Peroxynitrite detoxification by ferryl Mycobacterium leprae truncated hemoglobin O

Ascenzi, Paolo; Marinis, Elisabetta De; Visca, Paolo; Ciaccio, Chiara; Coletta, Massimo

doi:10.1016/j.bbrc.2009.01.088

Cited by 15 publications

(16 citation statements)

References 41 publications

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“…(3), k lim(top) and k lim(bottom) could represent the second-order rate constants for MbAFe(IV)@O-and HbAFe(IV)@O-mediated scavenging of peroxynitrous acid at pH ( pK a and of peroxynitrite at pH ) pK a , respectively. In agreement with: (i) kinetics of peroxynitrite scavenging by M. leprae trHbOAFe(IV)@O [29], and (ii) kinetic simulations concerning peroxynitrite scavenging by horse heart MbAFe(IV)@O [19], k lim(top) values for peroxynitrite scavenging by MbAFe(IV)@O and HbAFe(IV)@O exceed those of k lim(bottom) (i.e., k lim(top) /k lim(bottom) = 4.7 and 7.9, respectively). Accordingly, the reaction of HbAFe(IV)@O with ONOOH shows a lower activa- ) with respect to that with ONOO À .…”

Section: Resultssupporting

confidence: 82%

“…(3) allowed to determine values of pK a = 6.9 and 6.7, respectively. The pK a values for peroxynitrite scavenging by MbAFe(IV)@O (=6.9) and HbAFe(IV)@O (=6.7), in the absence of CO 2 , are similar to those reported for: (i) peroxynitrite detoxification by ferryl Mycobacterium leprae truncated HbO (=6.7; trHbOAFe(IV)@O) [29], and (ii) the peroxynitrous acid/peroxynitrite (i.e., ONOOH/ONOO) equilibrium (=6.5-6.8) [10,34]. This suggests that peroxynitrous acid is the species that reacts preferentially with heme-Fe(IV)@O.…”

Section: Resultssupporting

confidence: 78%

“…In the presence of CO 2 , values of k on for peroxynitrite scavenging by MbAFe(IV)@O and HbAFe(IV)@O are pH-independent (the average k on values are 7. Tables 2 and 3), as reported for M. leprae trHbO-Fe(IV)@O, Glycine max leghemoglobin-Fe(IV)@O (Lb-Fe(IV)@O), horse heart MbAFe(IV)@O, and human HbAFe(IV)@O [19,22,24,29]. This agrees with the reaction mechanism proposed for peroxynitrite scavenging by hemeFe(IV)@O in the presence of CO 2 involving the transient highly reactive species Å NO 2 .…”

Section: Kj Mol à1supporting

confidence: 86%

“…The time course of peroxynitrite scavenging by MbAFe(IV)@O and HbAFe(IV)@O, in the absence and presence of CO 2 , was fitted to a single exponential process according to the minimum reaction mechanism represented by Scheme 1 [29].…”

Section: Methodsmentioning

confidence: 99%

“…These reactions play an important physiological role in the defense against nitrosative and oxidative stress [7,[12][13][14][15][16]. Peroxynitrite scavenging has been reported to be facilitated by the ferrous oxygenated (heme-Fe(II)-O 2 ), ferrous nitrosylated (heme-Fe(II)-NO), and ferric (heme-Fe(III)) derivatives of heme-proteins [7,15,[17][18][19][20][21][22][23][24][25][26][27][28][29].…”

mentioning

confidence: 99%

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Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin

Ascenzi

Marinis

Masi

et al. 2009

Biochemical and Biophysical Research Communications

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Section: Resultssupporting

confidence: 82%

Section: Resultssupporting

confidence: 78%

Section: Kj Mol à1supporting

confidence: 86%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin

Ascenzi

Marinis

Masi

et al. 2009

Biochemical and Biophysical Research Communications

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Peroxynitrite—An ugly biofactor?

Ascenzi

Masi

Sciorati³

et al. 2010

BioFactors

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Cellular damage occurring under oxidative conditions has been ascribed mainly to the formation of peroxynitrite (ONOOH/ONOO(-)) that originates from the reaction of NO(*) with O(2) (*-). The detrimental effects of peroxynitrite are exacerbated by the reaction with CO(2) that leads to ONOOC(O)O(-), which further decays to the strong oxidant radicals NO(2) (*) and CO(3) (*-). The reaction with CO(2), however, may redirect peroxynitrite specificity. An excessive formation of peroxynitrite represents an important mechanism contributing to the DNA damage, the inactivation of metabolic enzymes, ionic pumps, and structural proteins, and the disruption of cell membranes. Because of its ability to oxidize biomolecules, peroxynitrite is implicated in an increasing list of diseases, including neurodegenerative and cardiovascular disorders, inflammation, pain, autoimmunity, cancer, and aging. However, peroxynitrite displays also protective activities: (i) at high concentrations, it shows anti-viral, anti-microbial, and anti-parasitic actions; and (ii) at low concentrations, it stimulates protective mechanisms in the cardiovascular, nervous, and respiratory systems. The detrimental effects of peroxynitrite and related reactive species are impaired by (pseudo-) enzymatic systems, mainly represented by heme-proteins (e.g., hemoglobin and myoglobin). Here, we report biochemical aspects of peroxynitrite actions being at the root of its biomedical effects.

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Structural determinants of ligand binding in truncated hemoglobins: Resonance Raman spectroscopy of the native states and their carbon monoxide and hydroxide complexes

et al. 2018

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The ligand binding characteristics of heme-containing proteins are determined by a number of factors, including the nature and conformation of the distal residues and their capability to stabilize the heme-bound ligand via hydrogen-bonding and electrostatic interactions. In this regard, the heme pockets of truncated hemoglobins (TrHbs) constitute an interesting case study as they share many common features, including a number of polar cavity residues. In this review, we will focus on three proteins of group II TrHbs, from Thermobifida fusca (Tf-HbO) and Pseudoalteromonas haloplanktis TAC125 (Ph-HbO). Although the residues in positions G8 (Trp) and B10 (Tyr) are conserved in all three proteins, the CD1 residue is a Tyr in T. fusca and a His in P. haloplanktis. Comparison of the ligand binding characteristics of these proteins, in particular the hydroxo and CO ligands by means of resonance Raman spectroscopy, reveals that this single difference in the key heme cavity residues markedly affects their ligand binding capability and conformation. Furthermore, although the two Ph-HbOs (Ph-HbO-2217 and Ph-HbO-0030) have identical key cavity residues, they display distinct ligand binding properties.

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Peroxynitrite detoxification by ferryl Mycobacterium leprae truncated hemoglobin O

Cited by 15 publications

References 41 publications

Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin

Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin

Peroxynitrite—An ugly biofactor?

Structural determinants of ligand binding in truncated hemoglobins: Resonance Raman spectroscopy of the native states and their carbon monoxide and hydroxide complexes

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