Electron-transfer reactions in proteins: electronic coupling in myoglobin
- Creators
- Siddarth, Prabha
-
Marcus, R. A.
Abstract
Recent measurements of electron-transfer (ET) rates in Ru(NH_3)_5 His myoglobin derivatives have shown the need for improved theories for treating the "path" of long-range ET. We have investigated these systems theoretically using a combined artificial intelligence (AI)-superexchange method. As in our previous articles, this model first employs an AI search technique that yields the important amino acid residues for the mediation of electrons between the donor and the acceptor. A quantum mechanical method is then used to diagonalize the orbitals of the selected protein subset and to calculate the electronic coupling. Encouraging agreement with experimental data is found, no adjustable parameters having been introduced. The results yield the relevant amino acid paths.
Additional Information
© 1993 American Chemical Society. Received: March 19, 1993; In Final Form: April 20, 1993. We thank Harry Gray for stimulating discussions. P.S. is grateful to Gary Brayer for the use of his computer facilities at UBC, where part of this work was performed. It is a pleasure to acknowledge the support of this research by the National Science Foundation, the Office of Naval Research, and the Arnold and Mabel Beckman Foundation. We would like to dedicate this article to Professor Zbignew R. Grabowski, in recognition of his insightful contributions to charge transfer and of the conference at Pultuskin 1992, celebrating his 65th birthday.Additional details
- Eprint ID
- 56835
- DOI
- 10.1021/j100125a004
- Resolver ID
- CaltechAUTHORS:20150421-133036781
- NSF
- Office of Naval Research (ONR)
- Arnold and Mabel Beckman Foundation
- Created
-
2015-04-21Created from EPrint's datestamp field
- Updated
-
2021-11-10Created from EPrint's last_modified field
- Other Numbering System Name
- Caltech Arthur Amos Noyes Laboratory
- Other Numbering System Identifier
- 8763