Dynamics of Myoglobin−CO with the Proximal Histidine Removed:  Vibrational Echo Experiments

Picosecond infrared vibrational echo measurements from 60 to 300 K on CO bound to the active site of a mutant myoglobin, H93G(N-MeIm), are presented and compared to measurements on native myoglobin and on the mutant H64V. Although in H93G(N-MeIm) (the proximal histidine replaced by glycine, with exo...

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Veröffentlicht in:The journal of physical chemistry. B 1998-01, Vol.102 (2), p.331-333
Hauptverfasser: Rector, K. D, Engholm, J. R, Hill, J. R, Myers, D. J, Hu, R, Boxer, Steven G, Dlott, Dana D, Fayer, M. D
Format: Artikel
Sprache:eng
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