Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin

Globins protect from the oxidative and nitrosative cell damage. Here, kinetics of peroxynitrite scavenging by ferryl sperm whale myoglobin (Mb{single bond}Fe(IV){double bond, long}O) and human hemoglobin (Hb{single bond}Fe(IV){double bond, long}O), between pH 5.8 and 8.3 at 20.0 °C, are reported. In...

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Published in:Biochemical and Biophysical Research Communications
Main Authors: Ascenzi P., De Marinis E., di Masi A., Ciaccio C., Coletta M.
Other Authors: Ascenzi, P., De Marinis, E., di Masi, A., Ciaccio, C., Coletta, M.
Format: Article in Journal/Newspaper
Language:English
Published: ACADEMIC PRESS INC ELSEVIER SCIENCE 2009
Subjects:
2
Kon
Online Access:http://hdl.handle.net/11573/1409634
https://doi.org/10.1016/j.bbrc.2009.09.050
id ftunivromairis:oai:iris.uniroma1.it:11573/1409634
record_format openpolar
spelling ftunivromairis:oai:iris.uniroma1.it:11573/1409634 2024-01-28T10:09:23+01:00 Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin Ascenzi P. De Marinis E. di Masi A. Ciaccio C. Coletta M. Ascenzi, P. De Marinis, E. di Masi, A. Ciaccio, C. Coletta, M. 2009 http://hdl.handle.net/11573/1409634 https://doi.org/10.1016/j.bbrc.2009.09.050 eng eng ACADEMIC PRESS INC ELSEVIER SCIENCE place:525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA info:eu-repo/semantics/altIdentifier/pmid/19766099 info:eu-repo/semantics/altIdentifier/wos/WOS:000271295500006 volume:390 issue:1 firstpage:27 lastpage:31 numberofpages:5 journal:BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS http://hdl.handle.net/11573/1409634 doi:10.1016/j.bbrc.2009.09.050 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-70349975706 Effect of CO 2 Ferric hemoglobin formation Ferric myoglobin formation Ferryl hemoglobin reduction Ferryl myoglobin reduction Kinetic Peroxynitrite scavenging Animal Hemoglobin Human Iron Mice Myoglobin Oxidation-Reduction Peroxynitrous Acid Sperm Whale info:eu-repo/semantics/article 2009 ftunivromairis https://doi.org/10.1016/j.bbrc.2009.09.050 2024-01-03T18:12:27Z Globins protect from the oxidative and nitrosative cell damage. Here, kinetics of peroxynitrite scavenging by ferryl sperm whale myoglobin (Mb{single bond}Fe(IV){double bond, long}O) and human hemoglobin (Hb{single bond}Fe(IV){double bond, long}O), between pH 5.8 and 8.3 at 20.0 °C, are reported. In the absence of CO2, values of the second-order rate constant for peroxynitrite scavenging by Mb{single bond}Fe(IV){double bond, long}O and Hb{single bond}Fe(IV){double bond, long}O (i.e., for Mb{single bond}Fe(III) and Hb{single bond}Fe(III) formation; kon) are 4.6 × 104 M-1 s-1 and 3.3 × 104 M-1 s-1, respectively, at pH 7.1. Values of kon increase on decreasing pH with pKa values of 6.9 and 6.7, this suggests that the ONOOH species reacts preferentially with Mb{single bond}Fe(IV){double bond, long}O and Hb{single bond}Fe(IV){double bond, long}O. In the presence of CO2 (=1.2 × 10-3 M), values of kon for peroxynitrite scavenging by Mb{single bond}Fe(IV){double bond, long}O and Hb{single bond}Fe(IV){double bond, long}O are essentially pH-independent, the average kon values are 7.1 × 104 M-1 s-1 and 1.2 × 105 M-1 s-1, respectively. As a whole, Mb{single bond}Fe(IV){double bond, long}O and Hb{single bond}Fe(IV){double bond, long}O, obtained by treatment with H2O2, undertake within the same cycle H2O2 and peroxynitrite detoxification. © 2009 Elsevier Inc. All rights reserved. Article in Journal/Newspaper Sperm whale Sapienza Università di Roma: CINECA IRIS Kon ENVELOPE(161.092,161.092,55.397,55.397) Biochemical and Biophysical Research Communications 390 1 27 31
institution Open Polar
collection Sapienza Università di Roma: CINECA IRIS
op_collection_id ftunivromairis
language English
topic Effect of CO
2
Ferric hemoglobin formation
Ferric myoglobin formation
Ferryl hemoglobin reduction
Ferryl myoglobin reduction
Kinetic
Peroxynitrite scavenging
Animal
Hemoglobin
Human
Iron
Mice
Myoglobin
Oxidation-Reduction
Peroxynitrous Acid
Sperm Whale
spellingShingle Effect of CO
2
Ferric hemoglobin formation
Ferric myoglobin formation
Ferryl hemoglobin reduction
Ferryl myoglobin reduction
Kinetic
Peroxynitrite scavenging
Animal
Hemoglobin
Human
Iron
Mice
Myoglobin
Oxidation-Reduction
Peroxynitrous Acid
Sperm Whale
Ascenzi P.
De Marinis E.
di Masi A.
Ciaccio C.
Coletta M.
Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin
topic_facet Effect of CO
2
Ferric hemoglobin formation
Ferric myoglobin formation
Ferryl hemoglobin reduction
Ferryl myoglobin reduction
Kinetic
Peroxynitrite scavenging
Animal
Hemoglobin
Human
Iron
Mice
Myoglobin
Oxidation-Reduction
Peroxynitrous Acid
Sperm Whale
description Globins protect from the oxidative and nitrosative cell damage. Here, kinetics of peroxynitrite scavenging by ferryl sperm whale myoglobin (Mb{single bond}Fe(IV){double bond, long}O) and human hemoglobin (Hb{single bond}Fe(IV){double bond, long}O), between pH 5.8 and 8.3 at 20.0 °C, are reported. In the absence of CO2, values of the second-order rate constant for peroxynitrite scavenging by Mb{single bond}Fe(IV){double bond, long}O and Hb{single bond}Fe(IV){double bond, long}O (i.e., for Mb{single bond}Fe(III) and Hb{single bond}Fe(III) formation; kon) are 4.6 × 104 M-1 s-1 and 3.3 × 104 M-1 s-1, respectively, at pH 7.1. Values of kon increase on decreasing pH with pKa values of 6.9 and 6.7, this suggests that the ONOOH species reacts preferentially with Mb{single bond}Fe(IV){double bond, long}O and Hb{single bond}Fe(IV){double bond, long}O. In the presence of CO2 (=1.2 × 10-3 M), values of kon for peroxynitrite scavenging by Mb{single bond}Fe(IV){double bond, long}O and Hb{single bond}Fe(IV){double bond, long}O are essentially pH-independent, the average kon values are 7.1 × 104 M-1 s-1 and 1.2 × 105 M-1 s-1, respectively. As a whole, Mb{single bond}Fe(IV){double bond, long}O and Hb{single bond}Fe(IV){double bond, long}O, obtained by treatment with H2O2, undertake within the same cycle H2O2 and peroxynitrite detoxification. © 2009 Elsevier Inc. All rights reserved.
author2 Ascenzi, P.
De Marinis, E.
di Masi, A.
Ciaccio, C.
Coletta, M.
format Article in Journal/Newspaper
author Ascenzi P.
De Marinis E.
di Masi A.
Ciaccio C.
Coletta M.
author_facet Ascenzi P.
De Marinis E.
di Masi A.
Ciaccio C.
Coletta M.
author_sort Ascenzi P.
title Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin
title_short Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin
title_full Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin
title_fullStr Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin
title_full_unstemmed Peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin
title_sort peroxynitrite scavenging by ferryl sperm whale myoglobin and human hemoglobin
publisher ACADEMIC PRESS INC ELSEVIER SCIENCE
publishDate 2009
url http://hdl.handle.net/11573/1409634
https://doi.org/10.1016/j.bbrc.2009.09.050
long_lat ENVELOPE(161.092,161.092,55.397,55.397)
geographic Kon
geographic_facet Kon
genre Sperm whale
genre_facet Sperm whale
op_relation info:eu-repo/semantics/altIdentifier/pmid/19766099
info:eu-repo/semantics/altIdentifier/wos/WOS:000271295500006
volume:390
issue:1
firstpage:27
lastpage:31
numberofpages:5
journal:BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
http://hdl.handle.net/11573/1409634
doi:10.1016/j.bbrc.2009.09.050
info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-70349975706
op_doi https://doi.org/10.1016/j.bbrc.2009.09.050
container_title Biochemical and Biophysical Research Communications
container_volume 390
container_issue 1
container_start_page 27
op_container_end_page 31
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