The first direct measurements of this translocation made use of the displacement, from the target DNA, of a triple helix
and this allowed the rate of translocation to be determined (Firman & Szczelkun, 2000).  The EcoR124I enzyme used
in these studies was able to translocate DNA in a bi-directional, highly processive manner at ~400 bp s-1 (Figure 5).

Firman & Szczelkun (2000) were subsequently able to demonstrate that the R1-complex was also able to translocate DNA in a unidirectional manner.  Although not as processive as the holoenzyme, the R1-complex is still able to translocate at a comparable rate to the holoenzyme, but does not cut the DNA when translocation is blocked (Firman, unpublished observations).  Instead, the enzyme appears to reset when translocation is halted and then begin the process again.  It is also able to perform this re-setting process at the end of a linear DNA molecule (see video).

Therefore, this R1-complex provides an ATP-driven molecular machine that can act as a molecular actuator by
moving objects attached to the end of the DNA.