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J Biol Chem. 2013 Sep 27;288(39):27702-11. doi: 10.1074/jbc.R113.473249. Epub 2013 Aug 8.

Heme-based globin-coupled oxygen sensors: linking oxygen binding to functional regulation of diguanylate cyclase, histidine kinase, and methyl-accepting chemotaxis.

Author information

1
From the Department of Biochemistry, Faculty of Science, Charles University in Prague, 128 43 Prague 2, Czech Republic.

Abstract

An emerging class of novel heme-based oxygen sensors containing a globin fold binds and senses environmental O2 via a heme iron complex. Structure-function relationships of oxygen sensors containing a heme-bound globin fold are different from those containing heme-bound PAS and GAF folds. It is thus worth reconsidering from an evolutionary perspective how heme-bound proteins with a globin fold similar to that of hemoglobin and myoglobin could act as O2 sensors. Here, we summarize the molecular mechanisms of heme-based oxygen sensors containing a globin fold in an effort to shed light on the O2-sensing properties and O2-stimulated catalytic enhancement observed for these proteins.

KEYWORDS:

Chemotaxis; Cyclic GMP (cGMP); Heme; Hemoglobin; Histidine Kinases; Myoglobin; Oxygen Binding

PMID:
23928310
PMCID:
PMC3784688
DOI:
10.1074/jbc.R113.473249
[Indexed for MEDLINE]
Free PMC Article

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