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Tracing the Structure‐Function Relationship of Neuroglobin and Cytoglobin using Resonance Raman and Electron Paramagnetic Resonance Spectroscopy
Author(s) -
Van Doorslaer S.,
Vinck E.,
Trandafir F.,
Ioanitescu I.,
Dewilde S.,
Moens L.
Publication year - 2004
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540500037877
Subject(s) - neuroglobin , globin , resonance raman spectroscopy , heme , chemistry , myoglobin , biophysics , resonance (particle physics) , raman spectroscopy , histidine , nuclear magnetic resonance , biochemistry , biology , hemoglobin , physics , amino acid , atomic physics , optics , enzyme
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 functions, 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.IUBMB Life, 56: 665‐670, 2004