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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ACADEMIC PRESS INC ELSEVIER SCIENCE
2009
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Online Access: | http://hdl.handle.net/11573/1409634 https://doi.org/10.1016/j.bbrc.2009.09.050 |
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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 |
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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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1789339254555410432 |