The Fox1 ferroxidase of Chlamydomonas reinhardtii: a new multicopper oxidase structural paradigm.

ABSTRACT: Multicopper oxidases (MCO) contain at least four copper atoms arrayed in three distinct ligand fields supported by two canonical structural features: (1) multiples of the cupredoxin fold and (2) four unique sequence elements that include the ten histidine and one cysteine ligands to the four copper atoms. Ferroxidases are a subfamily of MCO proteins that contain residues supporting a specific reactivity towards ferrous iron; these MCOs play a vital role in iron metabolism in bacteria, algae, fungi, and mammals. In contrast to the fungal ferroxidases, e.g., Fet3p from Saccharomyces cerevisiae, the mammalian ceruloplasmin (Cp) is twice as large (six vs. three cupredoxin domains) and contains three type 1, or "blue," copper sites. Chlamydomonas reinhardtii expresses a putative ferroxidase, Fo

SUBMITTER: Terzulli AJ 

PROVIDER: S-EPMC2675754 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature