c domain of the cytochrome cd1 nitrite reductase

The isolated c domain is an electron carrier

In cytochrome cd1 nitrite reductase, the c domain functions as the port of entry of electrons.

Heme ligation and conformational plasticity in the isolated c domain of cytochrome cd1 nitrite reductase.

Nitrite reductase precursor (Cytochrome cd1) (Cytochrome oxidase) (Hydroxylamine reductase)

cytochrome cd1 nitrite reductase [Paracoccus denitrificans]

cytochrome cd1 nitrite reductase [Paracoccus pantotrophus]

Cytochrome Cd1 Nitrite Reductase, Oxidised Form

Cytochrome Cd1 Nitrite Reductase, Reoxidised Enzyme

Cytochrome Cd1 Nitrite Reductase, X-Ray Reduced Dioxygen Complex

Cytochrome Cd1 Nitrite Reductase, Dioxygen Complex

Cytochrome Cd1 Nitrite Reductase, Oxidised From From Tetragonal Crystals

Cytochrome Cd1 Nitrite Reductase, Reduced Form Complexed To Cn

Cytochrome Cd1 Nitrite Reductase, Reduced Form

Cytochrome Cd1 Nitrite Reductase, Y25s Mutant, Oxidised Form

Cytochrome Cd1 Nitrite Reductase, Reduced And Cyanide Bound

Cytochrome Cd1 Nitrite Reductase, Co Complex

Cytochrome Cd1 Nitrite Reductase With Substrate And Product Bound

Substrate And Product Bound To Cytochrome Cd1 Nitrite Reductase

P. pantotrophus prosequence is used to translocate the isolated c domain to the E. coli periplasm.

the isolated c domain is a haem-containing protein

Chemical shifts of 1H resonances of the heme protons and of the side chain
protons of the two axial ligands, His69 and Met106, and of Trp109 of the
isolated c domain of Paracoccus pantotrophus in the reduced state

The sample contains a slight excess of sodium ascorbate