Moessbauer Study of Reduced Putidaredoxin in Zero and Intermediate Applied Fields
type: CreativeWork
description: An ('57)Fe Mossbauer investigation of the reduced (S = 1/2) active center of the redox and effector protein, putidaredoxin, is reported. Putidaredoxin is a prototype of a 2Fe-2S protein; it functions as an electron shuttle in a bacterial enzyme system. Several 2Fe-2S proteins, including putidaredoxin, have already been subjected to numerous Mossbauer and magnetic resonance studies, but current understanding of the active center is still very incomplete, and the mechanism of electron transfer is not known.
abstract: An ('57)Fe Mossbauer investigation of the reduced (S = 1/2) active center of the redox and effector protein, putidaredoxin, is reported. Putidaredoxin is a prototype of a 2Fe-2S protein; it functions as an electron shuttle in a bacterial enzyme system. Several 2Fe-2S proteins, including putidaredoxin, have already been subjected to numerous Mossbauer and magnetic resonance studies, but current understanding of the active center is still very incomplete, and the mechanism of electron transfer is not known.
author: Valentine, Mark
language: eng
keywords: Mathematics, Physics, Molecular, Biophysics, General
date published: 2015-05-13T15:41:37Z
date modified: 2026-07-22T22:26:10Z
provider: University of Illinois - Urbana-Champaign
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Illinois at Urbana-Champaign

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2142/77356