Picosecond dynamics of ligand interconversion in the primary docking site of heme proteins

Journal of the American Chemical Society

Volumn 127, Issue 16, 2005, Pages 5786-5787

  Kim, Seongheun ^a   Lim, Manho ^a  

^a Pusan National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN; MYOGLOBIN;

ARTICLE; BINDING KINETICS; BINDING SITE; CONFORMATIONAL TRANSITION; INFRARED SPECTROSCOPY; LIGAND BINDING; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN STRUCTURE;

ANIMALS; BINDING SITES; CARBON MONOXIDE; CARBOXYHEMOGLOBIN; HEMOGLOBINS; KINETICS; MYOGLOBIN; THERMODYNAMICS;

EID: 17744370742     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja050734h     Document Type: Article

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32. In the first 100 ps, two states interconvert without geminate recombination and ligand escape. Consequently, other states (bound, secondary pockets, and solvent) need not be included in this analysis. The fact that the total integrated area remains constant after the initial growth indicates that the population of CO in each state is proportional to its integrated absorbance,