Fe Vibrational Spectroscopy of Myoglobin and Cytochromef

Fe vibrational spectroscopy of myoglobin and cytochrome f.

The Fe vibrational density of states (VDOS) has been determined for the heme proteins deoxymyoglobin, metmyoglobin, and cytochrome f in the oxidized and reduced states, using nuclear resonance vibrational spectroscopy (NRVS). For cytochrome f in particular, the NRVS spectrum is compared with multiwavelength resonance Raman spectra to identify those Raman modes with significant Fe displacement. ...

Vibrational spectroscopy and normal-mode analysis of Fe(II) octaethylporphyrin.

The normal-mode spectrum for the four-coordinated heme compound Fe(II) octaethylporphyrin, Fe(OEP), has been determined by refining force constants to the experimental Fe vibrational density of states measured with nuclear resonance vibrational spectroscopy (NRVS). Convergence of the calculated spectrum to the data was achieved by first imposing D4 symmetry on the model structure as well as the...

Nuclear Resonance Vibrational Spectroscopy (NRVS) of Fe–S model compounds, Fe–S proteins, and nitrogenase

We have used nuclear resonance vibrational spectroscopy (NRVS) to examine the nature of the Fe–S unit. Specifically, vibrational characteristics have been determined, and through incremental steps in model system complexity, applied to analysis of the enzyme nitrogenase. This stepwise strategy demonstrates NRVS as a viable bioinorganic tool, and will undoubtedly increase the application of sync...

Vibrational spectroscopy and imaging.

Vibrational Spectroscopy of C60

The fullerene era was started in 1985 with the discovery of the stable C60 cluster and its interpretation as a cage structure with the familiar shape of a soccer ball [1]. An explosive growth in fullerene research was triggered in 1990 by the development of a method to produce fullerenes in bulk quantities [2]. Subsequently, the structural, electronic, and vibrational properties of many fullere...