Multicopper blue oxidases are composed of three or six domains, one of which includes Ceruloplasmin, a domain found only in metazoa. Recent genetic complementation studies in prokaryotic Bacillus sp. SG-1, targeting genes involved in manganese oxidation, revealed a gene (mnxG), the product of which displays an intriguing similarity in its domain organization to Ceruloplasmin. Occurrence of a ceruloplasmin-like sequence in a prokaryote may have very important evolutionary implications. To bridge the gap between prokaryotes and eukaryotes, we manipulated the blue copper binding protein gene in Chlamydomonas reinhardtii , a unicellular eukaryotic organism containing a metazoan ortholog. PCR methods were applied to amplify the DNA fragment encoding the protein using the genomic DNA of Chlamydomonas reinhardtii as a template. Reactions were run in various conditions in the hope of finding an optimal PCR environment. Once a successful amplification can be performed, the DNA will be subsequently inserted into a eukaryote baker?s yeast Saccharomyces cerevisae . We anticipate this system will produce correctly folded protein bodies sufficient for biophysical studies.