Abstract

Recent studies have sparked heated debate over whether catalytical reactions would enhance the diffusion coefficients D of enzymes. Through high statistics of the transient (600 s) displacements of unhindered single molecules freely diffusing in common buffers, we here quantify D for four highly contested enzymes under catalytic turnovers. We thus formulate how precisions of better than {+/-}1% may be achieved for D at the 95% confidence level, and show no changes in diffusivity for catalase, urease, aldolase, and alkaline phosphatase under the application of wide concentration ranges of substrates. Our single-molecule approach thus overcomes potential limitations and artifacts underscored by recent studies to show no enhanced diffusion in enzymatic reactions. Table of Contents artwork O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=57 SRC="FIGDIR/small/452795v1_ufig1.gif" ALT="Figure 1"> View larger version (11K): org.highwire.dtl.DTLVardef@1c78ba4org.highwire.dtl.DTLVardef@1a0c727org.highwire.dtl.DTLVardef@73027dorg.highwire.dtl.DTLVardef@a87771_HPS_FORMAT_FIGEXP M_FIG C_FIG