The 143Cys mutant, however, still maintains some activity and indicates that the role of the –S-S- bond is not similar to the ferredoxin:thioredoxin reductase system. The disulphide bond appears to have a structural role, ensuring close proximity of PQQ to cytochrome c. Substitution of one or both of the Cys with Ser residues would increase flexibility of the enzyme leading

to a conformational change with a negative 5-FU mw impact on the electron flow. Homology structure prediction indicates that mutation to either one or both Cys residues would result in a conformation change, notably, protein homology structure of the 143CysSer mutant (Fig. 5b) with Chimera software (Pettersen et al., 2004) predicted three major deviations from wild-type LH structure (Fig. 5a) in terms of α-helices Galunisertib mw and four differences in β-pleated sheets. The predicted tertiary structure of the 124,143CysSer mutant (Fig. 5c) appeared to deviate even more from the wild type with six changes in α-helices and nine differences in β-pleated sheets. More importantly, the N-terminal and cytochrome c domain linker appears

to be significantly affected. These mutations appear to have resulted in the enlargement of the molecule with a possible significant effect on the active site. Thus, the loss of disulphide bond alters the structure dramatically and probably affects the enzyme activity because of changes to the cytochrome c domain. In conclusion, SPTBN5 LH is in possession of a disulphide bond formed between spatially distal residues 124Cys and 143Cys. Although this bond is not undergoing cycles of reduction and oxidation during catalytic breakdown of the substrate, its formation is crucial for enzyme activity as it ensures structural rigidity and correct protein conformation. This work was privately funded and supported by IBERS, Aberystwyth University. We would like to acknowledge Dr Ian Mercer and

Dr Maurice Bosch for proof reading the drafts. Molecular graphics images were produced using the UCSF Chimera package from the Resource for Biocomputing, Visualization and Informatics at the University of California, San Francisco (supported by NIH P41 RR001081). “
“Several representatives of the euryarchaeal class Archaeoglobi are able to grow facultative autotrophically using the reductive acetyl-CoA pathway, with ‘Archaeoglobus lithotrophicus’ being an obligate autotroph. However, genome sequencing revealed that some species harbor genes for key enzymes of other autotrophic pathways, i.e. 4-hydroxybutyryl-CoA dehydratase of the dicarboxylate/hydroxybutyrate cycle and the hydroxypropionate/hydroxybutyrate cycle and ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) of the Calvin–Benson cycle. This raised the question of whether only one or multiple autotrophic pathways are operating in these species. We searched for the presence of enzyme activities specific for the dicarboxylate/hydroxybutyrate or the hydroxypropionate/hydroxybutyrate cycles in ‘A.