Dayle M. A. Smith
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Research Interests
Dayle M. A. Smith has a total of 4 co-authors. Here are the top co-authors by number of shared publications:
Kevin M. Rosso
Department of Physics, Whitman College, Walla Walla, Washington 99362, and Environmental Dynamics and Simulation, Chemical Sciences Division, Molecular Interactions and Transformations, Chemical Sciences Division, Molecuar Sciences Software Group, Environmental Molecular Sciences Laboratory, and Computational Biology and Bioinformatics, Computational Sciences and Mathematics Division, Pacific Northwest National Laboratory, Richland, Washington 99352
1 shared publicationMarat Valiev
Department of Physics, Whitman College, Walla Walla, Washington 99362, and Environmental Dynamics and Simulation, Chemical Sciences Division, Molecular Interactions and Transformations, Chemical Sciences Division, Molecuar Sciences Software Group, Environmental Molecular Sciences Laboratory, and Computational Biology and Bioinformatics, Computational Sciences and Mathematics Division, Pacific Northwest National Laboratory, Richland, Washington 99352
1 shared publicationMichel Dupuis
Department of Physics, Whitman College, Walla Walla, Washington 99362, and Environmental Dynamics and Simulation, Chemical Sciences Division, Molecular Interactions and Transformations, Chemical Sciences Division, Molecuar Sciences Software Group, Environmental Molecular Sciences Laboratory, and Computational Biology and Bioinformatics, Computational Sciences and Mathematics Division, Pacific Northwest National Laboratory, Richland, Washington 99352
1 shared publicationT. P. Straatsma
Department of Physics, Whitman College, Walla Walla, Washington 99362, and Environmental Dynamics and Simulation, Chemical Sciences Division, Molecular Interactions and Transformations, Chemical Sciences Division, Molecuar Sciences Software Group, Environmental Molecular Sciences Laboratory, and Computational Biology and Bioinformatics, Computational Sciences and Mathematics Division, Pacific Northwest National Laboratory, Richland, Washington 99352
1 shared publication
Latest Publications
- 18 July 2006
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry B
- Vol. 110 (31) , 15582-15588
Electronic Coupling between Heme Electron-Transfer Centers and Its Decay with Distance Depends Strongly on Relative Orientation
A method for calculating the electron-transfer matrix element VRP using density functional theory Kohn−Sham orbitals is presented and applied to heme dimers of varying relative orientation. The electronic coupling decays with increased iron separation according to VRP = exp(−βr/2) with a distance dependence parameter β ≈ 2 Å-1 for hemes with parallel porphyrins and either 1.1 or 4.0 Å-1 when the porphyrin planes are perpendicular, depending on the alignment of the iron dπ orbital. These findings are used to interpret the observed orientation of the hemes in tetraheme redox proteins such as Flavocytochrome c3 fumarate reductase (Ifc3, PDB code 1QJD) of Shewanella frigidimarina, another flavocytochrome from the same bacterium (Fcc3, 1E39) and a small tetraheme cytochrome of Shewanella oneidensis strain MR1 (1M1P). Our results show that shifting and rotating the hemes controls the adiabaticity of the three electron hopping steps.
- 18 July 2006
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry B
- Vol. 110 (31) , 15582-15588
Electronic Coupling between Heme Electron-Transfer Centers and Its Decay with Distance Depends Strongly on Relative Orientation
A method for calculating the electron-transfer matrix element VRP using density functional theory Kohn−Sham orbitals is presented and applied to heme dimers of varying relative orientation. The electronic coupling decays with increased iron separation according to VRP = exp(−βr/2) with a distance dependence parameter β ≈ 2 Å-1 for hemes with parallel porphyrins and either 1.1 or 4.0 Å-1 when the porphyrin planes are perpendicular, depending on the alignment of the iron dπ orbital. These findings are used to interpret the observed orientation of the hemes in tetraheme redox proteins such as Flavocytochrome c3 fumarate reductase (Ifc3, PDB code 1QJD) of Shewanella frigidimarina, another flavocytochrome from the same bacterium (Fcc3, 1E39) and a small tetraheme cytochrome of Shewanella oneidensis strain MR1 (1M1P). Our results show that shifting and rotating the hemes controls the adiabaticity of the three electron hopping steps.