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Determinants of Ligand Affinity and Heme Reactivity in H‐NOX Domains
Author(s) -
Weinert Emily E.,
Plate Lars,
Whited Charlotte A.,
Olea Charles,
Marletta Michael A.
Publication year - 2010
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.200904799
Subject(s) - heme , chemistry , reactivity (psychology) , ligand (biochemistry) , nitric oxide , kinetics , nox , hemeprotein , stereochemistry , biochemistry , biophysics , receptor , biology , enzyme , organic chemistry , physics , medicine , alternative medicine , pathology , quantum mechanics , combustion
O 2 balks at extra bulk : The introduction of distal‐pocket bulk into the Thermoanaerobacter tengcongensis H‐NOX (heme nitric oxide/oxygen) domain caused key changes in the protein structure. Rearrangement of the heme pocket resulted in dramatic differences in O 2 ‐binding kinetics and heme reactivity (see picture).