Asymmetric sulfoxidation and amine binding by H64D/V68A and H64D/V68S Mb: mechanistic insight into the chiral discrimination step.
The H64D/V68A and H64D/V68S mutants of Myoglobin are found to oxidize thioanisole with high enantioselectivity and reactivity. These mutants are also capable of enantioselective binding of alpha-methylbenzylamine, which mimics an expected sulfoxidation intermediate. The kinetic study of the amine binding shows that the Fe-O bond cleavage in the intermediate may be the chiral discrimination step of the sulfoxidation.
Department of Structural Molecular Science, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan.
Shigeru
S
Kato
Hui-Jun
HJ
Yang
Takafumi
T
Ueno
Shin-ichi
S
Ozaki
George N
GN
Phillips
Shunichi
S
Fukuzumi
Yoshihito
Y
Watanabe
D007700:Kinetics; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010627:Phenethylamines / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D013237:Stereoisomerism; D013379:Substrate Specificity; D013440:Sulfides / Q000737:chemistry / Q000378:metabolism; D013454:Sulfoxides / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics
D009211:Myoglobin; D010627:Phenethylamines; D013440:Sulfides; D013454:Sulfoxides; C093850:methylphenylsulfide; C033198:1-phenethylamine