Tracing the structure-function relationship of neuroglobin and cytoglobin using resonance Raman and electron paramagnetic resonance spectroscopy.
The physiological role of neuroglobin and cytoglobin, two vertebrate globins discovered in the last 5 years, is not yet clearly understood. In this work, we review the structural information on these globins and its implication on the possible protein function, obtained by electron paramagnetic resonance and resonance Raman spectroscopy. All studies reveal a high flexibility in the heme-pocket region of neuroglobin. Together with the observation that the distal ligand of the heme iron is the endogenous E7-histidine in both the ferric and ferrous form of neuroglobin and cytoglobin, the flexibility of the heme environment in neuroglobin will play a crucial role in the globins' ability to bind and stabilize exogenous ligands.
Van Doorslaer
S
S
Department of Physics, University of Antwerp, Wilrijk-Antwerp, Belgium. sabine.vandoorslaer@ua.ac.be
Vinck
E
E
Trandafir
F
F
Ioanitescu
I
I
Dewilde
S
S
Moens
L
L
D000818:Animals; D003553:Cystine; D000078842:Cytoglobin; D004578:Electron Spin Resonance Spectroscopy; D005914:Globins / Q000737:chemistry / Q000378:metabolism*; D006418:Heme / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D051379:Mice; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism*; D000078787:Neuroglobin; D009569:Nitric Oxide / Q000378:metabolism; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism*; D013059:Spectrum Analysis, Raman; D013329:Structure-Activity Relationship
C000627265:CYGB protein, human; C000627267:Cygb protein, mouse; D000078842:Cytoglobin; D009419:Nerve Tissue Proteins; D000078787:Neuroglobin; D009687:Nuclear Proteins; D009569:Nitric Oxide; D006418:Heme; D003553:Cystine; D005914:Globins