Publicação
Redox properties of cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774
| dc.contributor.author | Costa, Cristina | |
| dc.contributor.author | Moura, José J. G. | |
| dc.contributor.author | Moura, Isabel | |
| dc.contributor.author | Wang, Yaning | |
| dc.contributor.author | Huynh, Boi Hanh | |
| dc.contributor.institution | DQ - Departamento de Química | |
| dc.contributor.institution | CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE) | |
| dc.contributor.pbl | ASBMB - American Society for Biochemistry and Molecular Biology | |
| dc.date.accessioned | 2019-09-09T22:37:06Z | |
| dc.date.available | 2019-09-09T22:37:06Z | |
| dc.date.issued | 1996-09-30 | |
| dc.description | NIGMS NIH HHS (GM 39803) NIGMS NIH HHS (GM 47295) | |
| dc.description.abstract | The dissimilatory nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 catalyzes the reduction of nitrite to ammonia. Previous spectroscopic investigation revealed that it is a hexaheme cytochrome containing one high spin ferric heme and five low spin ferric hemes in the oxidized enzyme. The current study uses the high resolution of Mossbauer spectroscopy to obtain redox properties of the six heme groups. Correlating the Mossbauer findings with the EPR data reveals the pair-wise spin-spin coupling among four of the heme groups. The other two hemes are found to be magnetically isolated. Reduction with dithionite and reaction with CO further indicate that only the high spin heme is capable of binding small exogenous ligands. These results confirm our previous finding that Desulfovibrio desulfuricans nitrite reductase contains six heme groups and that the high spin ferric heme is the substrate and inhibitor binding site. | en |
| dc.description.version | publishersversion | |
| dc.description.version | published | |
| dc.format.extent | 6 | |
| dc.format.extent | 228798 | |
| dc.identifier.doi | 10.1074/jbc.271.38.23191 | |
| dc.identifier.issn | 0021-9258 | |
| dc.identifier.other | PURE: 14620899 | |
| dc.identifier.other | PURE UUID: 9a35afe4-bd50-4dc5-836f-af6fcd8e6b6f | |
| dc.identifier.other | Scopus: 0029841950 | |
| dc.identifier.other | PubMed: 8798514 | |
| dc.identifier.other | WOS: A1996VH76800040 | |
| dc.identifier.other | ORCID: /0000-0002-8611-9023/work/62320637 | |
| dc.identifier.other | ORCID: /0000-0002-4726-2388/work/68772360 | |
| dc.identifier.uri | http://www.scopus.com/inward/record.url?scp=0029841950&partnerID=8YFLogxK | |
| dc.identifier.url | https://www.scopus.com/pages/publications/0029841950 | |
| dc.language.iso | eng | |
| dc.peerreviewed | yes | |
| dc.subject | Biochemistry | |
| dc.subject | Molecular Biology | |
| dc.subject | Cell Biology | |
| dc.title | Redox properties of cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 | en |
| dc.type | journal article | |
| degois.publication.firstPage | 23191 | |
| degois.publication.issue | 38 | |
| degois.publication.lastPage | 23196 | |
| degois.publication.title | Journal of Biological Chemistry | |
| degois.publication.volume | 271 | |
| dspace.entity.type | Publication | |
| rcaap.rights | openAccess |
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