Investigation of the reaction between phosphoenolpyruvic acid and thiosulfate-nitrosyl iron complex

The process of transformation of a mononuclear cationic complex with N-ethylthiourea ligands in Tris-HCl buffer, as well as in a reaction mixture with reduced glutathione and bovine serum albumin, has been studied. It was found that in the presence of glutathione, the complex dimer-izes, while its initial ligands are replaced by glutathione. In the presence of albumin, the decay product of the complex is coordinated with amino acid residues (Cys34 and His39) to form a protein-bound complex.

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Iron complexes of tris(4-nitrophenyl)corrole, with emphasis on the (nitrosyl)iron complex

Journal of Porphyrins and Phthalocyanines ◽

10.1142/s1088424612500605 ◽

2012 ◽

Vol 16 (05n06) ◽

pp. 663-673 ◽

Cited By ~ 20

Author(s):

Pinky Singh ◽

Irena Saltsman ◽

Atif Mahammed ◽

Israel Goldberg ◽

Boris Tumanskii ◽

...

Keyword(s):

Iron Complexes ◽

Iron Complex ◽

Oxidation Products ◽

Spectroscopic Techniques ◽

X Ray ◽

Nitrosyl Iron Complex ◽

Reduction And Oxidation ◽

Electron Reduction ◽

The One ◽

Redox Centre

The iron complexes of 5,10,15-tris(4-nitrophenyl)corrole have been prepared and characterized by various spectroscopic techniques. The (nitrosyl)iron complex is diamagnetic and its X-ray structure reveals an almost perfectly linear Fe–N–O bond. EPR spectroscopy in conjunction with 15N labelling were used to deduce the redox centre of the one-electron reduction and oxidation products of the (nitrosyl)iron corrole.

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Revealing of the cation-binding sites on the surface of hemoglobin in its reaction with the NO donor, the nitrosyl iron complex {Fe2[S(CH2)2NH3]2(NO)4}SO4·2.5H2O

Russian Chemical Bulletin ◽

10.1007/s11172-012-0330-0 ◽

2012 ◽

Vol 61 (12) ◽

pp. 2350-2355 ◽

Cited By ~ 2

Author(s):

N. A. Sanina ◽

L. A. Syrtsova ◽

B. L. Psikha ◽

I. A. Tukhvatullin ◽

N. I. Shkondina ◽

...

Keyword(s):

Binding Sites ◽

Iron Complex ◽

Cation Binding ◽

No Donor ◽

Nitrosyl Iron Complex

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Mechanism of transcriptional regulation by the Escherichia coli nitric oxide sensor NorR

Biochemical Society Transactions ◽

10.1042/bst0340191 ◽

2006 ◽

Vol 34 (1) ◽

pp. 191-194 ◽

Cited By ~ 20

Author(s):

N.P. Tucker ◽

B. D'Autréaux ◽

S. Spiro ◽

R. Dixon

Keyword(s):

Nitric Oxide ◽

Escherichia Coli ◽

Iron Complex ◽

Water Soluble ◽

Site Directed Mutagenesis ◽

Mononuclear Iron ◽

Protein Ligands ◽

Nitric Oxide Sensor ◽

Enhancer Binding Protein ◽

Nitrosyl Iron Complex

Nitric oxide (NO) is a highly reactive water-soluble gas encountered by bacteria endogenously as an intermediate of denitrification and exogenously as one of the radical species deployed by macrophages against invading pathogens. Bacteria therefore require a mechanism to detoxify NO. Escherichia coli flavorubredoxin and its associated oxidoreductase, encoded by the norV and norW genes respectively, reduces NO to nitrous oxide under anaerobic conditions. Transcription of the norVW genes is activated in response to NO by the σ54-dependent regulator NorR, a member of the prokaryotic enhancer binding protein family. NorR binds co-operatively to three enhancer sites to regulate transcription of both norVW and the divergently transcribed norR gene. In the present paper, we show that disruption of any one of the three GT-(N7)-AC NorR binding sites in the norR–norVW intergenic region prevents both activation of norVW expression and autogenous repression of the norR promoter by NorR. We have recently demonstrated that the N-terminal GAF (cGMP-specific and -stimulated phosphodiesterases, Anabaena adenylate cyclases and Escherichia coli FhlA) domain of NorR contains a non-haem mononuclear iron centre and senses NO by formation of a mono-nitrosyl iron complex. Site-directed mutagenesis has identified candidate protein ligands to the ferrous iron centre in the GAF domain.

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