Solution Structure of Oxidized Cytochrome c6 from the Green Alga Monoraphidium braunii,

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Abstract
Cytochrome c6 from Monoraphidium braunii, an 89-amino acid electron transfer protein, has been investigated by NMR in solution, in its oxidized form, at pH 7 and 300 K. By using a combination of COSY, TOCSY, and NOESY experiments, 84% of the proton resonances have been assigned. A total of 1668 experimental NOE constraints, 1109 of which were meaningful, together with 288 pseudocontact shifts, have been used to determine the structure in solution. This is represented as a family of 40 structures which have been energy minimized. The rmsd values with respect to the mean structure are 0.57 ± 0.08 and 0.94 ± 0.09 Å for the backbone and heavy atoms, respectively. The structure has been found to be very similar to that of the reduced form, except for a rearrangement in propionate 7, a feature which has been observed in all c-type cytochromes investigated so far. Such a feature could be relevant for the efficiency of the electron transfer pathway with either the oxidizing or the reducing partners. Other differences in the oxidation states have been noted in the region proposed to be involved in the interaction with the physiological partners.