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. 2010;49(4):720-3.
doi: 10.1002/anie.200904799.

Determinants of ligand affinity and heme reactivity in H-NOX domains

Emily E Weinert  1 , Lars Plate, Charlotte A Whited, Charles Olea Jr, Michael A Marletta
Affiliations

Determinants of ligand affinity and heme reactivity in H-NOX domains

Emily E Weinert et al. Angew Chem Int Ed Engl. 2010.
No abstract available

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Figures

Figure 1
Figure 1
Structure of WT Tt H-NOX heme pocket.[4] The heme and key residues are shown in green. L144 and I75 are highlighted in blue.
Figure 2
Figure 2
A. Overlay of WT Tt (green) and I75F/L144F (purple) structures. The structures have been aligned along the C-terminal β-sheets since this alignment resulted in the hemes being approximately overlaid. A calculated distance difference matrix (Figure S2) shows that the C-terminal β-sheets change very little between the structures. B. Heme environments of WT and I75F/L144F highlighting changes in inter-atom distances and heme planarity and tilt.
Figure 3
Figure 3
Heme environment of the I75F/L144F mutant (purple) as compared to WT Tt H-NOX (green). A. Arrangement of F75 and F144 (blue) in the distal pocket. B. Changes in positioning of adjacent residue F78 upon introduction of the phenylalanine mutations.
Scheme 1
Scheme 1
NO dioxygenation reaction.
See this image and copyright information in PMC

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