生物化学资料：Biological Oxidation.pptVIP

Mitochondrial ATP synthase complex. (d) Side view of the FoF1 structure. This is a composite, in which the crystallographic coordinates of bovine mitochondrial F1 (shades of purple and gray) have been combined with those of yeast mitochondrial Fo (shades of yellow and orange). Subunits a, b, ?, and ? were not part of the crystal structure shown here. (e) The FoF1 structure, viewed end-on in the direction P side to N side. The major structures visible in this cross section are the two transmembrane helices of each of ten c subunits arranged in concentric circles. (f) Diagram of the FoF1 complex, deduced from biochemical and crystallographic studies. The two b subunits of Fo associate firmly with the ? and ? subunits of F1, holding them fixed relative to the membrane. In Fo, the membrane-embedded cylinder of c subunits is attached to the shaft made up of F1 subunits ? and ?. As protons flow through the membrane from the P side to the N side through Fo, the cylinder and shaft rotate, and the ? subunits of F1 change conformation as the ? subunit associates with each in turn. On the basis of detailed kinetic and binding studies of the reactions catalyzed by FoF1, Paul Boyer proposed a rotational catalysis mechanism in which the three active sites of F1 take turns catalyzing ATP synthesis. On the basis of detailed kinetic and binding studies of the reactions catalyzed by FoF1, Paul Boyer proposed a rotational catalysis mechanism in which the three active sites of F1 take turns catalyzing ATP synthesis. There is a remarkable and instructive exception to the general rule that respiration slows when the ATP supply is adequate. Most newborn mammals, including humans, have a type of adipose tissue called brown fat in which fuel oxidation serves not to produce ATP but to generate heat to keep the newborn warm. This specialized adipose tissue is brown because of the presence of large numbers of mitochondria and thus large amounts of cytochromes, whose heme groups are strong abs