Hemes and Hemoproteins. 5: Kinetics of the Peroxidatic Activity of Microperoxidase-8: Model for the Peroxidase Enzymes
References (40)
- et al.
- et al.
J. Biol. Chem.
(1980) - et al.
J. Inorg. Biochem.
(1986) - et al.
J. Inorg. Biochem.
(1986) - et al.
J. Inorg. Biochem.
(1987) - et al.
Biochim. Biophys. Acta
(1972) - et al.
J. Biol. Chem.
(1972) - et al.
J. Theor. Biol.
(1977) - et al.
J. Biol. Chem
(1980) - et al.
FEBS Lett.
(1985)
Anal. Biochem.
Inorg. Chim. Acta
Biochim. Biophys. Acta
J. Biol. Chem.
Biochem. Biophys. Res. Commun.
FEBS Lett.
Adv. Inorg. Bioinorg. Mech.
Ann. Rev. Biochem.
Cited by (111)
Peroxidase activity enhancement of myoglobin by two cooperative distal histidines and a channel to the heme pocket
2016, Journal of Molecular Catalysis B: EnzymaticCitation Excerpt :The reaction using ABTS as a substrate was followed by monitoring the formation the ABTS+· cation radical at 660 nm. The initial rate was calculated based on the initial linear changes using an extinction coefficient of ε470 nm = 26.6 mM−1 × cm−1 [29], and ε660nm = 14.0 mM−1 × cm−1 [30], respectively. The curve of initial rates versus substrate concentrations was fitted to the Michaelis-Menten equation: ν/[protein] = kcat[substrate]/(Km + [substrate]).
An intramolecular disulfide bond designed in myoglobin fine-tunes both protein structure and peroxidase activity
2016, Archives of Biochemistry and BiophysicsCitation Excerpt :The reaction was followed by monitoring the change in absorbance of the product at 470 nm, as proposed to be a dimeric form of guaiacol (3, 3′-dimethoxy-4, 4′-biphenylquinone) [38]. The initial rate was calculated based on the initial linear changes using an extinction coefficient of ε470 = 26.6 mM−1 cm−1 [39]. To determine the steady-state kinetic parameters, one syringe contains 2 μM protein mixed with various concentrations (0.1–6 mM) of guaiacol, and the second syringe contains 200 mM H2O2.
Conjugation of cytochrome c with ferrocene-terminated hyperbranched polymer and its influence on protein structure, conformation and function
2016, Spectrochimica Acta - Part A: Molecular and Biomolecular SpectroscopyCitation Excerpt :The peroxidase activity of cyt c (1 μM) in the absence or presence of 1 to 18 equivalents of HPU-Fc was estimated in Tris HCl buffer(2 mL, 50 mM, pH 7.0) at 25 °C, with guaiacol (10 mM) as a substrate. The reaction was initiated by the addition of hydrogen peroxide (H2O2) with a concentration of 4.8 mM to the starting mixtures and followed by monitoring the change in absorbance (for 5 min with 6 s intervals) of the product, as proposed to be a dimeric form of guaiacol (3, 3′-dimethoxy-4, 4′-biphenylquinone) [38], at 470 nm using an extinction coefficient of Ɛ470 = 26.6 Mm− 1 cm− 1 [39] on UV–Vis spectrometer. The relative ideal architectures of the third generation of HPU-Fc with 29 ferrocene terminals are depicted in Scheme 1.
A spectroscopic study of uranyl-cytochrome b<inf>5</inf>/cytochrome c interactions
2014, Spectrochimica Acta - Part A: Molecular and Biomolecular SpectroscopyPeroxidase activity of a myoglobin mutant with three distal histidines forming a metal-binding site: Implications for the cross-reactivity of cytochrome c oxidase
2013, Journal of Molecular Catalysis B: Enzymatic
- 2
Address reprint requests to Dr. D.A. Baldwin, National Chemical Research Laboratory, CSIR, P.O. Box 395, Pretoria, 0001, South Africa.
- 1
Present address: Department of Chemistry, University of Surrey, Guildford, England, GU2 5XH.