Abstract

The initial electron transfer rate and protein dynamics in wild type and five mutant reaction centers from Rhodobacter sphaeroides have been studied as a function of temperature (10-295 K). Detailed kinetic measurements of initial electron transfer in Rhodobacter sphaeroides reaction centers can be quantitatively described by a reaction diffusion formalism at all temperatures from 10 to 295 K. In this model, the time course of electron transfer is determined by the ability of the protein to interconvert between conformations until one is found where the activation energy for electron transfer is near zero. In reaction centers with a free energy for electron transfer similar to wild type, the reaction proceeds at least as fast at cryogenic temperatures as at room temperature. This may be because interconversion between conformations at low temperature is restricted to conformations with near zero activation energy (it is not possible to diffuse away from this region of conformational space). In contrast, mutants with a decreased free energy initially find themselves in conformations unfavorable for electron transfer and require more extensive conformational diffusion to achieve a low activation energy conformation. They therefore undergo electron transfer more slowly at 10 K vs 295 K.

Original languageEnglish (US)
Pages (from-to)818-824
Number of pages7
JournalJournal of Physical Chemistry B
Volume113
Issue number3
DOIs
StatePublished - Jan 22 2009

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electron transfer
proteins
Proteins
Conformations
temperature dependence
Electrons
Activation energy
Temperature
activation energy
Free energy
free energy
cryogenic temperature
Cryogenics
formalism
Kinetics
temperature
kinetics
room temperature

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films

Cite this

Unusual temperature dependence of photosynthetic electron transfer due to protein dynamics. / Wang, Haiyu; Lin, Su; Katilius, Evaldas; Laser, Christa; Allen, James; Williams, Joann; Woodbury, Neal.

In: Journal of Physical Chemistry B, Vol. 113, No. 3, 22.01.2009, p. 818-824.

Research output: Contribution to journalArticle

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abstract = "The initial electron transfer rate and protein dynamics in wild type and five mutant reaction centers from Rhodobacter sphaeroides have been studied as a function of temperature (10-295 K). Detailed kinetic measurements of initial electron transfer in Rhodobacter sphaeroides reaction centers can be quantitatively described by a reaction diffusion formalism at all temperatures from 10 to 295 K. In this model, the time course of electron transfer is determined by the ability of the protein to interconvert between conformations until one is found where the activation energy for electron transfer is near zero. In reaction centers with a free energy for electron transfer similar to wild type, the reaction proceeds at least as fast at cryogenic temperatures as at room temperature. This may be because interconversion between conformations at low temperature is restricted to conformations with near zero activation energy (it is not possible to diffuse away from this region of conformational space). In contrast, mutants with a decreased free energy initially find themselves in conformations unfavorable for electron transfer and require more extensive conformational diffusion to achieve a low activation energy conformation. They therefore undergo electron transfer more slowly at 10 K vs 295 K.",
author = "Haiyu Wang and Su Lin and Evaldas Katilius and Christa Laser and James Allen and Joann Williams and Neal Woodbury",
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AU - Wang, Haiyu

AU - Lin, Su

AU - Katilius, Evaldas

AU - Laser, Christa

AU - Allen, James

AU - Williams, Joann

AU - Woodbury, Neal

PY - 2009/1/22

Y1 - 2009/1/22

N2 - The initial electron transfer rate and protein dynamics in wild type and five mutant reaction centers from Rhodobacter sphaeroides have been studied as a function of temperature (10-295 K). Detailed kinetic measurements of initial electron transfer in Rhodobacter sphaeroides reaction centers can be quantitatively described by a reaction diffusion formalism at all temperatures from 10 to 295 K. In this model, the time course of electron transfer is determined by the ability of the protein to interconvert between conformations until one is found where the activation energy for electron transfer is near zero. In reaction centers with a free energy for electron transfer similar to wild type, the reaction proceeds at least as fast at cryogenic temperatures as at room temperature. This may be because interconversion between conformations at low temperature is restricted to conformations with near zero activation energy (it is not possible to diffuse away from this region of conformational space). In contrast, mutants with a decreased free energy initially find themselves in conformations unfavorable for electron transfer and require more extensive conformational diffusion to achieve a low activation energy conformation. They therefore undergo electron transfer more slowly at 10 K vs 295 K.

AB - The initial electron transfer rate and protein dynamics in wild type and five mutant reaction centers from Rhodobacter sphaeroides have been studied as a function of temperature (10-295 K). Detailed kinetic measurements of initial electron transfer in Rhodobacter sphaeroides reaction centers can be quantitatively described by a reaction diffusion formalism at all temperatures from 10 to 295 K. In this model, the time course of electron transfer is determined by the ability of the protein to interconvert between conformations until one is found where the activation energy for electron transfer is near zero. In reaction centers with a free energy for electron transfer similar to wild type, the reaction proceeds at least as fast at cryogenic temperatures as at room temperature. This may be because interconversion between conformations at low temperature is restricted to conformations with near zero activation energy (it is not possible to diffuse away from this region of conformational space). In contrast, mutants with a decreased free energy initially find themselves in conformations unfavorable for electron transfer and require more extensive conformational diffusion to achieve a low activation energy conformation. They therefore undergo electron transfer more slowly at 10 K vs 295 K.

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