Redox properties of cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774

Cristina Costa, José J. G. Moura, Isabel Moura, Yaning Wang, Boi Hanh Huynh

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)
3 Downloads (Pure)

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.

Original languageEnglish
Pages (from-to)23191-23196
Number of pages6
JournalJournal of Biological Chemistry
Volume271
Issue number38
DOIs
Publication statusPublished - 30 Sep 1996

Fingerprint

Dive into the research topics of 'Redox properties of cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774'. Together they form a unique fingerprint.

Cite this