{"title":"修正“蛋白质和二氧化碳对抗过氧亚硝酸盐”","authors":"","doi":"10.1002/biof.70040","DOIUrl":null,"url":null,"abstract":"<p>G. De Simone, A. di Masi, G. R. Tundo, et al., “Proteins and Carbon Dioxide Struggle Against Peroxynitrite,” <i>BioFactors</i> 51, no. 4 (2025): e70030, 10.1002/biof.70030.</p><p>In the originally published article, the title of Table 2 is incorrect. The correct title is shown below.</p><p>Incorrect</p><p>Values of <span></span><math>\n <semantics>\n <mrow>\n <msubsup>\n <mi>k</mi>\n <mn>0</mn>\n <mi>obs</mi>\n </msubsup>\n </mrow>\n <annotation>$$ {k}_0^{obs} $$</annotation>\n </semantics></math> for various actors of peroxynitrite decomposition, predicted on the basis of their physiological concentration reported in Table 1.</p><p>Correct</p><p>Values of <span></span><math>\n <semantics>\n <mrow>\n <msubsup>\n <mi>k</mi>\n <mn>0</mn>\n <mi>obs</mi>\n </msubsup>\n </mrow>\n <annotation>$$ {k}_0^{obs} $$</annotation>\n </semantics></math> for various actors of peroxynitrite decomposition were predicted on the basis of data reported in Table 1.</p><p>Incorrect</p><p>4.1 The Thiol-Protein-Dependent Inactivation of Peroxyinitrite.</p><p>Correct</p><p>4.1 The Thiol-Protein-Dependent Inactivation of Peroxynitrite.</p><p>On the second line of Table 2, CO<sub>2</sub> (extracellular)<sup>b</sup> is incorrectly spelled as CO<sub>2</sub> (extracellare).<sup>b</sup></p><p>In Section 5, the following text is incorrect. The correct text is shown below.</p><p>Incorrect</p><p>As a matter of fact, since the average Hb concentration in the blood is 8.0 × 10<sup>−3</sup> M (resulting from the intraerythrocytic concentration 2.0 × 10<sup>−2</sup> M times the hematocrit of 40%) and the value of (= 8.8 × 10<sup>4</sup> M<sup>−1</sup> s<sup>−1</sup>; Table 1), the expected maximal rate for peroxynitrite isomerization = 700 s<sup>−1</sup>; therefore, HbO<sub>2</sub> indeed is potentially more efficient than carbon dioxide in the reaction from peroxynitrite, this being especially relevant as a boost during the rising of peroxynitrite after the deactivation of PRDXs. However, the reaction of HbO<sub>2</sub> brings about the oxidation of a portion of it (never exceeding 10% of whole HbO<sub>2</sub>), even though Hb(III) participates to peroxynitrite scavenging as well; therefore, after the initial powerful boost from HbO<sub>2</sub> a steady-state role of peroxynitrite isomerization, corresponding to the average 10% of Hb(III) (i.e., ≈ 8.0 × 10<sup>−4</sup> M) [75], suggests a constant rate ≈ 30 s<sup>−1</sup> (corresponding to = 3.9 × 10<sup>4</sup> M<sup>−1</sup> s<sup>−1</sup> for Hb(III); Table 1).</p><p>Correct</p><p>As a matter of fact, since the average Hb concentration in the blood is 8.0 × 10<sup>−3</sup> M and the value of <span></span><math>\n <semantics>\n <mrow>\n <msubsup>\n <mi>k</mi>\n <mi>onL</mi>\n <mi>obs</mi>\n </msubsup>\n </mrow>\n <annotation>$$ {k}_{onL}^{obs} $$</annotation>\n </semantics></math> is 8.8 × 10<sup>4</sup> M<sup>−1</sup> s<sup>−1</sup> (Table 1), the expected maximal rate for peroxynitrite isomerization (<span></span><math>\n <semantics>\n <mrow>\n <msubsup>\n <mi>k</mi>\n <mn>0</mn>\n <mi>obs</mi>\n </msubsup>\n </mrow>\n <annotation>$$ {k}_0^{obs} $$</annotation>\n </semantics></math>) is 700 s<sup>−1</sup> (Table 2). Therefore, HbO<sub>2</sub> is potentially more efficient than CO<sub>2</sub> in peroxynitrite scavenging. This is especially relevant during the rising of peroxynitrite after PRDX deactivation. The reaction of HbO<sub>2</sub> with peroxynitrite brings about the oxidation of the heme-Fe atom never exceeding 10% of the whole oxygenated tetrameric protein (i.e., ≈ 8.0 × 10<sup>−4</sup> M) [75]. The rate constants of Hb(III)-dependent peroxynitrite scavenging are 3.9 × 10<sup>4</sup> M<sup>1</sup> s<sup>−1</sup> and 30 s<sup>−1</sup> (see Tables 1 and 2, respectively).</p><p>We apologize for these errors.</p>","PeriodicalId":8923,"journal":{"name":"BioFactors","volume":"51 4","pages":""},"PeriodicalIF":5.0000,"publicationDate":"2025-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://iubmb.onlinelibrary.wiley.com/doi/epdf/10.1002/biof.70040","citationCount":"0","resultStr":"{\"title\":\"Correction to “Proteins and Carbon Dioxide Struggle Against Peroxynitrite”\",\"authors\":\"\",\"doi\":\"10.1002/biof.70040\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>G. De Simone, A. di Masi, G. R. Tundo, et al., “Proteins and Carbon Dioxide Struggle Against Peroxynitrite,” <i>BioFactors</i> 51, no. 4 (2025): e70030, 10.1002/biof.70030.</p><p>In the originally published article, the title of Table 2 is incorrect. The correct title is shown below.</p><p>Incorrect</p><p>Values of <span></span><math>\\n <semantics>\\n <mrow>\\n <msubsup>\\n <mi>k</mi>\\n <mn>0</mn>\\n <mi>obs</mi>\\n </msubsup>\\n </mrow>\\n <annotation>$$ {k}_0^{obs} $$</annotation>\\n </semantics></math> for various actors of peroxynitrite decomposition, predicted on the basis of their physiological concentration reported in Table 1.</p><p>Correct</p><p>Values of <span></span><math>\\n <semantics>\\n <mrow>\\n <msubsup>\\n <mi>k</mi>\\n <mn>0</mn>\\n <mi>obs</mi>\\n </msubsup>\\n </mrow>\\n <annotation>$$ {k}_0^{obs} $$</annotation>\\n </semantics></math> for various actors of peroxynitrite decomposition were predicted on the basis of data reported in Table 1.</p><p>Incorrect</p><p>4.1 The Thiol-Protein-Dependent Inactivation of Peroxyinitrite.</p><p>Correct</p><p>4.1 The Thiol-Protein-Dependent Inactivation of Peroxynitrite.</p><p>On the second line of Table 2, CO<sub>2</sub> (extracellular)<sup>b</sup> is incorrectly spelled as CO<sub>2</sub> (extracellare).<sup>b</sup></p><p>In Section 5, the following text is incorrect. The correct text is shown below.</p><p>Incorrect</p><p>As a matter of fact, since the average Hb concentration in the blood is 8.0 × 10<sup>−3</sup> M (resulting from the intraerythrocytic concentration 2.0 × 10<sup>−2</sup> M times the hematocrit of 40%) and the value of (= 8.8 × 10<sup>4</sup> M<sup>−1</sup> s<sup>−1</sup>; Table 1), the expected maximal rate for peroxynitrite isomerization = 700 s<sup>−1</sup>; therefore, HbO<sub>2</sub> indeed is potentially more efficient than carbon dioxide in the reaction from peroxynitrite, this being especially relevant as a boost during the rising of peroxynitrite after the deactivation of PRDXs. However, the reaction of HbO<sub>2</sub> brings about the oxidation of a portion of it (never exceeding 10% of whole HbO<sub>2</sub>), even though Hb(III) participates to peroxynitrite scavenging as well; therefore, after the initial powerful boost from HbO<sub>2</sub> a steady-state role of peroxynitrite isomerization, corresponding to the average 10% of Hb(III) (i.e., ≈ 8.0 × 10<sup>−4</sup> M) [75], suggests a constant rate ≈ 30 s<sup>−1</sup> (corresponding to = 3.9 × 10<sup>4</sup> M<sup>−1</sup> s<sup>−1</sup> for Hb(III); Table 1).</p><p>Correct</p><p>As a matter of fact, since the average Hb concentration in the blood is 8.0 × 10<sup>−3</sup> M and the value of <span></span><math>\\n <semantics>\\n <mrow>\\n <msubsup>\\n <mi>k</mi>\\n <mi>onL</mi>\\n <mi>obs</mi>\\n </msubsup>\\n </mrow>\\n <annotation>$$ {k}_{onL}^{obs} $$</annotation>\\n </semantics></math> is 8.8 × 10<sup>4</sup> M<sup>−1</sup> s<sup>−1</sup> (Table 1), the expected maximal rate for peroxynitrite isomerization (<span></span><math>\\n <semantics>\\n <mrow>\\n <msubsup>\\n <mi>k</mi>\\n <mn>0</mn>\\n <mi>obs</mi>\\n </msubsup>\\n </mrow>\\n <annotation>$$ {k}_0^{obs} $$</annotation>\\n </semantics></math>) is 700 s<sup>−1</sup> (Table 2). Therefore, HbO<sub>2</sub> is potentially more efficient than CO<sub>2</sub> in peroxynitrite scavenging. This is especially relevant during the rising of peroxynitrite after PRDX deactivation. The reaction of HbO<sub>2</sub> with peroxynitrite brings about the oxidation of the heme-Fe atom never exceeding 10% of the whole oxygenated tetrameric protein (i.e., ≈ 8.0 × 10<sup>−4</sup> M) [75]. The rate constants of Hb(III)-dependent peroxynitrite scavenging are 3.9 × 10<sup>4</sup> M<sup>1</sup> s<sup>−1</sup> and 30 s<sup>−1</sup> (see Tables 1 and 2, respectively).</p><p>We apologize for these errors.</p>\",\"PeriodicalId\":8923,\"journal\":{\"name\":\"BioFactors\",\"volume\":\"51 4\",\"pages\":\"\"},\"PeriodicalIF\":5.0000,\"publicationDate\":\"2025-08-14\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://iubmb.onlinelibrary.wiley.com/doi/epdf/10.1002/biof.70040\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"BioFactors\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://iubmb.onlinelibrary.wiley.com/doi/10.1002/biof.70040\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"BioFactors","FirstCategoryId":"99","ListUrlMain":"https://iubmb.onlinelibrary.wiley.com/doi/10.1002/biof.70040","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
摘要
G. De Simone, A. di Masi, G. R. Tundo等,“蛋白质和二氧化碳对抗过氧亚硝酸盐”,《生物因子》第51期。4 (2025): e70030, 10.1002/ bioof .70030。在最初发表的文章中,表2的标题不正确。正确的标题如下所示。根据表1中报告的生理浓度预测的各种过氧亚硝酸盐分解因子的k0 obs $$ {k}_0^{obs} $$值的不正确。根据表1中报告的数据,预测了各种过氧亚硝酸盐分解因子的k0 obs $$ {k}_0^{obs} $$值。在表2的第二行,CO2(胞外)b被错误地拼写为CO2(胞外)。在第5节中,以下文本不正确。正确的文本如下所示。事实上,由于血液中Hb的平均浓度为8.0 × 10−3 M(由红细胞内浓度2.0 × 10−2 M乘以40的红细胞压积)%) and the value of (= 8.8 × 104 M−1 s−1; Table 1), the expected maximal rate for peroxynitrite isomerization = 700 s−1; therefore, HbO2 indeed is potentially more efficient than carbon dioxide in the reaction from peroxynitrite, this being especially relevant as a boost during the rising of peroxynitrite after the deactivation of PRDXs. However, the reaction of HbO2 brings about the oxidation of a portion of it (never exceeding 10% of whole HbO2), even though Hb(III) participates to peroxynitrite scavenging as well; therefore, after the initial powerful boost from HbO2 a steady-state role of peroxynitrite isomerization, corresponding to the average 10% of Hb(III) (i.e., ≈ 8.0 × 10−4 M) [75], suggests a constant rate ≈ 30 s−1 (corresponding to = 3.9 × 104 M−1 s−1 for Hb(III); Table 1).CorrectAs a matter of fact, since the average Hb concentration in the blood is 8.0 × 10−3 M and the value of k onL obs $$ {k}_{onL}^{obs} $$ is 8.8 × 104 M−1 s−1 (Table 1), the expected maximal rate for peroxynitrite isomerization ( k 0 obs $$ {k}_0^{obs} $$ ) is 700 s−1 (Table 2). Therefore, HbO2 is potentially more efficient than CO2 in peroxynitrite scavenging. This is especially relevant during the rising of peroxynitrite after PRDX deactivation. The reaction of HbO2 with peroxynitrite brings about the oxidation of the heme-Fe atom never exceeding 10% of the whole oxygenated tetrameric protein (i.e., ≈ 8.0 × 10−4 M) [75]. The rate constants of Hb(III)-dependent peroxynitrite scavenging are 3.9 × 104 M1 s−1 and 30 s−1 (see Tables 1 and 2, respectively).We apologize for these errors.
Correction to “Proteins and Carbon Dioxide Struggle Against Peroxynitrite”
G. De Simone, A. di Masi, G. R. Tundo, et al., “Proteins and Carbon Dioxide Struggle Against Peroxynitrite,” BioFactors 51, no. 4 (2025): e70030, 10.1002/biof.70030.
In the originally published article, the title of Table 2 is incorrect. The correct title is shown below.
Incorrect
Values of for various actors of peroxynitrite decomposition, predicted on the basis of their physiological concentration reported in Table 1.
Correct
Values of for various actors of peroxynitrite decomposition were predicted on the basis of data reported in Table 1.
Incorrect
4.1 The Thiol-Protein-Dependent Inactivation of Peroxyinitrite.
Correct
4.1 The Thiol-Protein-Dependent Inactivation of Peroxynitrite.
On the second line of Table 2, CO2 (extracellular)b is incorrectly spelled as CO2 (extracellare).b
In Section 5, the following text is incorrect. The correct text is shown below.
Incorrect
As a matter of fact, since the average Hb concentration in the blood is 8.0 × 10−3 M (resulting from the intraerythrocytic concentration 2.0 × 10−2 M times the hematocrit of 40%) and the value of (= 8.8 × 104 M−1 s−1; Table 1), the expected maximal rate for peroxynitrite isomerization = 700 s−1; therefore, HbO2 indeed is potentially more efficient than carbon dioxide in the reaction from peroxynitrite, this being especially relevant as a boost during the rising of peroxynitrite after the deactivation of PRDXs. However, the reaction of HbO2 brings about the oxidation of a portion of it (never exceeding 10% of whole HbO2), even though Hb(III) participates to peroxynitrite scavenging as well; therefore, after the initial powerful boost from HbO2 a steady-state role of peroxynitrite isomerization, corresponding to the average 10% of Hb(III) (i.e., ≈ 8.0 × 10−4 M) [75], suggests a constant rate ≈ 30 s−1 (corresponding to = 3.9 × 104 M−1 s−1 for Hb(III); Table 1).
Correct
As a matter of fact, since the average Hb concentration in the blood is 8.0 × 10−3 M and the value of is 8.8 × 104 M−1 s−1 (Table 1), the expected maximal rate for peroxynitrite isomerization () is 700 s−1 (Table 2). Therefore, HbO2 is potentially more efficient than CO2 in peroxynitrite scavenging. This is especially relevant during the rising of peroxynitrite after PRDX deactivation. The reaction of HbO2 with peroxynitrite brings about the oxidation of the heme-Fe atom never exceeding 10% of the whole oxygenated tetrameric protein (i.e., ≈ 8.0 × 10−4 M) [75]. The rate constants of Hb(III)-dependent peroxynitrite scavenging are 3.9 × 104 M1 s−1 and 30 s−1 (see Tables 1 and 2, respectively).
期刊介绍:
BioFactors, a journal of the International Union of Biochemistry and Molecular Biology, is devoted to the rapid publication of highly significant original research articles and reviews in experimental biology in health and disease.
The word “biofactors” refers to the many compounds that regulate biological functions. Biological factors comprise many molecules produced or modified by living organisms, and present in many essential systems like the blood, the nervous or immunological systems. A non-exhaustive list of biological factors includes neurotransmitters, cytokines, chemokines, hormones, coagulation factors, transcription factors, signaling molecules, receptor ligands and many more. In the group of biofactors we can accommodate several classical molecules not synthetized in the body such as vitamins, micronutrients or essential trace elements.
In keeping with this unified view of biochemistry, BioFactors publishes research dealing with the identification of new substances and the elucidation of their functions at the biophysical, biochemical, cellular and human level as well as studies revealing novel functions of already known biofactors. The journal encourages the submission of studies that use biochemistry, biophysics, cell and molecular biology and/or cell signaling approaches.