scholarly journals pH Dependence of Cyanide Binding to the Ferric Heme Domain of the Direct Oxygen Sensor fromEscherichia coliand the Effect of Alkaline Denaturation†

Biochemistry ◽  
2008 ◽  
Vol 47 (39) ◽  
pp. 10458-10470 ◽  
Author(s):  
Anil K. Bidwai ◽  
Esther Y. Ok ◽  
James E. Erman
Keyword(s):  
Oxygen Sensor ◽  
Ph Dependence ◽  
Cyanide Binding ◽  
Alkaline Denaturation ◽  
Heme Domain ◽  
Ferric Heme

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

Cloning, purification, crystallization and preliminary X-ray analysis of DOS heme domain, a new heme oxygen sensor inEscherichia coli

2002 ◽  
Vol 58 (9) ◽  
pp. 1504-1506 ◽  
Author(s):  
HaJeung Park ◽  
Christine Suquet ◽  
Marina I. Savenkova ◽  
James D. Satterlee ◽  
ChulHee Kang
Keyword(s):  
Oxygen Sensor ◽  
Inescherichia Coli ◽  
X Ray ◽  
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

pH Dependence of Heme Iron Coordination, Hydrogen Peroxide Reactivity, and Cyanide Binding in CytochromecPeroxidase(H52K)†

Biochemistry ◽  
2004 ◽  
Vol 43 (17) ◽  
pp. 5065-5072 ◽  
Author(s):  
Miriam C. Foshay ◽  
Lidia B. Vitello ◽  
James E. Erman
Keyword(s):  
Hydrogen Peroxide ◽  
Ph Dependence ◽  
Heme Iron ◽  
Cyanide Binding ◽  
Iron Coordination

Cyanide binding to canine myeloperoxidase

1989 ◽  
Vol 67 (4-5) ◽  
pp. 187-191 ◽  
Author(s):  
Leah A. Marquez ◽  
H. Brian Dunford
Keyword(s):  
Rate Constant ◽  
Binding Sites ◽  
Ph Dependence ◽  
Order Rate Constant ◽  
Protonated Form ◽  
Isosbestic Point ◽  
Equilibrium Binding ◽  
Cyanide Binding ◽  
Kinetics Of ◽  
Base Group

Equilibria and kinetics of cyanide binding to canine myeloperoxidase were studied. Spectral results support the presence of two heme binding sites; an isosbestic point at 444 nm and a linear Scatchard plot suggest that the binding affinity of cyanide to the two subunits of the enzyme is the same. The dissociation constant is 0.53 μM. The pH dependence of the apparent second order rate constant indicates the presence of an acid–base group on the enzyme with a pKa of 3.8 ± 0.1. The protonated form of cyanide binds to the basic enzyme with a rate constant of (4.3 ± 0.3) × 106 M−1 s−1.Key words: myeloperoxidase, cyanide binding, equilibrium binding, ligand binding kinetics.

scholarly journals The binding of ethyl isocyanide to ferroperoxidase

1972 ◽  
Vol 128 (2) ◽  
pp. 377-382 ◽  
Author(s):  
Charles Phelps ◽  
Eraldo Antonini ◽  
Maurizio Brunori
Keyword(s):  
Process Model ◽  
Dissociation Constants ◽  
Ph Dependence ◽  
Affinity Constant ◽  
Dependent Manner ◽  
Ph Values ◽  
Cyanide Binding ◽  
Equilibrium And Kinetics ◽  
Kinetics Of ◽  
A New Species

The equilibrium and kinetics of ethyl isocyanide binding to ferroperoxidase were studied. At pH9.1 the results of both studies are consistent with a single-process model with an affinity constant of 95m−1 and combination and dissociation constants of 2.2×103m−1·s−1 and 23s−1 respectively. Ethyl isocyanide is not bound significantly at pH values lower than 6.0, and in this behaviour and the pH-dependence of the affinity constant, similarities exist between isocyanide and cyanide binding. The enthalpy of the process measured by equilibrium methods is −59kJ/mol (−14kcal/mol). At pH values below 9, the ethyl isocyanide adduct changes in a slow time-dependent manner, giving rise to a new species. These changes are reversible on increasing the pH. The results are discussed in relation to other known information about ligand binding to ferroperoxidase and to myoglobin.

Role of Distal Arginine in Early Sensing Intermediates in the Heme Domain of the Oxygen Sensor FixL†

Biochemistry ◽  
2006 ◽  
Vol 45 (19) ◽  
pp. 6018-6026 ◽  
Author(s):  
Audrius Jasaitis ◽  
Klara Hola ◽  
Latifa Bouzhir-Sima ◽  
Jean-Christophe Lambry ◽  
Veronique Balland ◽  
...  
Keyword(s):  
Oxygen Sensor ◽  
Heme Domain

scholarly journals Stationary and Time-resolved Resonance Raman Spectra of His77and Met95Mutants of the Isolated Heme Domain of a Direct Oxygen Sensor fromEscherichia coli

2002 ◽  
Vol 277 (36) ◽  
pp. 32650-32658 ◽  
Author(s):  
Akira Sato ◽  
Yukie Sasakura ◽  
Shunpei Sugiyama ◽  
Ikuko Sagami ◽  
Toru Shimizu ◽  
...  
Keyword(s):  
Raman Spectra ◽  
Oxygen Sensor ◽  
Resonance Raman ◽  
Time Resolved ◽  
Fromescherichia Coli ◽  
Heme Domain ◽  
Resonance Raman Spectra
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