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Protein Dynamics from Intramolecular Electron Transfer

Published online by Cambridge University Press:  10 February 2011

G. U. Nienhaus ,
B. H. McMahon ,
J. D. Müller  and
C. A. Wraight
G. U. Nienhaus
Affiliation:
Dept. of Biophysics, University of Ulm, D-89069 Ulm, Germany, [email protected] Dept. of Plant Biology, University of Illinois, Urbana IL 61801, USA
B. H. McMahon
Affiliation:
Dept. of Physics, University of Illinois, Urbana IL 61801, USA
J. D. Müller
Affiliation:
Dept. of Physics, University of Illinois, Urbana IL 61801, USA
C. A. Wraight
Affiliation:
Dept. of Plant Biology, University of Illinois, Urbana IL 61801, USA
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Abstract

Proteins are complex systems that share essential properties with viscous liquids and polymers. Structure, dynamics, and function of proteins are strongly interrelated, and structural and dynamic aspects can be revealed by studying protein function. Here we report measurements of the kinetics of intramolecular electron transfer (ET) from the primary quinone (QA) to the special pair (P) of reaction center (RC) proteins from Rhodobacter sphaeroides as a function of temperature (5 to 300 K) and illumination protocol (cooled in the dark and under illumination from 280 K). From the data, information about structural heterogeneity, relaxations and fluctuations of these molecules is obtained.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 455: Symposium T – Glasses and Glass Formers–Current Issues , 1996 , 337
Copyright
Copyright © Materials Research Society 1997

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References

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