Table 2 Liquid chromatography mass spectrometry analyses of EcFrmR proteins treated with formaldehyde.

From: The mechanism of a formaldehyde-sensing transcriptional regulator

Protein sample

Measured mass (Da)

Relative abundance (a. u.)

Mass difference(Da)a

Commentb

EcFrmR

10186.60

2.0 × 107

0.1

FrmR monomer

20371.02

4.4 × 106

−2.18

FrmR disulfide-linked dimer

HCHO-treated EcFrmR

10187.02

1.8 × 106

0.52

FrmR monomer

20396.87

2.0 × 105

23.67

FrmR dimer with 2 methylene bridges

40768.73

2.0 × 105

22.30

Two FrmR dimers, each with 1 methylene bridge, linked to form a tetramer by 1 disulfide bond

HCHO-treated EcFrmR plus Zn(II)

10187.01

1.8 × 106

0.51

FrmR monomer

20396.95

3.0 × 105

23.75

FrmR dimer with 2 methylene bridges

Zn(II)-treated EcFrmR plus HCHO

10187.04

1.8 × 106

0.54

FrmR monomer

20396.99

4.0 × 105

23.79

FrmR dimer with 2 methylene bridges

HCHO-treated EcFrmR(P2A)

20319.69

4.0 × 105

−1.11

FrmR(P2A) disulfide-linked dimer

HCHO-treated EcFrmR(P2A)c

10190.71

6.8 × 105

29.91

Hydroxymethylated FrmR(P2A) monomer

HCHO-treated EcFrmR(C35A)

20307.40

2.8 × 106

−1.40

FrmR(C35A) disulfide-linked dimer

HCHO-treated EcFrmR(C35A)c

20307.21

1.7 × 105

−1.59

FrmR(C35A) disulfide-linked dimer

  1. aDifference between predicted mass and measured mass.
  2. bInterpretation of mass difference; disulfide bond, −2.2 Da; methylene bridge, net mass gain 12 Da; hydroxymethylation, net mass gain 30 Da.
  3. cExposure to formaldehyde without quenching.