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Proton nmr spectroscopy of paracoccus denitrificans cytochrome c 550



Proton nmr spectroscopy of paracoccus denitrificans cytochrome c 550



Biochemistry 23(15): 3526-3533



The 1H NMR spectra of ferri- and ferrocytochrome c-550 from P. denitrificans (ATCC 13543) were investigated at 300 MHz. The ferricytochrome c-550 shows hyperfine-shifted heme methyl resonances at 29.90, 29.10, 16.70 and 12.95 ppm, and a ligand methionyl methyl resonance at -15.80 ppm (pH 8 and 23.degree. C). Four pH-linked structural transitions were detected in spectra taken as a function of pH. The transitions were interpreted as loss of the histidine heme ligand (pK .ltoreq. 3), ionization of a buried heme propionate (pK = 6.3 .+-. 0.2), displacement of the methionine heme ligand by a lysyl amino group (pK .simeq. 10.5), and loss of the lysyl ligand (pK .gtoreq. 11.3). The temperature behavior of hyperfine-shifted resonances was determined. Two heme methyl resonances (at 16.70 and 12.95 ppm) showed downfield hyperfine shifts with increasing temperature. The cyanoferricytochrome had methyl resonances at 23.3, 20.1 and 19.4 ppm. NMR spectroscopy did not detect the formation of a complex with azide. The second-order rate constant for electron transfer between ferric and ferrous forms was determined to be 1.6 .times. 104 M -1 s-1. Heme proton resonances were assigned in both oxidation states by cross-saturation and nuclear Overhauser enhancement experiments. Spin-coupling patterns in the aromatic region of the ferrocytochrome spectrum were investigated.

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