Open AccessA heterodimeric cytochrome c complex with a very low redox potential from an anaerobic ammonium‐oxidizing enrichment culture
Author(s) -
Ukita Saki,
Fujii Takao,
Hira Daisuke,
Nishiyama Takashi,
Kawase Tatsushi,
Migita Catharina T.,
Furukawa Kenji
Publication year - 2010
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2010.02122.x
Subject(s) - redox , heme , chemistry , cytochrome , electron transfer , cytochrome c , hemeprotein , biochemistry , anammox , dithionite , ferredoxin , photochemistry , denitrification , inorganic chemistry , mitochondrion , enzyme , denitrifying bacteria , organic chemistry , nitrogen
A dimeric cytochrome c with an apparent molecular mass of 25 kDa was isolated from an anammox bacterium, strain KSU‐1, in a relatively large quantity. This protein was named the NaxLS complex. The spectrum of the oxidized form exhibited a peculiar Soret peak at 419 nm. The reduction of NaxLS was not complete even with the addition of excess dithionite, but was complete with titanium (III) citrate, indicating that the NaxLS complex has a very low redox potential. The genes encoding the two subunits, naxL and naxS , are adjacent on the genome. The deduced amino‐acid sequences of the genes showed high identities with those of two genes encoding ‘unknown proteins’ in the genome of Candidatus Kuenenia stuttgartiensis, but had lower identities with other c ‐type heme proteins. The electron paramagnetic resonance spectra of NaxLS exhibited low‐spin signals of two heme species in the range between g =2.6 and g =1.8, which strongly suggested an unusual His/Cys coordination. This unique coordination might account for the low redox potential of the hemes in NaxLS. NaxLS might participate in the transfer of low redox potential electrons in the intracellular anammoxosome compartment or the cytoplasm.