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Proton nmr studies of the coordination geometry at the heme iron and the electronic structure of the heme group in cytochrome c 552 from euglena gracilis



Proton nmr studies of the coordination geometry at the heme iron and the electronic structure of the heme group in cytochrome c 552 from euglena gracilis



Biochimica et Biophysica Acta 626(1): 15-22



The 1H-NMR lines of heme c in reduced and oxidized cytochrome c-552 from E. gracilis were assigned and coordination geometry of the axial ligands was investigated. The electronic structure of the heme and chirality of the axially bound methionine were the same type as in mammalian cytochrome c, but different from cytochrome c-551 from Pseudomonas aeruginosa. A previously proposed correlation between chirality of attachment of the axial methionine and electronic wave functions in oxidized cytochromes of the c type was supported. Comparison of mammalian cytochrome c, cytochrome c-551 and cytochrome c-552 indicated that chirality of the axially bound methionine was not linked with the evolutionary increase of the polypeptide chain length.

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Accession: 006215941

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Related references

1H-NMR studies of the coordination geometry at the heme iron and the electronic structure of the heme group in cytochrome c-552 from Euglena gracilis. Biochimica et Biophysica Acta 626(1): 15-22, 1980

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