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Modification of heme c binding motifs in the small subunit (NrfH) of the Wolinella succinogenes cytochrome c nitrite reductase complex.

Simon, J. ; Eichler, R. ; Pisa, R. ; Biel, S. ; Gross, R. (2002)
Modification of heme c binding motifs in the small subunit (NrfH) of the Wolinella succinogenes cytochrome c nitrite reductase complex.
In: FEBS letters, 522 (1-3)
Artikel, Bibliographie

Kurzbeschreibung (Abstract)

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.

Typ des Eintrags: Artikel
Erschienen: 2002
Autor(en): Simon, J. ; Eichler, R. ; Pisa, R. ; Biel, S. ; Gross, R.
Art des Eintrags: Bibliographie
Titel: Modification of heme c binding motifs in the small subunit (NrfH) of the Wolinella succinogenes cytochrome c nitrite reductase complex.
Sprache: Englisch
Publikationsjahr: 2002
Titel der Zeitschrift, Zeitung oder Schriftenreihe: FEBS letters
Jahrgang/Volume einer Zeitschrift: 522
(Heft-)Nummer: 1-3
Kurzbeschreibung (Abstract):

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.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie > Microbial Energy Conversion and Biotechnology
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10 Fachbereich Biologie
Hinterlegungsdatum: 07 Dez 2010 15:16
Letzte Änderung: 05 Mär 2013 09:42
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