Structural and molecular weight studies on the small copper protein, plastocyanin.
نویسندگان
چکیده
The plastocyanin from Phaseolus vulgaris has been shown to consist of a single polypeptide chain of 100 residues to which 1 atom of copper is bound. This plastocyanin is the smallest copper-protein yet reported; its molecular weight is 10,690. The molar extinction coefficient (E& of the copper chromophore was shown to be 4.5 x 103. The copper content and molecular weight contrast with that of plastocyanin preparations from spinach (mol. wt., 21,000) and Chenopodium atbum (mol. wt., 11,500), which both contain 2 copper atoms
منابع مشابه
plasts and functions as an electron carrier from cytochrome f to P7OO in the electron transport chain between photosystem II and I.3) The redox reaction of plastocyanin is due to its copper valency change
Plastocyanin, a copper protein, was first isolated by Katoh in 1960 from the green alga, Chlorella ellipsoidea, and subsequently from various higher plants.l~,2) The protein is present in the chloroplasts and functions as an electron carrier from cytochrome f to P7OO in the electron transport chain between photosystem II and I.3) The redox reaction of plastocyanin is due to its copper valency c...
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 245 7 شماره
صفحات -
تاریخ انتشار 1970