Coupling coherence distinguishes structure sensitivity in protein electron transfer.

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 2, 2007

Published In

Volume / Issue

  • 315 / 5812

Start / End Page

  • 622 - 625

PubMed ID

  • 17272715

Electronic International Standard Serial Number (EISSN)

  • 1095-9203

Digital Object Identifier (DOI)

  • 10.1126/science.1134862

Language

  • eng

Conference Location

  • United States