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The Structural Plasticity of the Proximal [4Fe3S] Cluster is Responsible for the O 2 Tolerance of Membrane‐Bound [NiFe] Hydrogenases
Author(s) -
Mouesca JeanMarie,
FontecillaCamps Juan C.,
Amara Patricia
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.201209063
Subject(s) - hydrogenase , deprotonation , structural plasticity , chemistry , cluster (spacecraft) , plasticity , crystallography , computer science , stereochemistry , biochemistry , biology , materials science , computer network , enzyme , neuroscience , ion , organic chemistry , composite material
The main difference between O 2 ‐sensitive and O 2 ‐tolerant [NiFe] hydrogenases is the plasticity of the proximal [4Fe3S] cluster in the latter hydrogenase (see scheme). Deprotonation of a conserved glutamate residue initiates the movement of the iron atom, resulting in its binding to the amide nitrogen atom of one of the two supernumerary cysteine ligands and superoxidation of the proximal cluster.