help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Biophysical Journal 70: 2092-2099 (1996)
© 1996 the Biophysical Society

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Melchers, B
Right arrow Articles by Leone, M
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Melchers, B
Right arrow Articles by Leone, M

Structural fluctuations of myoglobin from normal-modes, Mössbauer, Raman, and absorption spectroscopy.

B Melchers, E W Knapp, F Parak, L Cordone, A Cupane and M Leone

Freie Universität Berlin, Fachbereich Chemie, Institut für Kristallographie, Berlin, Germany.

ABSTRACT

A normal-mode analysis of carbon monoxymyoglobin (MbCO) and deoxymyoglobin (Mb) with 170 water molecules is performed for (54)Fe and (57)Fe. A projection is defined that extracts iron out-of-plane vibrational modes and is used to calculate spectra that can be compared with those from resonance Raman scattering. The calculated spectra and the isotopic shift (57)Fe versus (54)Fe agree with the experimental data. At low temperatures the average mean square fluctuations (MSFs) of the protein backbone atoms agree with molecular dynamics simulation. Below 180 K the MSFs of the heme iron agree with the data from Mossbauer spectroscopy. The MSFs of the iron atom relative to the heme are an order of magnitude smaller than the total MSFs of the iron atom. They agree with the data from optical absorption spectroscopy. Thus the MSFs of the iron atom as measured by Mossbauer spectroscopy can be used to probe the overall motion of the heme within the protein matrix, whereas the Gaussian thermal line broadening of the Soret band and the resonance Raman bands can be used to detect local intramolecular iron-porphyrin motions.




This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
Z. W. Cao, Y. Xue, L. Y. Han, B. Xie, H. Zhou, C. J. Zheng, H. H. Lin, and Y. Z. Chen
MoViES: molecular vibrations evaluation server for analysis of fluctuational dynamics of proteins and nucleic acids
Nucleic Acids Res., July 1, 2004; 32(suppl_2): W679 - W685.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
P. W. Fenimore, H. Frauenfelder, B. H. McMahon, and F. G. Parak
Slaving: Solvent fluctuations dominate protein dynamics and functions
PNAS, December 10, 2002; 99(25): 16047 - 16051.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
V. Reat, R. Dunn, M. Ferrand, J. L. Finney, R. M. Daniel, and J. C. Smith
Solvent dependence of dynamic transitions in protein solutions
PNAS, August 29, 2000; 97(18): 9961 - 9966.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
V. Reat, H. Patzelt, M. Ferrand, C. Pfister, D. Oesterhelt, and G. Zaccai
Dynamics of different functional parts of bacteriorhodopsin: H-2H labeling and neutron scattering
PNAS, April 28, 1998; 95(9): 4970 - 4975.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Cupane, M. Leone, V. Militello, F. K. Friedman, A. P. Koley, G. B. Vasquez, W. S. Brinigar, M. Karavitis, and C. Fronticelli
Modification of alpha -Chain or beta -Chain Heme Pocket Polarity by Val(E11) right-arrow Thr Substitution Has Different Effects on the Steric, Dynamic, and Functional Properties of Human Recombinant Hemoglobin. DEOXY DERIVATIVES
J. Biol. Chem., October 17, 1997; 272(42): 26271 - 26278.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1996 by the Biophysical Society.