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Mössbauer spectra of the heme peptide (HP) 1–50 and the heme peptide:non-heme peptide (NHP) non-covalent complex 1–50:51–104 derived from cytochrome c: evidence for cytochrome c iron site solvation in aqueous solution

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Abstract

Mössbauer spectroscopic studies on a heme peptide (HP) derived from cytochrome c and on the HP recombined non-covalently with the remaining cleaved section are reported. The results suggest that the environment of the heme site in the known crystal structure of cytochrome c may differ in detail from the environment of the heme in the working protein.

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Authors and Affiliations

  1. MRC Biomembrane Research Unit, Department of Chemical Pathology, University of Cape Town Medical School, Observatory, Cape Town, Republic of South Africa

    Paul A. Adams

  2. MRC Regulatory Peptides Research Unit, Department of Chemical Pathology, University of Cape Town Medical School, Observatory, Cape Town, Republic of South Africa

    Raymond C. de L. Milton

  3. Department of Chemistry and Biological Chemistry, University of Essex, Colchester, Essex, UK

    Jack Silver

Authors
  1. Paul A. Adams
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  2. Raymond C. de L. Milton
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  3. Jack Silver
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Adams, P.A., de L. Milton, R.C. & Silver, J. Mössbauer spectra of the heme peptide (HP) 1–50 and the heme peptide:non-heme peptide (NHP) non-covalent complex 1–50:51–104 derived from cytochrome c: evidence for cytochrome c iron site solvation in aqueous solution. Biometals 7, 217–220 (1994). https://doi.org/10.1007/BF00149551

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  • DOI: https://doi.org/10.1007/BF00149551

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