Requiring only two hydrogen bonds to be bound to its complement, it is a crucial component of both an important second-messenger protein and the principal energy transfer molecule in the human body.
The permeability transition pore of one of the cristae contains a protein named for its ability to transport this molecule. It has two nitrogen-containing rings connected to an amine functional group, and is theorized to have been first formed from the polymerization of five hydrogen cyanide molecules. Formerly known as vitamin B4, it was one of the subjects of Edwin Chargaff's studies during the 1940s. Requiring only two hydrogen bonds to be bound to its complement, it is a crucial component of both an important second-messenger protein and the principal energy transfer molecule in the human body. FTP, name this nitrogenous base, a purine that pairs with thymine in DNA.
The permeability transition pore of one of the cristae contains a protein named for its ability to transport this molecule.
adenine