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

This Article
Right arrow Full Text
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 Flores, M.
Right arrow Articles by Bemski, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Flores, M.
Right arrow Articles by Bemski, G.

Biophys J, April 2000, p. 2107-2115, Vol. 78, No. 4

Proton Electron Nuclear Double Resonance from Nitrosyl Horse Heart Myoglobin: The Role of His-E7 and Val-E11

Marco Flores, Eliane Wajnberg, and George Bemski

Centro Brasileiro de Pesquisas Físicas, 22290-180 Rio de Janeiro, Brazil

Electron nuclear double resonance (ENDOR) spectroscopy has been used to study protons in nitrosyl horse heart myoglobin (MbNO). 1H ENDOR spectra were recorded for different settings of the magnetic field. Detailed analysis of the ENDOR powder spectra, using computer simulation, based on the "orientation-selection" principle, leads to the identification of the available protons in the heme pocket. We observe hyperfine interactions of the N(HisF8)-Fe2+-N(NO) complex with five protons in axial and with eight protons in the rhombic symmetry along different orientations, including those of the principal axes of the g-tensor. Protons from His-E7 and Val-E11 residues are identified in the two symmetries, rhombic and axial, exhibited by MbNO. Our results indicate that both residues are present inside the heme pocket and help to stabilize one particular conformation.

Biophys J, April 2000, p. 2107-2115, Vol. 78, No. 4
© 2000 by the Biophysical Society   0006-3495/00/04/2107/09  $2.00



This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
C. Karunakaran, H. Zhang, J. P. Crow, W. E. Antholine, and B. Kalyanaraman
Direct Probing of Copper Active Site and Free Radical Formed during Bicarbonate-dependent Peroxidase Activity of Bovine and Human Copper,Zinc-superoxide Dismutases: LOW-TEMPERATURE ELECTRON PARAMAGNETIC RESONANCE AND ELECTRON NUCLEAR DOUBLE RESONANCE STUDIES
J. Biol. Chem., July 30, 2004; 279(31): 32534 - 32540.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Van Doorslaer, S. Dewilde, L. Kiger, S. V. Nistor, E. Goovaerts, M. C. Marden, and L. Moens
Nitric Oxide Binding Properties of Neuroglobin. A CHARACTERIZATION BY EPR AND FLASH PHOTOLYSIS
J. Biol. Chem., February 7, 2003; 278(7): 4919 - 4925.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by the Biophysical Society.