Identification and characterization of transposable elements of Paracoccus pantotrophus.
Molecular hijacking of siroheme for the synthesis of heme and d1 heme.
NirJ, a radical SAM family member of the d1 heme biogenesis cluster.
Enzymes and genes of taurine and isethionate dissimilation in Paracoccus denitrificans.
Novel genes coding for lithotrophic sulfur oxidation of Paracoccus pantotrophus GB17.
Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation.
The unusal redox centers of SoxXA, a novel c-type heme-enzyme essential for chemotrophic sulfur-oxidation of Paracoccus pantotrophus.
The complete amino acid sequence confirms the presence of pseudoazurin in Thiosphaera pantotropha.
The pseudoazurin gene from Thiosphaera pantotropha: analysis of upstream putative regulatory sequences and overexpression in Escherichia coli.
Identification of ccdA in Paracoccus pantotrophus GB17: disruption of ccdA causes complete deficiency in c-type cytochromes.
The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha.
Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds.
Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme.
Proton-coupled structural changes upon binding of carbon monoxide to cytochrome cd1: a combined flash photolysis and X-ray crystallography study.
Structure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase.
The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1.
The cytochrome c domain of dimeric cytochrome cd(1) of Paracoccus pantotrophus can be produced at high levels as a monomeric holoprotein using an improved c-type cytochrome expression system in Escherichia coli.
The structure of an alternative form of Paracoccus pantotrophus cytochrome cd1 nitrite reductase.
Transcriptional analysis of the nirS gene, encoding cytochrome cd1 nitrite reductase, of Paracoccus pantotrophus LMD 92.63.
X-ray crystallographic study of cyanide binding provides insights into the structure-function relationship for cytochrome cd1 nitrite reductase from Paracoccus pantotrophus.
d(1) haem biogenesis - assessing the roles of three nir gene products.
Maximal expression of membrane-bound nitrate reductase in Paracoccus is induced by nitrate via a third FNR-like regulator named NarR.