Many enzymes require the presence of nonprotein chemical “partners” in order to function (Table 8.2):
Type of molecule | Role in catalyzed reactions |
---|---|
Prosthetic groups | |
Heme | Binds ions, O2, and electrons |
FAD | Carries electrons/protons |
Retinal | Converts light energy |
Inorganic cofactors | |
Iron (Fe2+ or Fe3+) | Oxidation/reduction |
Copper (Cu+ or Cu2+) | Oxidation/reduction |
Zinc (Zn2+) | Stabilizes DNA binding structure |
Coenzymes | |
Biotin | Carries —COO– |
Coenzyme A | Carries —CO— |
NAD | Carries electrons/protons |
ATP | Provides/extracts energy |
Prosthetic groups are distinct, non–
Inorganic cofactors include ions such as copper, zinc, and iron that are permanently bound to certain enzymes. For example, the enzyme alcohol dehydrogenase contains the cofactor zinc.
A coenzyme is a nonprotein carbon-
A coenzyme moves from enzyme to enzyme, adding or removing chemical groups from the substrate. A coenzyme is like a substrate in that it does not permanently bind to the enzyme: it binds to the active site, changes chemically during the reaction, and then separates from the enzyme to participate in other reactions. There is actually no clear distinction between the functions of coenzymes and some substrates. For example, ATP and ADP have been described as coenzymes, even though they are really substrates that gain or lose phosphate groups during chemical reactions. The term “coenzyme” was coined before the functions of these molecules were fully understood. Biochemists continue to use the term, and for consistency with the field, we use it in this book.