2010
DOI: 10.1007/s11120-009-9524-1
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Heliobacterial Rieske/cytb complex

Abstract: Data on structure and function of the Rieske/cytb complex from Heliobacteria are scarce. They indicate that the complex is related to the b (6) f complex in agreement with the phylogenetic position of the organism. It is composed of a diheme cytochrome c, and a Rieske iron-sulfur protein, together with transmembrane cytochrome b (6) and subunit IV. Additional small subunits may be part of the complex. The cofactor content comprises heme c (i), first discovered in the Q(i) binding pocket of b (6) f complexes. T… Show more

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Cited by 18 publications
(17 citation statements)
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“…Unfortunately, as discussed in Baymann and Nitschke (2010), the lack of a functional isolate hampers more indepth comparisons of the heliobacterial complex with its better studied homologs. Nevertheless, the results obtained on Heliobacteria so far (summarised in Baymann and Nitschke 2010) are helpful to better define the evolutionary appearance of specific marker traits and functional particularities within this enzyme family.…”
Section: Discussionmentioning
confidence: 99%
See 3 more Smart Citations
“…Unfortunately, as discussed in Baymann and Nitschke (2010), the lack of a functional isolate hampers more indepth comparisons of the heliobacterial complex with its better studied homologs. Nevertheless, the results obtained on Heliobacteria so far (summarised in Baymann and Nitschke 2010) are helpful to better define the evolutionary appearance of specific marker traits and functional particularities within this enzyme family.…”
Section: Discussionmentioning
confidence: 99%
“…Nevertheless, the results obtained on Heliobacteria so far (summarised in Baymann and Nitschke 2010) are helpful to better define the evolutionary appearance of specific marker traits and functional particularities within this enzyme family.…”
Section: Discussionmentioning
confidence: 99%
See 2 more Smart Citations
“…1B), because CO 2 is produced through the OTCA cycle. Table 2 shows that over 50% aspartate and 60% glutamate were labeled in the ␤-carboxyl group with [1][2][3][4][5][6][7][8][9][10][11][12][13] C]pyruvate as the carbon source, implying that citrate formation is possibly catalyzed by (Re)-citrate synthase ((Re)-CS) (Fig. 3).…”
Section: Carbon Metabolism In H Modesticaldummentioning
confidence: 99%