Probing the unusual oxidation/reduction behavior of Paracoccus pantotrophus cytochrome cd1 nitrite reductase by replacing a switchable methionine heme iron ligand with histidine.

Abstract

A M106H variant, where M106 is a c-type heme iron axial ligand, of cytochrome cd(1) nitrite reductase is an inactive protein in vivo. Expression of the holoprotein in Paracoccus pantotrophus required generation of nitric oxide during cell growth through simultaneous expression of an exogenous copper nitrite reductase from Alcaligenes faecalis. In the… (More)

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