2S3-6 Torque, Speed and Steps of the Bacterial Flagellar Motor(2S3 Structure and functional mechanism of the bacterial flagellar motor,The 46th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri Biophysical Society of Japan 48:supplement (2008) s9

Authors:

Chien-Jung Lo, Richard M Berry

3P-133 Step detection of flagellar rotation at high temporal and spatial resolution(The 46th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri Biophysical Society of Japan 48:supplement (2008) s148

Authors:

Yoshiyuki Sowa, Richard M Berry

ATP synthesis without R210 of subunit a in the Escherichia coli ATP synthase

Biochimica et Biophysica Acta - Bioenergetics 1777:1 (2008) 32-38

Authors:

RR Ishmukhametov, JB Pond, A Al-Huqail, MA Galkin, SB Vik

Characterization and Application of Controllable Local Chemical Changes Produced by Reagent Delivery from a Nanopipet.

J. Am. Chem. Soc. 130 (2008) 10387-10393

Authors:

JD Piper, C Li, C-J Lo, R Berry, Y Korchev, L Ying, D Klenerman

Abundance of Escherichia coli F1-ATPase molecules observed to rotate via single-molecule microscopy with gold nanorod probes.

J Bioenerg Biomembr 39:5-6 (2007) 435-439

Authors:

J York, D Spetzler, T Hornung, R Ishmukhametov, J Martin, WD Frasch

Abstract:

The abundance of E. coli F1-ATPase molecules observed to rotate using gold nanorods attached to the gamma-subunit was quantitated. Individual F1 molecules were determined to be rotating based upon time dependent fluctuations of red and green light scattered from the nanorods when viewed through a polarizing filter. The average number of F1 molecules observed to rotate in the presence of GTP, ATP, and without nucleotide was approximately 50, approximately 25, and approximately 4% respectively. In some experiments, the fraction of molecules observed to rotate in the presence of GTP was as high as 65%. These data indicate that rotational measurements made using gold nanorods provide information of the F1-ATPase mechanism that is representative of the characteristics of the enzyme population as a whole.