Enteromorpha prolifera

Bond Cu(SCPh3)L Azurin Populus plastocyanin Enteromorpha prolifera plastocyanin Pseudoazurin Cucumber basic blue copper protein"... 

The first crystal structure information on a blue copper protein, for poplar plastocyanin in the Cu(II) state, was published in 1978 (2, 3). Since then, the Cu(I) state and related apo and Hg(II) substituted forms (5, 6), the green algal plastocyanin from Enteromorpha prolifera [Cu(II)] (7), azurin from Alcaligenes denitrificans [Cu(II) and Cu(D] (8, 9), azurin from Pseudomonas aeruginosa [Cu(II)] (10, 11), as well as pseudoazurin from Alcaligenes faecalis S-6 (12), and the cucumber basic protein, both in the Cu(II) state, have been published (13), making this one of the best-documented class of proteins. In addition, information as to three-dimensional structure in solution has been obtained from two-dimensional NMR studies on French bean and Scenedesmus obliquus plastocyanins (14,15). This review is concerned in the main with the active site chemistry. Other recent reviews are listed (16-20). 

In the most recent study, the crystal structure of plastocyanin from the green alga Enteromorpha prolifera PCu(II) has been reported to a resolution of 1.85 A (7). The /3-sandwich structure is virtually the same as that of poplar plastocyanin, with which it has a 56% sequence homology. Two of the residues (57 and 58), which are components of one of the two prominent kinks in poplar plastocyanin, are missing, and there is a resultant tightening up in the structure and change in position of the sole helical turn in the molecule. The dimensions of the Cu site in the two plastocyanins are, within the limits of precision, the same. An intramolecular H bond between two carboxylates, Glu 43 and Asp 53, has been noted and could explain the unusually high pilTa values ( 5) obtained for all Cu(II) plastocyanins (20). 

Enteromorpha sp. Ao-nori Mixture of species E. prolifera et E. intestinalis used as a seasoning powder... 

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