1H NMR and ESR studies of oxidized cytochrome c551 from Pseudomonas aeruginosa.

Near neutral pH, Fe(III) cytochrome c551 exhibits an ESR absorption due primarily to a single species with g values of 3.24, 2.06, and 1.48. These g values are somewhat different from those of horse heart cytochrome c and can be interpreted by the generalizations of Brautigan et al. [(1977) J. Biol. Chem. 252, 574] to be due to Fe binding by the imidazole anion of histidine rather than by neutral imidazole. The NMR spectrum of Fe(III) cytochrome c551 exhibits a number of hyperfine-shifted peaks whose pattern shows similarities to but many differences from that of horse heart cytochrome c. Variation in shifts of some of the peaks in the pH range 5--9 is ascribed to ionization of a somewhat buried propionic acid side chain (pK = 5.8) and to ionization of the N-terminal NH3+ group (pK = 7.7). At alkaline pH greater than 9.4, as shown by a variety of optical and ESR spectral changes, the Met-61 S ligand is replaced by other ligands.