Structural change of the heme pocket due to disulfide bridge formation is significantly larger for neuroglobin than for cytoglobin.
Human neuroglobin (hNgb) and human cytoglobin (hCygb), two recently discovered members of the vertebrate globin family, are known to be able to form an intramolecular disulfide bridge. Using electron paramagnetic resonance (EPR), we show that formation of a disulfide bridge in ferric hNgb causes a considerable change in the heme pocket structure, whereas this is not so clear for ferric hCygb. The structural results can be related nicely to earlier histidine and dioxygen affinity studies of the ferrous proteins.
Vinck
Evi
E
Department of Physics, University of Antwerp, B-2610 Antwerp, Belgium.
Van Doorslaer
Sabine
S
Dewilde
Sylvia
S
Moens
Luc
L
D000078842:Cytoglobin; D004220:Disulfides / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D005914:Globins / Q000737:chemistry*; D006418:Heme / Q000737:chemistry*; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D000078787:Neuroglobin; D011487:Protein Conformation
C000627265:CYGB protein, human; D000078842:Cytoglobin; D004220:Disulfides; D009419:Nerve Tissue Proteins; D000078787:Neuroglobin; D006418:Heme; D005914:Globins