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

FEBS Letters

Pisa, René¹  Eichler, Robert¹  Biel, Simone¹  Gross, Roland¹  Simon, Jörg¹ 

[1] Institut für Mikrobiologie, Johann Wolfgang Goethe-Universität, Marie-Curie-Str. 9, D-60439 Frankfurt am Main, Germany

关键词: Cytochrome c nitrite reductase;    Respiratory nitrite ammonification;    Heme c binding motif;    NapC/NirT family;    Cytochrome c biogenesis;    Wolinella succinogenes;    DMNH2;    2;    3-dimethyl-1;    4-naphthoquinol;   

DOI  :  10.1016/S0014-5793(02)02885-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown