Hydroxylamine-induced oxidation of ferrous nitrobindins

G, De Simone; Tundo, Grazia R.; Coletta, Andrea; Coletta, Massimo; Ascenzi, Paolo

doi:10.1007/s00775-022-01940-9

Cited by 4 publications

(2 citation statements)

References 68 publications

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“…Dr -Nb(III) was cloned, expressed, and purified as already reported [ 52 ]. The Dr -Nb(III) concentration was determined spectrophotometrically by measuring the absorbance at 407 nm (ε = 1.57 × 10 5 M −1 cm −1 ) [ 52 ]. Apo- Dr -Nb was prepared, as already reported [ 53 ].…”

Section: Methodsmentioning

confidence: 99%

The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO2: The Case of Zebrafish Nitrobindin

Coletta

Masi

et al. 2022

Antioxidants

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Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric Danio rerio Nb (Dr-Nb(III)) in the absence and presence of CO2 is reported. The Dr-Nb(III)-catalyzed scavenging of peroxynitrite is facilitated by a low pH, indicating that the heme protein interacts preferentially with peroxynitrous acid, leading to the formation of nitrate (~91%) and nitrite (~9%). The physiological levels of CO2 dramatically facilitate the spontaneous decay of peroxynitrite, overwhelming the scavenging activity of Dr-Nb(III). The effect of Dr-Nb(III) on the peroxynitrite-induced nitration of L-tyrosine was also investigated. Dr-Nb(III) inhibits the peroxynitrite-mediated nitration of free L-tyrosine, while, in the presence of CO2, Dr-Nb(III) does not impair nitro-L-tyrosine formation. The comparative analysis of the present results with data reported in the literature indicates that, to act as efficient peroxynitrite scavengers in vivo, i.e., in the presence of physiological levels of CO2, the ferric heme protein concentration must be higher than 10−4 M. Thus, only the circulating ferric hemoglobin levels appear to be high enough to efficiently compete with CO2/HCO3− in peroxynitrite inactivation. The present results are of the utmost importance for tissues, like the eye retina in fish, where blood circulation is critical for adaptation to diving conditions.

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Section: Methodsmentioning

confidence: 99%

The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO2: The Case of Zebrafish Nitrobindin

Coletta

Masi

et al. 2022

Antioxidants

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“…The survival of M. tuberculosis in the host suggests ferric Nb as part of a detoxifcation system scavenging RNS and ROS produced by the immunity response, as reported for mammalian globins [ 169 , 170 ] and mycobacterial truncated hemoglobins [ 171 ]. If confirmed with future additional in vitro and in vivo experiments, Nb may emerge as a therapeutic target for the treatment of not only pulmonary tuberculosis but also extra-pulmonary manifestations, such as ocular infections involving conjunctiva, cornea, and sclera [ 172 ].…”

Section: Nitrobindinmentioning

confidence: 99%

Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins

2023

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Hemoproteins include several heme-binding proteins with distinct structure and function. The presence of the heme group confers specific reactivity and spectroscopic properties to hemoproteins. In this review, we provide an overview of five families of hemoproteins in terms of dynamics and reactivity. First, we describe how ligands modulate cooperativity and reactivity in globins, such as myoglobin and hemoglobin. Second, we move on to another family of hemoproteins devoted to electron transport, such as cytochromes. Later, we consider heme-based reactivity in hemopexin, the main heme-scavenging protein. Then, we focus on heme–albumin, a chronosteric hemoprotein with peculiar spectroscopic and enzymatic properties. Eventually, we analyze the reactivity and dynamics of the most recently discovered family of hemoproteins, i.e., nitrobindins.

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Nitrosylation of ferric zebrafish nitrobindin: A spectroscopic, kinetic, and thermodynamic study

Sebastiani

Smulevich

et al. 2022

Journal of Inorganic Biochemistry

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Hydroxylamine-induced oxidation of ferrous nitrobindins

Cited by 4 publications

References 68 publications

The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO2: The Case of Zebrafish Nitrobindin

The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO2: The Case of Zebrafish Nitrobindin

Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins

Nitrosylation of ferric zebrafish nitrobindin: A spectroscopic, kinetic, and thermodynamic study

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