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| | ATP Hydrolysis in the B^sub TP^ and B^sub DP^ Catalytic Sites of F^sub 1^-ATPase Biophysical Journal - Find Articles (Site not responding. Last check: 2007-10-16) |
 | | Notwithstanding a large amount of biochemical and, recently, structural data, we still lack an understanding of how ATP hydrolysis in F^sub 1^ is coupled to mechanical motion and how the catalytic sites achieve cooperativity during rotatory catalysis. |
 | | This is evidenced by the fact that during steady-state hydrolysis the three binding pockets exhibit different binding affinities for ATP, i.e., there is a high, a medium, and a low affinity site with K^sub d^ values for ATP of ?50 nmol, 0.5 µmol, and 25 µmol, respectively (Weber et al., 1994). |
 | | For the catalytic sites this meant that the effect of specific protein side chains on the hydrolysis reaction could be related to their spatial location with respect to the nucleotide. |
| www.findarticles.com /p/articles/mi_qa3938/is_200411/ai_n9464965 (887 words) |
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