PMID: 9533619Apr 9, 1998Paper

Nitric oxide myoglobin: crystal structure and analysis of ligand geometry

Proteins
E A BruckerG N Phillips

Abstract

The structure of the ferrous nitric oxide form of native sperm whale myoglobin has been determined by X-ray crystallography to 1.7 angstroms resolution. The nitric oxide ligand is bent with respect to the heme plane: the Fe-N-O angle is 112 degrees. This angle is smaller than those observed in model compounds and in lupin leghemoglobin. The exact angle appears to be influenced by the strength of the proximal bond and hydrogen bonding interactions between the distal histidine and the bound ligand. Specifically, the N(epsilon) atom of histidine64 is located 2.8 angstroms away from the nitrogen atom of the bound ligand, implying electrostatic stabilization of the FeNO complex. This interpretation is supported by mutagenesis studies. When histidine64 is replaced with apolar amino acids, the rate of nitric oxide dissociation from myoglobin increases tenfold.

Citations

Aug 11, 2005·Journal of the American Chemical Society·Weiqiao ZengJ Timothy Sage
Dec 21, 2006·Journal of the American Chemical Society·Mohammed IbrahimThomas G Spiro
Feb 16, 2008·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Changliang Xu, G Spiro Thomas
Jan 24, 2009·Journal of the American Chemical Society·Nathan J SilvernailW Robert Scheidt
Dec 1, 2007·Journal of Biological Physics·Karin Nienhaus, G Ulrich Nienhaus
Nov 27, 2009·Antioxidants & Redox Signaling·Mayumi KajimuraMakoto Suematsu
Mar 12, 2010·Journal of the American Chemical Society·Alexandra V SoldatovaThomas G Spiro
Mar 30, 2010·Archives of Biochemistry and Biophysics·Paola D'AngeloAndrea Battistoni
May 13, 1999·Biochimica Et Biophysica Acta·F Cutruzzolà
Dec 26, 2006·Biochemical and Biophysical Research Communications·Paolo Ascenzi, Mauro Fasano
Jul 1, 2014·IUBMB Life·Paolo AscenziMassimo Coletta
May 12, 2010·The FEBS Journal·Paolo AscenziMassimo Coletta

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