Repair of Iron Center Proteins—A Different Class of Hemerythrin-like Proteins
Repair of Iron Center proteins (RIC) form a family of di-iron proteins that are widely spread in the microbial world. RICs contain a binuclear nonheme iron site in a four-helix bundle fold, two basic features of hemerythrin-like proteins. In this work, we review the data on microbial RICs including...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-06-01
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| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/27/13/4051 |
| _version_ | 1797442669018873856 |
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| author | Liliana S. O. Silva Pedro M. Matias Célia V. Romão Lígia M. Saraiva |
| author_facet | Liliana S. O. Silva Pedro M. Matias Célia V. Romão Lígia M. Saraiva |
| author_sort | Liliana S. O. Silva |
| collection | DOAJ |
| description | Repair of Iron Center proteins (RIC) form a family of di-iron proteins that are widely spread in the microbial world. RICs contain a binuclear nonheme iron site in a four-helix bundle fold, two basic features of hemerythrin-like proteins. In this work, we review the data on microbial RICs including how their genes are regulated and contribute to the survival of pathogenic bacteria. We gathered the currently available biochemical, spectroscopic and structural data on RICs with a particular focus on <i>Escherichia coli</i> RIC (also known as YtfE), which remains the best-studied protein with extensive biochemical characterization. Additionally, we present novel structural data for <i>Escherichia coli</i> YtfE harboring a di-manganese site and the protein’s affinity for this metal. The networking of protein interactions involving YtfE is also described and integrated into the proposed physiological role as an iron donor for reassembling of stress-damaged iron-sulfur centers. |
| first_indexed | 2024-03-09T12:45:18Z |
| format | Article |
| id | doaj.art-dc345c174e934d5fa2a9d0323f7a8dc4 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-09T12:45:18Z |
| publishDate | 2022-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-dc345c174e934d5fa2a9d0323f7a8dc42023-11-30T22:13:30ZengMDPI AGMolecules1420-30492022-06-012713405110.3390/molecules27134051Repair of Iron Center Proteins—A Different Class of Hemerythrin-like ProteinsLiliana S. O. Silva0Pedro M. Matias1Célia V. Romão2Lígia M. Saraiva3Instituto Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, 2780-157 Oeiras, PortugalInstituto Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, 2780-157 Oeiras, PortugalInstituto Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, 2780-157 Oeiras, PortugalInstituto Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, 2780-157 Oeiras, PortugalRepair of Iron Center proteins (RIC) form a family of di-iron proteins that are widely spread in the microbial world. RICs contain a binuclear nonheme iron site in a four-helix bundle fold, two basic features of hemerythrin-like proteins. In this work, we review the data on microbial RICs including how their genes are regulated and contribute to the survival of pathogenic bacteria. We gathered the currently available biochemical, spectroscopic and structural data on RICs with a particular focus on <i>Escherichia coli</i> RIC (also known as YtfE), which remains the best-studied protein with extensive biochemical characterization. Additionally, we present novel structural data for <i>Escherichia coli</i> YtfE harboring a di-manganese site and the protein’s affinity for this metal. The networking of protein interactions involving YtfE is also described and integrated into the proposed physiological role as an iron donor for reassembling of stress-damaged iron-sulfur centers.https://www.mdpi.com/1420-3049/27/13/4051Repair of Iron Center proteinshemerythrindi-iron proteiniron-sulfur biogenesisnitrosative stress |
| spellingShingle | Liliana S. O. Silva Pedro M. Matias Célia V. Romão Lígia M. Saraiva Repair of Iron Center Proteins—A Different Class of Hemerythrin-like Proteins Molecules Repair of Iron Center proteins hemerythrin di-iron protein iron-sulfur biogenesis nitrosative stress |
| title | Repair of Iron Center Proteins—A Different Class of Hemerythrin-like Proteins |
| title_full | Repair of Iron Center Proteins—A Different Class of Hemerythrin-like Proteins |
| title_fullStr | Repair of Iron Center Proteins—A Different Class of Hemerythrin-like Proteins |
| title_full_unstemmed | Repair of Iron Center Proteins—A Different Class of Hemerythrin-like Proteins |
| title_short | Repair of Iron Center Proteins—A Different Class of Hemerythrin-like Proteins |
| title_sort | repair of iron center proteins a different class of hemerythrin like proteins |
| topic | Repair of Iron Center proteins hemerythrin di-iron protein iron-sulfur biogenesis nitrosative stress |
| url | https://www.mdpi.com/1420-3049/27/13/4051 |
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