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Table 1 List of the model parameters

From: On the control mechanisms of the nitrite level in Escherichia coli cells: the mathematical model

Parameter

Parameter name

Parameter value

Sub system

Estimation source

k flow

the flow rate constant

1.65 · 10−4 s−1

(1)

[1]

δ nrf, 1

parameters of the m nrf generalized function that describes the nrf operon activity changes in relation to the nitrite concentration established in the chemostat

60

(6)

[1], [35]

K nrf ,1

0.36 mM

h nrf ,1

1.3

δ nrf, 2

0.16

K nrf ,2

1.7 mM

h nrf ,2

3.0

ks Nrf

the maximum specific rate of the NrfA and NrfB proteins synthesis

1.13 10−5 mM/s

(6)

[*]b

ks NirC

the maximum specific rate of the NirC potein synthesis

7.3 · 10−5

mM/s

(6)

k s NirB = = k s NirD

the maximum specific rate of the NirB and NirD proteins synthesis

k s NirB = = k s NirC / 5

(6)

k d , Nrf

the rate constant for the NrfA and NrfB monomers degradation in cytoplasm

9.6 10−5 s−1

(11)

[29]

kt Nrf , cp

the rate constant for the NrfA and NrfB passage into the periplasm

0.01 s –1

(7)

[*]b

kt Nrf , pc

the rate constant for the NrfA and NrfB transport into the cytoplasm

10 s –1

(7)

k dis , NrfAB

the rate constant for the NrfAB dimer dissociation into subunits

10 s –1

(9)

 

K dis , NrfAB

the equilibrium dissociation constant for the NrfAB dimer

0.00004 mM

(9)

[18]

k dis , N r f A 2 B 2

the rate constant for the Nrf(AB)2 dissociation into two NrfAB dimer proteins

10 s –1

(9)

K dis , N r f A 2 B 2

the equilibrium dissociation constant for the NrfA2B2 tetramer

0.004 mM

(9)

δ peripl

the constant for the cytoplasmic volume to periplasmic volume ratio

6

(7)

[25]

d U

parameters of the U generalized function that describes membrane potential relative value in relation to the added NO2

3

(7)

[16]

δ

0.015

K pmf ,1

0.115 mM

h pmf ,1

2

K pmf ,2

0.83 mM

h pmf ,2

17

ω 1, ω 2 с

0с

(7)

[*]b

K pmf ,3 с

2.2

h pmf ,3 с

15

k d , NrfA

the rate constant for the NrfA monomer degradation in cytoplasm

9.6 10−6

sec –1

(11)

[29]

k d , NrfA

the rate constant for the NrfA monomer degradation in the periplasm

k d , NrfAB

the rate constant for the NrfAB degradation

k d , N r f A 2 B 2

the rate constant for the NrfA2B2 degradation

k cat , N r f A 2 B 2 u

the rate constant for the NrfA reductase turnover

700 s –1

(2)

[9]

K dis , N r f A 2 B 2 u

the NrfA reductase Michaelis constant for nitrite

0.03 mM

[10]

δ nir, 1

parameters of the m nir generalized function that describes the nir operon activity changes in relation to the nitrite concentration established in the chemostat

7.86

(6)

[1], [35]

K nir ,1

1.0 mM

h nir ,1

2.0

δ nir, 2

5.76

K nir ,2

1.7 mM

h nir ,2

8.3

K dis , N i r B 2

the equilibrium dissociation constant for the NirB2 association reaction

0.002 mM

(10)

[*]b

K dis , N i r B 2 D

the equilibrium dissociation constant for the NirB2D trimer association reaction

0.002 mM

(10)

k cat , N i r B 2 D w

the rate constant for the NirB enzyme catalytic turnover

1100.0 s –1

(5)

[*]b

K dis , N i r B 2 D w

assumed to be equal the NirB reductase Michaelis constant

0.006 mM

[21]

K dis , N i r C 5

the rate constant for the NirC5 dissociation

0.0475 mM

(8)

[*]b

k cat , NirCin

the rate constant for nitrite import by the NirC protein

100 s –1

(3)

[*]b

K dis , N i r C 5 u

assumed to be equal the Michaelis constant for nitrite import by the NirC protein

1 mM

(3)

[31]

k cat , NirCout

the rate constant for the nitrite export by the NirC protein

1000 s−1

(4)

[*]b

K dis , N i r C 5 w

assumed to be equal the Michaelis constant for the nitrite export by the NirC protein

1 mM

(4)

[31]

k d,NirC

the rate constant for the NirC monomer degradation

0.0011 s−1

(11)

[*]b

k d,NirC5

the rate constant for the NirC5 pentamer degradation

0.00011 s−1

k d,NirB

the rate constant for the NirВ monomer degradation

0.00011 s−1

k d,NirD

the rate constant for the NirD monomer degradation

0.00011 s−1

k d,NirB2

the rate constant for the NirВ2 dimer degradation

0.000011 s−1

k d,NirB2D

the rate constant for the NirВ2D dimer degradation

0.000011 sec−1

C

cell volume relative fraction in chemostat

0.0003

(2, 3)

[7], [29]

  1. a – mM (millimole/litre), sec (second), if dimension is not specified, the quantity is dimensionless
  2. b – parameter value was estimated based on the experimental data
  3. c – members, before which the ω 1 and ω 2 coefficients are standing in the membrane potential formula, are zeroed in (1) model, the formula used in the model calculation is with nrf operon constitutive expression and enabled NirC and NirB enzymes functions