Regulatory Switching by Concerted Motions on the Microsecond Time Scale of the Oxygen Sensor Protein FixL

2021 ◽  
Author(s):  
Takeo Yamawaki ◽  
Misao Mizuno ◽  
Haruto Ishikawa ◽  
Kazuhiro Takemura ◽  
Akio Kitao ◽  
...  
Keyword(s):  
Time Scale ◽  
Oxygen Sensor ◽  
Sensor Protein

scholarly journals Site-specific Protein Dynamics in Communication Pathway from Sensor to Signaling Domain of Oxygen Sensor Protein, HemAT-Bs

2012 ◽  
Vol 287 (24) ◽  
pp. 19973-19984 ◽  
Author(s):  
Samir F. El-Mashtoly ◽  
Minoru Kubo ◽  
Yuzong Gu ◽  
Hitomi Sawai ◽  
Satoru Nakashima ◽  
...  
Keyword(s):  
Protein Dynamics ◽  
Oxygen Sensor ◽  
Specific Protein ◽  
Site Specific ◽  
Sensor Protein ◽  
Signaling Domain ◽  
Communication Pathway

scholarly journals Heme coordination structure of Dos, an oxygen sensor protein from Escherichia coli

2001 ◽  
Vol 41 (supplement) ◽  
pp. S116
Author(s):  
T. Uno ◽  
M. Oshima ◽  
Y. Tomisugi ◽  
Y. Ishokawa
Keyword(s):  
Escherichia Coli ◽  
Oxygen Sensor ◽  
Coordination Structure ◽  
Sensor Protein

Identification of the Hydrophobic Amino Acid Residues Required for Heme Assembly in the Rhizobial Oxygen Sensor Protein FixL

1998 ◽  
Vol 247 (2) ◽  
pp. 427-431 ◽  
Author(s):  
Hiro Nakamura ◽  
Ken Saito ◽  
Eiichi Ito ◽  
Koji Tamura ◽  
Terumasa Tsuchiya ◽  
...  
Keyword(s):  
Amino Acid ◽  
Oxygen Sensor ◽  
Amino Acid Residues ◽  
Hydrophobic Amino Acid ◽  
Sensor Protein

scholarly journals The Oxygen Sensor Protein, FixL, ofRhizobium meliloti

1995 ◽  
Vol 270 (10) ◽  
pp. 5243-5250 ◽  
Author(s):  
Ellen K. Monson ◽  
Gary S. Ditta ◽  
Donald R. Helinski
Keyword(s):  
Oxygen Sensor ◽  
Sensor Protein ◽  
Ofrhizobium Meliloti

scholarly journals Subpicosecond oxygen trapping in the heme pocket of the oxygen sensor FixL observed by time-resolved resonance Raman spectroscopy

2007 ◽  
Vol 104 (18) ◽  
pp. 7408-7413 ◽  
Author(s):  
Sergei G. Kruglik ◽  
Audrius Jasaitis ◽  
Klara Hola ◽  
Taku Yamashita ◽  
Ursula Liebl ◽  
...  
Keyword(s):  
Oxygen Sensor ◽  
Protein Complexes ◽  
Signal Transmission ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Plane Motion ◽  
Heme Iron ◽  
Time Resolved ◽  
Mutant Proteins ◽  
Sensor Protein

Dissociation of oxygen from the heme domain of the bacterial oxygen sensor protein FixL constitutes the first step in hypoxia-induced signaling. In the present study, the photodissociation of the heme-O2 bond was used to synchronize this event, and time-resolved resonance Raman (TR3) spectroscopy with subpicosecond time resolution was implemented to characterize the heme configuration of the primary photoproduct. TR3 measurements on heme-oxycomplexes are highly challenging and have not yet been reported. Whereas in all other known six-coordinated heme protein complexes with diatomic ligands, including the oxymyoglobin reported here, heme iron out-of-plane motion (doming) occurs faster than 1 ps after iron–ligand bond breaking; surprisingly, no sizeable doming is observed in the oxycomplex of the Bradyrhizobium japonicum FixL sensor domain (FixLH). This assessment is deduced from the absence of the iron–histidine band around 217 cm−1 as early as 0.5 ps. We suggest that efficient ultrafast oxygen rebinding to the heme occurs on the femtosecond time scale, thus hindering heme doming. Comparing WT oxy-FixLH, mutant proteins FixLH-R220H and FixLH-R220Q, the respective carbonmonoxy-complexes, and oxymyoglobin, we show that a hydrogen bond of the terminal oxygen atom with the residue in position 220 is responsible for the observed behavior; in WT FixL this residue is arginine, crucially implicated in signal transmission. We propose that the rigid O2 configuration imposed by this residue, in combination with the hydrophobic and constrained properties of the distal cavity, keep dissociated oxygen in place. These results uncover the origin of the “oxygen cage” properties of this oxygen sensor protein.

Immunohistochemical demonstration of four subunits of neutrophil NAD(P)H oxidase in type I cells of carotid body

1995 ◽  
Vol 78 (5) ◽  
pp. 1904-1909 ◽  
Author(s):  
W. Kummer ◽  
H. Acker
Keyword(s):  
Hydrogen Peroxide ◽  
Carotid Body ◽  
Oxygen Sensor ◽  
Neutrophil Granulocytes ◽  
Type I ◽  
Body Type ◽  
Type I Cells ◽  
Carotid Bodies ◽  
Sensor Protein ◽  
I Cells

We demonstrate, by means of immunohistochemistry, that type I cells of human, guinea pig, and rat carotid bodies react with antisera raised against the subunits p22phox, gp91phox, p47phox, and p67phox of the NAD(P)H oxidase isolated from human neutrophil granulocytes. The findings support previous photometric studies that indicate that carotid body type I cells possess a putative oxygen sensor protein that is similar to the neutrophil NAD(P)H oxidase and consists of a hydrogen peroxide generating low-potential cytochrome b558 with cofactors regulating the electron transfer to oxygen.

scholarly journals 1P-114 Dynamic role of specific heme-ligand-residue interactions in functional motions on the direct oxygen sensor protein, DOS(The 46th Annual Meeting of the Biophysical Society of Japan)

2008 ◽  
Vol 48 (supplement) ◽  
pp. S39
Author(s):  
Taku Yamashita ◽  
Latifa Bouzhir(Sima) ◽  
Jean-Christophe Lambry ◽  
Ursula Liebl ◽  
Marten H. Vos ◽  
...  
Keyword(s):  
Annual Meeting ◽  
Oxygen Sensor ◽  
Sensor Protein ◽  
Biophysical Society
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