Abstract
Conditions for the specific labelling of the tetrahaeme protein cytochrome c3 of Desulfovibrio vulgaris Miyazaki F during culture of this sulphate-reducing bacterium in a minimal medium were established. Phenylalanine and tyrosine residues were specifically deuterated at more than 85% efficiency. Cytochrome c3 has nine histidine, three tyrosine and two phenylalamine residues. Eight histidine imidazoles are ligated to four haeme groups. Using the deuterated cytochrome c3, aromatic proton signals of phenylalanine and tyrosine residues in the fully oxidized state were identified. However, the signals of one phenylalanine residue were missing and this was tentatively assigned to Phe20. The aromatic proton signals of His67 were also assigned p2H titration. Its pk1 was much higher than that for the free histidine residue. No tyrosine residue was ionized up to p2H 12.
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