Metalloproteins in which the active site is a transition metal complex bound to sulphur atoms are essential components of enzymes involved in electron transfer processes.
Examples include blue copper proteins and nitrous oxide reductase.
The function of these enzymes is dependent on the fact that the transition metal ion can undergo redox reactions.
Other examples include iron–sulfur clusters as well as many copper, nickel, and iron proteins.
Most pervasive are the ferrodoxins, which serve as electron shuttles in cells.
In bacteria, the important nitrogenase enzymes contains an Fe–Mo–S cluster and is a catalyst that performs the important function of nitrogen fixation, converting atmospheric nitrogen to ammonia that can be used by microorganisms and plants to make proteins, DNA, RNA, alkaloids, and the other organic nitrogen compounds necessary for life.
Metalloproteins in which the active site is a transition metal complex bound to sulphur atoms are essential components of enzymes involved in electron transfer processes. Examples include blue copper proteins and nitrous oxide reductase. The function of these enzymes is dependent on the fact that the transition metal ion can undergo redox reactions.Other examples include iron–sulfur clusters as well as many copper, nickel, and iron proteins. Most pervasive are the ferrodoxins, which serve as electron shuttles in cells. In bacteria, the important nitrogenase enzymes contains an Fe–Mo–S cluster and is a catalyst that performs the important function of nitrogen fixation, converting atmospheric nitrogen to ammonia that can be used by microorganisms and plants to make proteins, DNA, RNA, alkaloids, and the other organic nitrogen compounds necessary for life.
Sulfur