Solution 1h NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin.
The solution 1H NMR spectrum of oxidized (met) mouse neuroglobin, metNgb, demonstrates that it is low-spin and hexacoordinate with strong spectral similarities to ferricytochrome b5. The axial ligands are identified as His(F8) and His(E7), with the latter exhibiting an unstrained Fe-His bond. The presence of two sets of resonances is shown to arise from equilibrium heme orientational isomers ( approximately 2:1). The ligation of cyanide is shown to be extraordinarily slow with a factor approximately 2 difference in rate for the two heme orientations. Not only is Ngb the first mamalian globin with equilibrium heme disorder, but the disorder also has additional functional consequences.
Du
Weihong
W
Department of Chemistry, University of California-Davis, Davis, CA 95616, USA.
Syvitski
Ray
R
Dewilde
Sylvia
S
Moens
Luc
L
La Mar
Gerd N
GN
D000818:Animals; D005914:Globins / Q000737:chemistry*; D006418:Heme / Q000737:chemistry*; D051379:Mice; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D000078787:Neuroglobin; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D012996:Solutions
D009419:Nerve Tissue Proteins; D000078787:Neuroglobin; D012996:Solutions; D006418:Heme; D005914:Globins