Modification of hemecbinding motifs in the small subunit (NrfH) of theWolinella succinogenescytochromecnitrite reductase complex
| Autor: | Simone Biel, René Pisa, Jörg Simon, Roland Gross, Robert Eichler |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Cytochrome
Respiratory nitrite ammonification Amino Acid Motifs Biophysics Cytochrome c Group Cytochromes c1 Heme Biochemistry Wolinella succinogenes Serine chemistry.chemical_compound Bacterial Proteins Nitrate Reductases Structural Biology Cytochromes a1 Genetics Cysteine Cytochrome c nitrite reductase Nitrite Molecular Biology Nitrites Binding Sites NapC/NirT family biology Cytochrome c RNA-Binding Proteins Cell Biology Culture Media Wolinella Heme C chemistry Cytochrome c biogenesis Mutagenesis Site-Directed biology.protein Oxidation-Reduction Heme c binding motif Transcription Factors |
| Zdroj: | FEBS Letters. 522:83-87 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(02)02885-5 |
| Popis: | The two multiheme c-type cytochromes NrfH and NrfA form a membrane-bound complex that catalyzes menaquinol oxidation by nitrite during respiratory nitrite ammonification of Wolinella succinogenes. Each cysteine residue of the four NrfH heme c binding motifs was individually replaced by serine. Of the resulting eight W. succinogenes mutants, only one is able to grow by nitrite respiration although its electron transport activity from formate to nitrite is decreased. NrfH from this mutant was shown by matrix-assisted laser desorption/ionization mass spectrometry to carry four covalently bound heme groups like wild-type NrfH indicating that the cytochrome c biogenesis system II organism W. succinogenes is able to attach heme to an SXXCH motif. |
| Databáze: | OpenAIRE |
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