Title

Solvent tuning of electrochemical potentials in the active sites of HiPIP versus ferredoxin

Document Type

Article

Publication Date

2007

Abstract

A persistent puzzle in the field of biological electron transfer is the conserved iron-sulfur cluster motif in both high potential iron-sulfur protein (HiPIP) and ferredoxin (Fd) active sites. Despite this structural similarity, HiPIPs react oxidatively at physiological potentials, whereas Fds are reduced. Sulfur K-edge x-ray absorption spectroscopy uncovers the substantial influence of hydration on this variation in reactivity. Fe-S covalency is much lower in natively hydrated Fd active sites than in HiPIPs but increases upon water removal; similarly, HiPIP covalency decreases when unfolding exposes an otherwise hydrophobically shielded active site to water. Studies on model compounds and accompanying density functional theory calculations support a correlation of Fe-S covalency with ease of oxidation and therefore suggest that hydration accounts for most of the difference between Fd and HiPIP reduction potentials.

Publication Title

Science

Volume

318

Issue

5855

First Page

1464

Last Page

1468

Comments

This article was published in Science, Volume 318, Issue 5855, Pages 1464-1468.

The published version is available at http://dx.doi.org/10.1126/science.1147753.

Copyright © 2007 AAAS.

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