FoF1-ATPase, rotary motor and biosensor

Abstract

F(o)F(1)-ATPase is an amazing molecular rotary motor at the nanoscale. Single molecule technologies have contributed much to the understanding of the motor. For example, fluorescence imaging and spectroscopy revealed the physical rotation of isolated F(1) and F(o), or F(o)F(1) holoenzyme. Magnetic tweezers were employed to manipulate the ATP synthesis/hydrolysis in F(1), and proton translation in F(o). Here, we briefly review our recent works including a systematic kinetics study of the holoenzyme, the mechanochemical coupling mechanism, reconstituting the delta-free F(o)F(1)-ATPase, direct observation of F(o) rotation at single molecule level and activity regulation through external links on the stator.

Silica Three-Dimensional Biosensors

“…In other words, the significant differences in fluorescence intensity compared with negative control suggest the successful capture of target molecule. F 0 F 1 -ATPase, a mitochondrial F 0 F 1 -ATP synthase, has a unique property due to its quickly rotary characteristics [12,13]. As we know, the F 0 F 1 motor has many rotary subunits such as α-subunits, β-subunits and ε-subunits.…”

“…F 0 F 1 -ATPase, one of important molecular motor, is a rotating biological molecular motor and is responsible for the biological energy conversion in vivo [12,13]. F 0 F 1 -ATPase consists of two parts, F 0 (ab2cn) and F 1 (α3β3γδε), and they are embedded in the membrane and prominent in membrane respectively [14][15][16].…”

Collective mechanism of molecular motors and a dynamic mechanical model for sarcomere

“…According to the asymmetrical periodicity of active free energy, we define the potential ( , ) i V x t as follows [19,20]:…”

δ-Free FoF1-ATPase, Nanomachine and Biosensor

“…The surface in Fig.2(b) also shows the sigmoid kinetics with respect to ∆pH at different Q (Junesch & Gräber, 1987;. The relation between k h /k s and ∆pH and damping coefficient of "rotor" can be determined by a stochastic mechanochemical coupling model (Li et al, 2009;Shu & Shi, 2004;Shu & Lai, 2008;Shu et al, 2010) …”

“…However, if the diffusions of the substrates and proton in buffer are rapid enough, i.e., the time that the system takes to achieve steady concentrations of substrates and proton inside is much less than the rate-limiting rotational step, the dynamics of this system can be directly derived form Eqs.1 with different initial conditions as shown in Fig.3. Here, we assumed that the rate-limiting rotational step is equal to the rate of ATP hydrolysis/synthesis and may approximately be calculated from Refs (Shu & Lai, 2008;Shu et al, 2010) Here, we only need to estimate the upper limit of the ATP diffusion time since ATP is the biggest molecule involved with radius ∼ 0.7 nm (Ravshan & Yasunobu, 2004). The distance to be covered is, therefore, at most, the radius of the vesicle which has been taken to be R v = 350 nm.…”