Unknown

Dataset Information

0

The nature of aqueous tunneling pathways between electron-transfer proteins.


ABSTRACT: Structured water molecules near redox cofactors were found recently to accelerate electron-transfer (ET) kinetics in several systems. Theoretical study of interprotein electron transfer across an aqueous interface reveals three distinctive electronic coupling mechanisms that we describe here: (i) a protein-mediated regime when the two proteins are in van der Waals contact; (ii) a structured water-mediated regime featuring anomalously weak distance decay at relatively close protein-protein contact distances; and (iii) a bulk water-mediated regime at large distances. Our analysis explains a range of otherwise puzzling biological ET kinetic data and provides a framework for including explicit water-mediated tunneling effects on ET kinetics.

SUBMITTER: Lin J 

PROVIDER: S-EPMC3613566 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

The nature of aqueous tunneling pathways between electron-transfer proteins.

Lin Jianping J   Balabin Ilya A IA   Beratan David N DN  

Science (New York, N.Y.) 20051101 5752


Structured water molecules near redox cofactors were found recently to accelerate electron-transfer (ET) kinetics in several systems. Theoretical study of interprotein electron transfer across an aqueous interface reveals three distinctive electronic coupling mechanisms that we describe here: (i) a protein-mediated regime when the two proteins are in van der Waals contact; (ii) a structured water-mediated regime featuring anomalously weak distance decay at relatively close protein-protein contac  ...[more]

Similar Datasets

| S-EPMC6279779 | biostudies-literature
| S-EPMC2797321 | biostudies-literature
| S-EPMC2900646 | biostudies-literature
| S-EPMC8016960 | biostudies-literature
| S-EPMC3132828 | biostudies-literature
| S-EPMC1783394 | biostudies-literature
| S-EPMC6249235 | biostudies-literature
| S-EPMC3986022 | biostudies-literature
| S-EPMC1266099 | biostudies-literature