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 ◽  
2008 ◽  
Vol 47 (34) ◽  
pp. 8874-8884 ◽  
Author(s):  
Yukako Ishitsuka ◽  
Yasuyuki Araki ◽  
Atsunari Tanaka ◽  
Jotaro Igarashi ◽  
Osamu Ito ◽  
...  
Keyword(s):  
Oxygen Sensor ◽  
Pas Domain ◽  
Fromescherichia Coli ◽  
Distal Side

Role of Phe113 at the distal side of the heme domain of an oxygen-sensor (Ec DOS) in the characterization of the heme environment

2009 ◽  
Vol 103 (7) ◽  
pp. 989-996 ◽  
Author(s):  
Shinya Ito ◽  
Yasuyuki Araki ◽  
Atsunari Tanaka ◽  
Jotaro Igarashi ◽  
Takehiko Wada ◽  
...  
Keyword(s):  
Oxygen Sensor ◽  
Distal Side ◽  
Heme Domain

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

Biochemistry ◽  
2003 ◽  
Vol 42 (21) ◽  
pp. 6527-6535 ◽  
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

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

Biochemistry ◽  
2000 ◽  
Vol 39 (10) ◽  
pp. 2685-2691 ◽  
Author(s):  
Vondolee Marie Delgado-Nixon ◽  
Gonzalo Gonzalez ◽  
Marie-Alda Gilles-Gonzalez
Keyword(s):  
Oxygen Sensor ◽  
Heme Binding ◽  
Fromescherichia Coli

scholarly journals Identification and Functional and Spectral Characterization of a Globin-coupled Histidine Kinase from Anaeromyxobacter sp. Fw109-5

2011 ◽  
Vol 286 (41) ◽  
pp. 35522-35534 ◽  
Author(s):  
Kenichi Kitanishi ◽  
Kazuo Kobayashi ◽  
Takeshi Uchida ◽  
Koichiro Ishimori ◽  
Jotaro Igarashi ◽  
...  
Keyword(s):  
Histidine Kinase ◽  
Oxygen Sensor ◽  
Response Regulator ◽  
Dissociation Rate ◽  
Amino Acid Sequences ◽  
Site Directed Mutagenesis ◽  
Significant Activity ◽  
Distal Side ◽  
Two Component Signal Transduction ◽  
First Time

Two-component signal transduction systems regulate numerous important physiological functions in bacteria. In this study we have identified, cloned, overexpressed, and characterized a dimeric full-length heme-bound (heme:protein, 1:1 stoichiometry) globin-coupled histidine kinase (AfGcHK) from Anaeromyxobacter sp. strain Fw109-5 for the first time. The Fe(III), Fe(II)-O2, and Fe(II)-CO complexes of the protein displayed autophosphorylation activity, whereas the Fe(II) complex had no significant activity. A H99A mutant lost heme binding ability, suggesting that this residue is the heme proximal ligand. Moreover, His-183 was proposed as the autophosphorylation site based on the finding that the H183A mutant protein was not phosphorylated. The phosphate group of autophosphorylated AfGcHK was transferred to Asp-52 and Asp-169 of a response regulator, as confirmed from site-directed mutagenesis experiments. Based on the amino acid sequences and crystal structures of other globin-coupled oxygen sensor enzymes, Tyr-45 was assumed to be the O2 binding site at the heme distal side. The O2 dissociation rate constant, 0.10 s−1, was substantially increased up to 8.0 s−1 upon Y45L mutation. The resonance Raman frequencies representing νFe-O2 (559 cm−1) and νO-O (1149 cm−1) of the Fe(II)-O2 complex of Y45F mutant AfGcHK were distinct from those of the wild-type protein (νFe-O2, 557 cm−1; νO-O, 1141 cm−1), supporting the proposal that Tyr-45 is located at the distal side and forms hydrogen bonds with the oxygen molecule bound to the Fe(II) complex. Thus, we have successfully identified and characterized a novel heme-based globin-coupled oxygen sensor histidine kinase, AfGcHK, in this study.

Leu65 in the heme distal side is critical for the stability of the Fe(II)–O2 complex of YddV, a globin-coupled oxygen sensor diguanylate cyclase

2012 ◽  
Vol 108 ◽  
pp. 163-170 ◽  
Author(s):  
Kyosuke Nakajima ◽  
Kenichi Kitanishi ◽  
Kazuo Kobayashi ◽  
Nagao Kobayashi ◽  
Jotaro Igarashi ◽  
...  
Keyword(s):  
Oxygen Sensor ◽  
Diguanylate Cyclase ◽  
Distal Side ◽  
The Stability

Important Roles of Tyr43 at the Putative Heme Distal Side in the Oxygen Recognition and Stability of the Fe(II)−O2Complex of YddV, a Globin-Coupled Heme-Based Oxygen Sensor Diguanylate Cyclase

Biochemistry ◽  
2010 ◽  
Vol 49 (49) ◽  
pp. 10381-10393 ◽  
Author(s):  
Kenichi Kitanishi ◽  
Kazuo Kobayashi ◽  
Yuriko Kawamura ◽  
Izumi Ishigami ◽  
Takashi Ogura ◽  
...  
Keyword(s):  
Oxygen Sensor ◽  
Diguanylate Cyclase ◽  
Distal Side

Conversion of a heme-based oxygen sensor to a heme oxygenase by hydrogen sulfide: effects of mutations in the heme distal side of a heme-based oxygen sensor phosphodiesterase (Ec DOS)

BioMetals ◽  
2013 ◽  
Vol 26 (5) ◽  
pp. 839-852 ◽  
Author(s):  
Yongming Du ◽  
Gefei Liu ◽  
Yinxia Yan ◽  
Dongyang Huang ◽  
Wenhong Luo ◽  
...  
Keyword(s):  
Hydrogen Sulfide ◽  
Heme Oxygenase ◽  
Oxygen Sensor ◽  
Distal Side

scholarly journals Characterization of a Direct Oxygen Sensor Heme Protein fromEscherichia coli

2002 ◽  
Vol 277 (26) ◽  
pp. 23821-23827 ◽  
Author(s):  
Yukie Sasakura ◽  
Satoshi Hirata ◽  
Shunpei Sugiyama ◽  
Shingo Suzuki ◽  
Sue Taguchi ◽  
...  
Keyword(s):  
Oxygen Sensor ◽  
Heme Protein ◽  
Fromescherichia Coli
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