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Measurement of Heme Synthesis Levels in Mammalian Cells
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Influence of heme c attachment on heme conformation and potential

Jesse G Kleingardner1,2, Benjamin D Levin3, Giorgio Zoppellaro4

  • 1Department of Chemistry, University of Rochester, Rochester, NY, 14627-0216, USA.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|August 26, 2018
PubMed

Insights

Variations in heme attachment motifs, like CX3CH and CX4CH, influence heme ruffling and reduction potentials in cytochrome c. These findings impact understanding of natural heme peptides and engineering novel structures.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Spectroscopy

Background:

  • Heme c proteins feature a heme group covalently attached to a polypeptide chain.
  • The typical attachment involves a CXXCH motif, forming thioether bonds with cysteine residues and histidine as a ligand.
  • Some cytochromes c utilize noncanonical motifs like CX3CH or CX4CH with more intervening residues.

Purpose of the Study:

  • To investigate the impact of variations in heme attachment motifs on heme ruffling and electronic structure.
  • To spectroscopically characterize CX3CH and CX4CH variants of Hydrogenobacter thermophilus cytochrome c552, alongside a novel CXCH variant.

Main Methods:

  • Spectroscopic characterization including 1H and 13C NMR, EPR, and resonance Raman spectroscopy.
  • Analysis of spectral data to determine the extent of heme ruffling.
  • Measurement of reduction potentials using protein film voltammetry.

Main Results:

  • CXCH and CX4CH variants exhibited enhanced heme ruffling compared to canonical motifs.
  • These variants also displayed lower reduction potentials.
  • The study provides insights into the structural and electronic consequences of altered heme attachment sites.

Conclusions:

  • Noncanonical heme attachment motifs can significantly alter heme structure and redox properties.
  • These findings have implications for understanding the diversity of natural cytochromes c.
  • The results inform the engineering of novel heme-binding peptides with tailored characteristics.

Keywords:
Cytochrome cCytochrome c maturationHeme distortionHeme rufflingReduction potential

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