MoFe protein 

2 pairs of identical subunits (tetramer, nif D & nif K)

A total of MW 180 ~ 235kD

Each subunit has 2 Mo-Fe-S clusters.

Both Fe proteins and MoFe proteins are sensitive to O2. 

TLS Online TPP Program

#Id: 9270

#XL - Q Biochemistry

MoFe protein 

2 pairs of identical subunits (tetramer, nif D & nif K)

A total of MW 180 ~ 235kD

Each subunit has 2 Mo-Fe-S clusters.

Both Fe proteins and MoFe proteins are sensitive to O2. 

TLS Online TPP Program

#Id: 9270

#XL - S Microbiology

MoFe protein 

2 pairs of identical subunits (tetramer, nif D & nif K)

A total of MW 180 ~ 235kD

Each subunit has 2 Mo-Fe-S clusters.

Both Fe proteins and MoFe proteins are sensitive to O2. 

TLS Online TPP Program

#Id: 8556

#XL - Q Biochemistry

The simplest forms of competitive inhibition considered are sometimes termed linear competitive inhibition because both primary and secondary plots are linear. 

TLS Online TPP Program

#Id: 8557

#XL - Q Biochemistry

In more complicated systems, the primary plots may be linear but the secondary plots non-linear. For example, if not one but two molecules of inhibitor can bind to the substrate binding site, then parabolic competitive inhibition is said to occur, because of the shape of the secondary and Dixon plots.

TLS Online TPP Program

#Id: 8558

#XL - Q Biochemistry

Similarly, if the inhibitor binds to a different site from the substrate and reduces the affinity of the enzyme for the substrate without altering the reaction characteristics of that substrate which does bind, then hyperbolic competitive inhibition results

TLS Online TPP Program

#Id: 8559

#XL - Q Biochemistry

Dixon plot for competitive inhibition

TLS Online TPP Program

#Id: 8560

#XL - Q Biochemistry

TLS Online TPP Program

#Id: 8561

#XL - Q Biochemistry

Uncompetitive inhibitors bind only to the enzyme-substrate complex and not to the free enzyme.