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Conformation of the c 552 : aa 3 electron transfer complex in Paracoccus denitrificans studied by EPR on oriented samples
Author(s) -
Lipowski Gérard,
Liebl Ursula,
Guigliarelli Bruno,
Nitschke Wolfgang,
Schoepp-Cothenet Barbara
Publication year - 2006
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/j.febslet.2006.09.038
Subject(s) - paracoccus denitrificans , chemistry , electron paramagnetic resonance , stereochemistry , electron transfer , cytochrome c oxidase , cytochrome c , crystallography , histidine , heme a , nuclear magnetic resonance , photochemistry , enzyme , biochemistry , physics , mitochondrion
The EPR spectral parameters of aa 3 oxidase and cyt c 552 from Paracoccus denitrificans were studied in purified oxidase and enriched cyt c 552 . The orientation of the g ‐tensors of hemes a and c 552 were determined on partially ordered membranes, enriched cyt c 552 and a c 552 : aa 3 subcomplex. The known correlation of g ‐tensor to molecular axes in histidine/methionine ligated hemes permits us to position cyt c 552 with respect to the parent membrane. Taken together with previous data on the interaction surface between aa 3 oxidase and cyt c 552 , these results allow us to arrive at a single conformation for the c 552 : aa 3 electron transfer complex.