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Near‐Atomic Resolution Neutron Crystallography on Perdeuterated Pyrococcus furiosus Rubredoxin: Implication of Hydronium Ions and Protonation State Equilibria in Redox Changes
Author(s) -
Cuypers M. G.,
Mason S. A.,
Blakeley M. P.,
Mitchell E. P.,
Haertlein M.,
Forsyth V. Trevor
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201207071
Subject(s) - rubredoxin , pyrococcus furiosus , protonation , crystallography , chemistry , thermostability , ion , biochemistry , organic chemistry , enzyme , archaea , gene
Neutron crystallographic analyses at near‐atomic resolution are presented for both reduced and oxidized forms of perdeuterated Pyrococcus furiosus rubredoxin, a small iron–sulfur redox protein with remarkable thermostability. Hydronium ions may play a key role in the protonation and charge‐transfer processes associated with the oxidized and reduced forms of the protein. Picture: overall structure showing D 3 O + ions (red and gray molecules).