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EPR studies of a 9 kDa polypeptide with an iron‐sulfur cluster(s) isolated from photosystem I complex by n ‐butanol extraction
Author(s) -
Oh-oka H.,
Takahashi Y.,
Matsubara H.,
Itoh S.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80101-7
Subject(s) - ferredoxin , electron paramagnetic resonance , sulfur , iron–sulfur cluster , chemistry , photosystem i , spinach , photosystem ii , photosynthetic reaction centre , redox , crystallography , biochemistry , inorganic chemistry , photosynthesis , enzyme , nuclear magnetic resonance , organic chemistry , physics
A 9 kDa polypeptide was isolated with an iron‐sulfur cluster(s) from spinach photosystem I complex [(1988) J. Biochem., in press]. Its EPR spectrum indicated that this protein was an iron‐sulfur protein similar to bacterial‐type ferredoxins. The reduction profiles and temperature dependence of its EPR signals suggested the existence of at least two iron‐sulfur clusters: the one with a lower redox potential shows similar characteristics to those of center B, while the other seems to be a degradation product of center A (or B).