Nitrite reductase relationships with

Although nitrite reductases do not belong to the cupredoxin family, they are discussed together with pseudoazurin because of their close functional relationships). 

Intramolecular ET between distinct copper centers is part of the catalytic cycles of many copper-containing redox enzymes, such as the multicopper oxidases, ascorbate oxidase, and ceruloplasmin, as well as the copper-containing nitrite reductases. Examination of internal LRET in these proteins is of considerable interest as it may also provide insights into the evolution of selected ET pathways in particular, whether and how the enzymes have evolved in order to optimize catalytic functions. With the increase in the number of known high-resolution 3D structures of transition metal containing redox enzymes, studies of structure-reactivity relationships have become feasible and indeed many have been carried out during the last two decades. 

Cu nitrite reductase The Cu-dependent nitrite reductase, which transforms nitrite to nitric oxide in denitrifying bacteria, contains both the type-1 and the type-2 Cu center but lacks the binuclear type-3 site [89]. Yet, its arrangement of Cu atoms within the protein indicates a strong structural relationship with the classical blue multicopper oxidases [85], It catalyzes the single-electron reduction of NO2 to NO and water [Eqs. (5)-(7)] ... 

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