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 multiwa...

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Bibliographic Details
Published in:The journal of physical chemistry. B 2006-01, Vol.110 (1), p.530-536
Main Authors: Adams, Kristl L, Tsoi, Stanislav, Yan, Jiusheng, Durbin, Stephen M, Ramdas, Anant K, Cramer, William A, Sturhahn, Wolfgang, Alp, E. Ercan, Schulz, Charles
Format: Article
Language:English
Subjects:
Cytochromes f - chemistry
Iron - chemistry
Myoglobin - chemistry
Oxidation-Reduction
Protein Conformation
Sensitivity and Specificity
Spectrum Analysis - methods
Spectrum Analysis, Raman - methods
Vibration
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Summary: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. Modes not seen by Raman due to optical selection rules appear in the NRVS spectrum. The mean Fe force constant extracted from the VDOS illustrates how Fe dynamics varies among these four monoheme proteins, and is correlated with oxidation and spin state trends seen in model heme compounds. The protein's contribution to Fe motion is dominant at low frequencies, where coupling to the backbone tightly constrains Fe displacements in cytochrome f, in contrast to enhanced heme flexibility in myoglobin.
ISSN:1520-6106
1520-5207
DOI:10.1021/jp053440r