Chemistry Reference
In-Depth Information
FIGURE 5.23 Components of the proton-translocating unit of ATP synthase (a, b) and the proton path through the membrane (c). Each proton
enters the cytosolic half-channel, follows a complete rotation of the c ring, and exits through the other half-channel into the matrix. (From Berg
et al., 2002 : pp. 974.)
REFERENCES
Abrahams, K. P., Leslie, A. G., Lutter, R., & Walker, J. E. (1994). Structure at 2.8 ˚ resolution of F 1 -ATPase from bovine heart mitochondria.
Nature, 370, 621 e 628.
Berg, J. M., Tymoczko, J. L., & Stryer, L. (2002). Biochemistry (5th ed.). New York: W.H. Freeman and Co.
Campbell, P. N., Smith, A. D., & Peters, T. J. (2005). Biochemistry illustrated niochemistry and molecular biology in the post-genomic era
(5th ed.). London and Oxford: Elsevier. pp. 242.
Capaldi, R., & Aggeler, R. (2002). Mechanism of F 1 F 0 -type ATP synthase, a biological rotary motor. TIBS, 27, 154 e 160.
Devlin, T. M. (2005). Textbook of Biochemistry with clinical correlations (6th ed.). Hoboken: John Wiley and Sons. pp. 1208.
Knowles, J. R. (1991). Enzyme catalysis: not different, just better. Nature, 350, 121 e 124.
Voet, D., & Voet, J. G. (2004). Biochemistry (3rd ed.). Hoboken: John Wiley and Sons.
 
Search WWH ::




Custom Search