Heme-based sensors in biological systems

Current Opinion in Chemical Biology

Volumn 3, Issue 2, 1999, Pages 158-167

  Rodgers, Kenton R ^a  

^a NORTH DAKOTA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; GUANYLATE CYCLASE; HEMOPROTEIN; NITRIC OXIDE; OXYGEN;

BIOSENSOR; BRADYRHIZOBIUM JAPONICUM; CRYSTAL STRUCTURE; NONHUMAN; REVIEW;

BRADYRHIZOBIUM JAPONICUM; RHIZOBIUM;

EID: 0033120934     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)80028-3     Document Type: Article

References (85)

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38. off) of CO; the Fe-imidazole bond remains intact in the presence of CO and YC-1. The authors also make an important point that maximal sGC stimulation by the combination of CO and YC-1 requires a partial pressure of CO beyond that which is likely to be provided endogenously by heme oxygenase.
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46. 2 boxes] of ∼50 residues each) fold. Differences between the two structures suggest that signal transmission involves large- scale motion of the FG loop, especially at Asp212. Whether this ligation-induced conformational change is coupled to its own kinase domain or that of a partner in a dimer cannot be addressed by these structures.
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54. -1 for deoxyRmFixL, which is the intermediate between myoglobin and soluble guanylyl cyclase (sGC). Formation of a sGC-type nitrosyl heme in FixL suggests the possibility of an NO-induced signal akin to that of sGC. Although this is possible in light of the reported results, there is no physiological evidence for such a signaling pathway.
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60. 2 boxes separated by helical structures. Nearly all the identified structures are sensory domains, suggesting a broad versatility of this fold in signal transduction mechanisms.
61. 1 box. Based upon locations of the heme in FixL and the 4-hydroxycinnamyl chromophore in PYP, the positions of their cofactors in the cavity of the fold are separated by about nine residues. The 4-hydroxycinnamyl cofactor is located at the end of the internal cavity near the amino terminus of the central helix, whereas the heme in the heme domain of B. japonium FixL is closer to the center of the cavity and over the center of the helix.
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81. 2+ and CO. The divalent metal ions were shown to stimulate erythropoietin (Epo) production through a common pathway consistent with transmetallation of a heme protein. Conversely, CO inhibited Epo production by locking the putative sensor in an oxy-like state.
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