Determinants of Ligand Affinity and Heme Reactivity in H-NOX Domains

O2 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 O2‐binding kinetics and heme reactivity (...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2010-01, Vol.49 (4), p.720-723
Main Authors: Weinert, Emily E, Plate, Lars, Whited, Charlotte A, Olea, Charles Jr, Marletta, Michael A
Format: Article
Language:English
Subjects:
bioinorganic chemistry
Guanylate Cyclase - chemistry
Heme - chemistry
heme proteins
Hydrogen Bonding
iron
Kinetics
ligand affinity
Ligands
Nitric Oxide - chemistry
Oxygen - chemistry
Oxygen - metabolism
Protein Binding
Protein Structure, Tertiary
structural biology
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Summary:O2 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 O2‐binding kinetics and heme reactivity (see picture).
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200904799