Dynamics of the heme cofactor and coupling of heme dynamics to polypeptide within proteins are expected to influence protein function. To characterize the dynamics of heme iron within the electron transfer protein cytochrome c, nuclear resonance vibrational spectroscopy (NRVS) has been performed on H. thermophilus cytochrome c552 and a series of isotopically-labeled derivatives. Analysis of the NRVS spectra reveals strong vibrational coupling between the heme iron and the protein surface where protein-protein interactions take place. Functional implications of this finding will be discussed.

Coupling between iron and polypeptide dynamics in cytochrome <i>c</i> revealed by nuclear resonance vibrational spectroscopy

245th National Meeting (2013)

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Coupling between iron and polypeptide dynamics in cytochrome c revealed by nuclear resonance vibrational spectroscopy