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The EPR spectrum and orientation of cytochrome b ‐563 in the chloroplast thylakoid membrane
Author(s) -
Bergström Jörgen
Publication year - 1985
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(85)80959-5
Subject(s) - thylakoid , cytochrome b6f complex , electron transport chain , electron paramagnetic resonance , cytochrome f , cytochrome , chloroplast , cytochrome b , chemistry , crystallography , cytochrome c1 , orientation (vector space) , cytochrome c , biophysics , photochemistry , nuclear magnetic resonance , biology , biochemistry , physics , coenzyme q – cytochrome c reductase , mitochondrion , mitochondrial dna , gene , enzyme , geometry , mathematics
The EPR spectrum of cytochrome b ‐563 in spinach chloroplasts shows that both hemes of the cytochrome are in a low‐spin state with g z = 3.5. The orientation of the two heme planes is found to be perpendicular to the thylakoid membrane plane in magnetically aligned chloroplasts. This may be relevant for the function of cytochrome b ‐563, e.g., in electron transport coupled to proton translocation.