| Autor: |
Adams KL; Department of Physics, Purdue University, West Lafayette, Indiana 47907, USA., Tsoi S, Yan J, Durbin SM, Ramdas AK, Cramer WA, Sturhahn W, Alp EE, Schulz C |
| Jazyk: |
angličtina |
| Zdroj: |
The journal of physical chemistry. B [J Phys Chem B] 2006 Jan 12; Vol. 110 (1), pp. 530-6. |
| DOI: |
10.1021/jp053440r |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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