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Editorial
. 2008 Nov 21;3(11):673-5.
doi: 10.1021/cb800269h.

A twist on heme signaling

Thomas Spiro  1
Affiliations
Editorial

A twist on heme signaling

Thomas Spiro. ACS Chem Biol. .

Abstract

Proteins in the H-NOX family act as sensors of NO or O2. This family includes soluble guanylate cyclase (sGC), the NO sensor that is responsible for vasodilation and neurotransmission in mammals. The crystal structures of bacterial H-NOX domains have revealed a highly distorted heme cofactor. This distortion has now been shown to be associated with a concerted displacement of the entire N-terminal half of the protein. This displacement likely provides the mechanism for transducing the ligand binding event into signaling.

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Figures

Figure 1
Figure 1
Heme prosthetic group (right) and a view of its distortion (left) in Tt H-NOX, showing the non-bonded contact with Pro115 (from ref 1).
Figure 2
Figure 2
Overlay of wild-type (gold) and P115A (silver) variants of Tt H-NOX molecules, showing the heme flattening and the concertedmovement of the N-terminal half of the structure, associated with theresidue substitution (from ref 1).
See this image and copyright information in PMC

Comment on

References

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