Table 1 Mo–ligand and SSub–O distances in the various structures obtained in this study.

From: QM/MM study of the reaction mechanism of sulfite oxidase

MPT

State

Distance to Mo (Å)

Distance to SSub (Å)

SCys

S1

S2

Oax

Oeq

O1

O2

O3

Oeq

MPD

R

2.44

2.49

2.45

1.76

1.76

1.56

1.56

1.64

2.58

 

TS1

2.43

2.43

2.42

1.75

2.05

1.52

1.52

1.54

1.90

IM

2.43

2.39

2.40

1.74

2.34

1.53

1.51

1.52

1.58

TS2

2.42

2.34

2.37

1.74

3.30

1.54

1.51

1.53

1.54

P

2.42

2.33

2.37

1.75

4.08

1.54

1.50

1.54

1.53

MPH

R

2.42

2.50

2.45

1.76

1.76

1.55

1.56

1.63

2.54

 

TS1

2.41

2.45

2.45

1.74

1.96

1.53

1.54

1.55

2.00

IM

2.42

2.39

2.42

1.74

2.29

1.51

1.51

1.53

1.60

TS2

2.40

2.33

2.38

1.74

3.70

1.51

1.51

1.55

1.54

P

2.40

2.33

2.38

1.74

3.85

1.54

1.51

1.54

1.54

MPO

R

2.42

2.51

2.46

1.76

1.76

1.55

1.56

1.63

2.52

 

TS1

2.41

2.46

2.45

1.74

1.96

1.53

1.53

1.55

2.00

IM

2.41

2.39

2.42

1.74

2.28

1.51

1.51

1.53

1.60

P

2.40

2.33

2.38

1.74

3.85

1.54

1.51

1.54

1.54

  1. SSub, O1, O2 and O3 are the four atoms of the substrate. SCys is the S atom of Cys185. S1 and S2 are the two S atoms of MPT. Oax and Oeq are the two oxo ligands of Mo.
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