期刊
NATURE CHEMICAL BIOLOGY
卷 1, 期 1, 页码 53-59出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio704
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资金
- NIGMS NIH HHS [F32GM069302] Funding Source: Medline
Soluble guanylate cyclases (sGCs) function as heme sensors that selectively bind nitric oxide (NO), triggering reactions essential to animal physiology. Recent discoveries place sGCs in the H-NOX family (heme nitric oxide/oxygen-binding domain), which includes bacterial proteins from aerobic and anaerobic organisms. Some H-NOX proteins tightly bind oxygen (O-2), whereas others show no measurable affinity for O-2, providing the basis for selective NO signaling in aerobic cells. Using a series of wild-type and mutant H-NOXs, we established a molecular basis for ligand discrimination. A distal pocket tyrosine is requisite for O-2 binding in the H-NOX family. These data suggest that sGC uses a kinetic selection against O-2; we propose that the O-2 dissociation rate in the absence of this tyrosine is fast and that a stable O-2 complex does not form.
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