Coupling coherence distinguishes structure sensitivity in protein electron transfer.
Journal Article (Journal Article)
Quantum mechanical analysis of electron tunneling in nine thermally fluctuating cytochrome b562 derivatives reveals two distinct protein-mediated coupling limits. A structure-insensitive regime arises for redox partners coupled through dynamically averaged multiple-coupling pathways (in seven of the nine derivatives) where heme-edge coupling leads to the multiple-pathway regime. A structure-dependent limit governs redox partners coupled through a dominant pathway (in two of the nine derivatives) where axial-ligand coupling generates the single-pathway limit and slower rates. This two-regime paradigm provides a unified description of electron transfer rates in 26 ruthenium-modified heme and blue-copper proteins, as well as in numerous photosynthetic proteins.
Full Text
Duke Authors
Cited Authors
- Prytkova, TR; Kurnikov, IV; Beratan, DN
Published Date
- February 2007
Published In
Volume / Issue
- 315 / 5812
Start / End Page
- 622 - 625
PubMed ID
- 17272715
Pubmed Central ID
- PMC3523119
Electronic International Standard Serial Number (EISSN)
- 1095-9203
International Standard Serial Number (ISSN)
- 0036-8075
Digital Object Identifier (DOI)
- 10.1126/science.1134862
Language
- eng