NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues
Heme proteins are a diverse group that includes several unrelated families. Their biological function is mainly associated with the reactivity of the heme group, which—among several other reactions—can bind to and react with nitric oxide (NO) and other nitrogen compounds for their production, scaven...
| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | English |
| Publicado em: |
MDPI AG
2023-01-01
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| Colecção: | Antioxidants |
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| Acesso em linha: | https://www.mdpi.com/2076-3921/12/2/321 |
| _version_ | 1827759004702474240 |
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| author | Cinzia Verde Daniela Giordano Stefano Bruno |
| author_facet | Cinzia Verde Daniela Giordano Stefano Bruno |
| author_sort | Cinzia Verde |
| collection | DOAJ |
| description | Heme proteins are a diverse group that includes several unrelated families. Their biological function is mainly associated with the reactivity of the heme group, which—among several other reactions—can bind to and react with nitric oxide (NO) and other nitrogen compounds for their production, scavenging, and transport. The S-nitrosylation of cysteine residues, which also results from the reaction with NO and other nitrogen compounds, is a post-translational modification regulating protein activity, with direct effects on a variety of signaling pathways. Heme proteins are unique in exhibiting this dual reactivity toward NO, with reported examples of cross-reactivity between the heme and cysteine residues within the same protein. In this work, we review the literature on this interplay, with particular emphasis on heme proteins in which heme-dependent nitrosylation has been reported and those for which both heme nitrosylation and S-nitrosylation have been associated with biological functions. |
| first_indexed | 2024-03-11T09:14:35Z |
| format | Article |
| id | doaj.art-fe44905ee792489da5a4947d4a90745c |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-11T09:14:35Z |
| publishDate | 2023-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-fe44905ee792489da5a4947d4a90745c2023-11-16T18:46:31ZengMDPI AGAntioxidants2076-39212023-01-0112232110.3390/antiox12020321NO and Heme Proteins: Cross-Talk between Heme and Cysteine ResiduesCinzia Verde0Daniela Giordano1Stefano Bruno2Institute of Biosciences and BioResources (IBBR), National Research Council (CNR), Via Pietro Castellino 111, 80131 Napoli, ItalyInstitute of Biosciences and BioResources (IBBR), National Research Council (CNR), Via Pietro Castellino 111, 80131 Napoli, ItalyDepartment of Food and Drug, University of Parma, 43124 Parma, ItalyHeme proteins are a diverse group that includes several unrelated families. Their biological function is mainly associated with the reactivity of the heme group, which—among several other reactions—can bind to and react with nitric oxide (NO) and other nitrogen compounds for their production, scavenging, and transport. The S-nitrosylation of cysteine residues, which also results from the reaction with NO and other nitrogen compounds, is a post-translational modification regulating protein activity, with direct effects on a variety of signaling pathways. Heme proteins are unique in exhibiting this dual reactivity toward NO, with reported examples of cross-reactivity between the heme and cysteine residues within the same protein. In this work, we review the literature on this interplay, with particular emphasis on heme proteins in which heme-dependent nitrosylation has been reported and those for which both heme nitrosylation and S-nitrosylation have been associated with biological functions.https://www.mdpi.com/2076-3921/12/2/321S-nitrosylationnitrosationnitric oxideheme proteinshemecysteine |
| spellingShingle | Cinzia Verde Daniela Giordano Stefano Bruno NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues Antioxidants S-nitrosylation nitrosation nitric oxide heme proteins heme cysteine |
| title | NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues |
| title_full | NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues |
| title_fullStr | NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues |
| title_full_unstemmed | NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues |
| title_short | NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues |
| title_sort | no and heme proteins cross talk between heme and cysteine residues |
| topic | S-nitrosylation nitrosation nitric oxide heme proteins heme cysteine |
| url | https://www.mdpi.com/2076-3921/12/2/321 |
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