Experimental evidence for a link among cupredoxins: red, blue, and purple copper transformations in nitrous oxide reductase.

ABSTRACT: The cupredoxin fold is an important motif in numerous proteins that are central to several critical cellular processes ranging from aerobic and anaerobic respiration to catalysis and iron homeostasis. Three types of copper sites have been found to date within cupredoxin folds: blue type 1 (T1) copper, red type 2 (T2) copper, and purple Cu(A). Although as much as 90% sequence difference has been observed among some members of this superfamily of proteins that span several kingdoms, sequence alignment and phylogenic trees strongly suggest an evolutionary link and common ancestry. However, experimental evidence for such a link has been lacking. We report herein the observation of pH-dependent transformation between blue T1 copper, red T2 copper, and the native purple Cu(A) centers of nitrous

SUBMITTER: Savelieff MG 

PROVIDER: S-EPMC2430339 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature