Structural insights into dissimilatory sulfite reductases: Structure of desulforubidin from Desulfomicrobium norvegicum
Dissimilatory sulfite reductases (dSiRs) are crucial enzymes in bacterial sulfur-based energy metabolism, which is likely to have been present in some of the earliest life forms on Earth. Several classes of dSiRs have been proposed on the basis of different biochemical and spectroscopic properties....
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2011-04-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmicb.2011.00071/full |
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| author | Tania F. Oliveira Tania F. Oliveira Edward eFranklin José P. Afonso Amir R. Khan Neil J. Oldham Inês A. C. ePereira Margarida eArcher |
| author_facet | Tania F. Oliveira Tania F. Oliveira Edward eFranklin José P. Afonso Amir R. Khan Neil J. Oldham Inês A. C. ePereira Margarida eArcher |
| author_sort | Tania F. Oliveira |
| collection | DOAJ |
| description | Dissimilatory sulfite reductases (dSiRs) are crucial enzymes in bacterial sulfur-based energy metabolism, which is likely to have been present in some of the earliest life forms on Earth. Several classes of dSiRs have been proposed on the basis of different biochemical and spectroscopic properties. Here, we describe the first structure of a dSiR from the desulforubidin (Drub) class isolated from Desulfomicrobium (Dm.) norvegicum. The desulforubidin structure is assembled as a2b2c2, in which two DsrC proteins are bound to the core [DsrA]2[DsrB]2 unit, as reported for the desulfoviridin (Dvir) structure from Desulfovibrio (D.) vulgaris. Unlike desulfoviridin, four sirohemes and eight [4Fe-4S] clusters are present in desulforubidin, but only two of the coupled siroheme-[4Fe-4S] cofactors are likely to be catalytically active. Mass spectrometry studies of purified desulforubidin and desulfoviridin show that both proteins may present different oligomeric complex forms that bind two, one or no DsrC proteins, providing an explanation for conflicting spectroscopic and biochemical results in the literature. |
| first_indexed | 2024-04-14T01:31:41Z |
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| id | doaj.art-39d029637f66485bac9d9585e94fe54e |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-04-14T01:31:41Z |
| publishDate | 2011-04-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-39d029637f66485bac9d9585e94fe54e2022-12-22T02:20:09ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2011-04-01210.3389/fmicb.2011.000719945Structural insights into dissimilatory sulfite reductases: Structure of desulforubidin from Desulfomicrobium norvegicumTania F. Oliveira0Tania F. Oliveira1Edward eFranklin2José P. Afonso3Amir R. Khan4Neil J. Oldham5Inês A. C. ePereira6Margarida eArcher7Instituto de Tecnologia Química e Biológica - UNLTrinity College Dublin (TCD)Trinity College Dublin (TCD)University of NottinghamTrinity College Dublin (TCD)University of NottinghamInstituto de Tecnologia Química e Biológica - UNLInstituto de Tecnologia Química e Biológica - UNLDissimilatory sulfite reductases (dSiRs) are crucial enzymes in bacterial sulfur-based energy metabolism, which is likely to have been present in some of the earliest life forms on Earth. Several classes of dSiRs have been proposed on the basis of different biochemical and spectroscopic properties. Here, we describe the first structure of a dSiR from the desulforubidin (Drub) class isolated from Desulfomicrobium (Dm.) norvegicum. The desulforubidin structure is assembled as a2b2c2, in which two DsrC proteins are bound to the core [DsrA]2[DsrB]2 unit, as reported for the desulfoviridin (Dvir) structure from Desulfovibrio (D.) vulgaris. Unlike desulfoviridin, four sirohemes and eight [4Fe-4S] clusters are present in desulforubidin, but only two of the coupled siroheme-[4Fe-4S] cofactors are likely to be catalytically active. Mass spectrometry studies of purified desulforubidin and desulfoviridin show that both proteins may present different oligomeric complex forms that bind two, one or no DsrC proteins, providing an explanation for conflicting spectroscopic and biochemical results in the literature.http://journal.frontiersin.org/Journal/10.3389/fmicb.2011.00071/fullSulfur metabolismiron-sulfur clusterssirohemeSulfate reducing bacteriasulfite reductasesX-ray structure |
| spellingShingle | Tania F. Oliveira Tania F. Oliveira Edward eFranklin José P. Afonso Amir R. Khan Neil J. Oldham Inês A. C. ePereira Margarida eArcher Structural insights into dissimilatory sulfite reductases: Structure of desulforubidin from Desulfomicrobium norvegicum Frontiers in Microbiology Sulfur metabolism iron-sulfur clusters siroheme Sulfate reducing bacteria sulfite reductases X-ray structure |
| title | Structural insights into dissimilatory sulfite reductases: Structure of desulforubidin from Desulfomicrobium norvegicum |
| title_full | Structural insights into dissimilatory sulfite reductases: Structure of desulforubidin from Desulfomicrobium norvegicum |
| title_fullStr | Structural insights into dissimilatory sulfite reductases: Structure of desulforubidin from Desulfomicrobium norvegicum |
| title_full_unstemmed | Structural insights into dissimilatory sulfite reductases: Structure of desulforubidin from Desulfomicrobium norvegicum |
| title_short | Structural insights into dissimilatory sulfite reductases: Structure of desulforubidin from Desulfomicrobium norvegicum |
| title_sort | structural insights into dissimilatory sulfite reductases structure of desulforubidin from desulfomicrobium norvegicum |
| topic | Sulfur metabolism iron-sulfur clusters siroheme Sulfate reducing bacteria sulfite reductases X-ray structure |
| url | http://journal.frontiersin.org/Journal/10.3389/fmicb.2011.00071/full |
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