EPR investigation of the role of B10 phenylalanine in neuroglobin - Evidence that B10Phe mediates structural changes in the heme region upon disulfide-bridge formation

A spectroscopic analysis shows that the B10Phe residue is essential to translate the formation of the internal disulfide bridge in human neuroglobin in a strong change of the heme-pocket conformation and that mutation of this residue leads to a reduced protein stability in the presence of H2O2.