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Spectral studies of horse heart porphyrin cytochrome c


, : Spectral studies of horse heart porphyrin cytochrome c. Journal of Biological Chemistry 259(11): 6931-6936

Removal of the heme iron from cytochrome c to generate porphyrin cytochrome c relieves the quenching of porphyrin fluorescence and enhances the fluorescence of the single tryptophan residue and the 4 tyrosine residues. The intensity of the porphyrin fluorescence is not perturbed by denaturation of the protein at neutral pH using either urea or guanidine hydrochloride. However, the amplitude of tryptophan fluorescence is increased by these denaturants from 5 to about 85% of a model tryptophan residue using solutions of 2 microM tryptophan. In contrast to cytochrome c, the tryptophan fluorescence amplitude of denatured porphyrin cytochrome c is independent of pH over the range pH 3.0 to 7.4. Acidification of solutions of either native or denatured porphyrin cytochrome c markedly alters both the visible absorbance and fluorescence of the protein consistent with protonation of two pyrrole nitrogens on the porphyrin. Preliminary analysis of the spectral changes occurring in the acid transition suggests the presence of an intermediate form having only one of these two pyrrole nitrogens protonated.

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Accession: 006459930

PMID: 6327700

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Related references

Vitello L.B.; Erman J.E., 1987: Binding of horse heart cytochrome c to yeast porphyrin cytochrome c peroxidase a fluorescence quenching study on the ionic strength dependence of the interaction. The binding of horse heart cytochrome c to yeast cytochrome c peroxidase in which the heme group was replaced by protoporphyrin IX was determined by a fluorescence quenching technique. The association between ferricytochrome c and cytochrome c per...

Kojo S.; Sang S.; Fukunishi K., 1981: Degradation of horse heart cytochrome c to a single dia stereo isomeric porphyrin c. Journal of the Chemical Society Chemical Communications (23): 1223-1224

Slama, J.T.; Willson, C.G.; Grimshaw, C.E.; Rapoport, H., 1977: Stereochemistry of the porphyrin-protein bond of cytochrome c. Stereochemical comparison of Rhodospirillum rubrum, yeast, and horse heart porphyrins c. Porphyrins c have been obtained from Rhodospirillum rubrum cytochrome c2, yeast cytochrome c, and horse heart cytochrome c and compared using proton magnetic resonance and circular dichroism. Identity of the spectra establishes that chemically and...

Borin, G.; Filippi, B.; Cavaggion, F.; Marchiori, F., 1977: Studies on cytochrome c. XIV. Synthesis of the protected heptadecapeptide (sequence 88-104) of horse heart cytochrome c. A solution synthesis is described of the partially protected N alpha-benzyloxycarbonylheptadecapeptide Z-Lys (Tfa)-Thr-Glu-Arg-Glu-Asp-Leu-Ile-Ala-Tyr-Leu-Lys (Tfa)-Lys (Tfa)-Ala-Thr-Asn-Glu (OBu t)-OBu t corresponding to sequence 88-104 of horse...

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Kihara, H.; Nakatani, H.; Hiromi, K.; Hon-Nami, K., 1977: Kinetic studies on redox reactions of hemoproteins. I. Reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide. The oxidation-reduction reaction of horse heart cytochrome c and cytochrome c (552, Thermus thermophilus), which is highly thermoresistant, was studied by temperature-jump method. Ferrohexacyanide was used as reductant. (Formula: see text.) Thermo...

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