Dos, a Heme-Binding PAS Protein fromEscherichia coli, Is a Direct Oxygen Sensor†

Vondolee Marie Delgado-Nixon; Gonzalo Gonzalez; Marie-Alda Gilles-Gonzalez

doi:10.1021/bi991911s

Dos, a Heme-Binding PAS Protein fromEscherichia coli, Is a Direct Oxygen Sensor†

Biochemistry ◽

10.1021/bi991911s ◽

2000 ◽

Vol 39 (10) ◽

pp. 2685-2691 ◽

Cited By ~ 171

Author(s):

Vondolee Marie Delgado-Nixon ◽

Gonzalo Gonzalez ◽

Marie-Alda Gilles-Gonzalez

Keyword(s):

Oxygen Sensor ◽

Heme Binding ◽

Fromescherichia Coli

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Ligand Binding Dynamics to the Heme Domain of the Oxygen Sensor Dos fromEscherichia coli

Biochemistry ◽

10.1021/bi027359f ◽

2003 ◽

Vol 42 (21) ◽

pp. 6527-6535 ◽

Cited By ~ 37

Author(s):

Ursula Liebl ◽

Latifa Bouzhir-Sima ◽

Laurent Kiger ◽

Michael C. Marden ◽

Jean-Christophe Lambry ◽

...

Keyword(s):

Ligand Binding ◽

Oxygen Sensor ◽

Fromescherichia Coli ◽

Heme Domain

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Arg97 at the Heme-Distal Side of the Isolated Heme-Bound PAS Domain of a Heme-Based Oxygen Sensor fromEscherichia coli(EcDOS) Plays Critical Roles in Autoxidation and Binding to Gases, Particularly O2†

Biochemistry ◽

10.1021/bi800248c ◽

2008 ◽

Vol 47 (34) ◽

pp. 8874-8884 ◽

Cited By ~ 27

Author(s):

Yukako Ishitsuka ◽

Yasuyuki Araki ◽

Atsunari Tanaka ◽

Jotaro Igarashi ◽

Osamu Ito ◽

...

Keyword(s):

Oxygen Sensor ◽

Pas Domain ◽

Fromescherichia Coli ◽

Distal Side

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Characterization of a Direct Oxygen Sensor Heme Protein fromEscherichia coli

Journal of Biological Chemistry ◽

10.1074/jbc.m202738200 ◽

2002 ◽

Vol 277 (26) ◽

pp. 23821-23827 ◽

Cited By ~ 75

Author(s):

Yukie Sasakura ◽

Satoshi Hirata ◽

Shunpei Sugiyama ◽

Shingo Suzuki ◽

Sue Taguchi ◽

...

Keyword(s):

Oxygen Sensor ◽

Heme Protein ◽

Fromescherichia Coli

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Signal transduction by heme-containing PAS-domain proteins

Journal of Applied Physiology ◽

10.1152/japplphysiol.00941.2003 ◽

2004 ◽

Vol 96 (2) ◽

pp. 774-783 ◽

Cited By ~ 111

Author(s):

Marie-Alda Gilles-Gonzalez ◽

Gonzalo Gonzalez

Keyword(s):

Signal Transduction ◽

Carbon Monoxide ◽

Oxygen Sensor ◽

Broad Class ◽

Pas Domain ◽

Heme Binding ◽

Cellulose Production ◽

Helix Loop Helix ◽

Binding Domains ◽

The One

The most common physiological strategy for detecting the gases oxygen, carbon monoxide, and nitric oxide is signal transduction by heme-based sensors, a broad class of modular proteins in which a heme-binding domain governs the activity of a neighboring transmitter domain. Different structures are possible for the heme-binding domains in these sensors, but, so far, the Per-ARNT-Sim motif, or PAS domain, is the one most commonly encountered. Heme-binding PAS (heme-PAS) domains can accomplish ligand-dependent switching of a variety of partner domains, including histidine kinase, phosphodiesterase, and basic helix-loop-helix (bHLH) DNA-binding modules. Proteins with heme-PAS domains occur in all kingdoms of life and are quite diverse in their physiological roles. Examples include the neuronal bHLH-PAS carbon monoxide sensor NPAS2 that is implicated in the mammalian circadian clock, the acetobacterial oxygen sensor AxPDEA1 that directs cellulose production, and the rhizobial oxygen sensor FixL, which governs nitrogen fixation. What factors determine the range of detection of these sensors? How do they transduce their signal? This review examines the recent advances in answering these questions.

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