Abstract:
:G. metallireducens bacterium has highly versatile respiratory pathways that provide the microorganism an enormous potential for many biotechnological applications. However, little is known about the structural and functional properties of its electron transfer components. In this work, the periplasmic cytochrome PpcA from G. metallireducens was studied in detail for the first time using complementary biophysical techniques, including UV-visible, CD and NMR spectroscopy. The results obtained showed that PpcA contains three low-spin c-type heme groups with His-His axial coordination, a feature also observed for its homologue in G. sulfurreducens. However, despite the high sequence homology between the two cytochromes, important structural and functional differences were observed. The comparative analysis of the backbone, side chain and heme substituents NMR signals revealed differences in the relative orientation of the hemes I and III. In addition, redox titrations followed by visible spectroscopy showed that the redox potential values for PpcA from G. metallireducens (-78 and -93 mV at pH 7 and 8, respectively) are considerably less negative. Overall, this study provides biochemical and biophysical data of a key cytochrome from G. metallireducens, paving the way to understand the extracellular electron transfer mechanisms in these bacteria.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Portela PC,Fernandes TM,Dantas JM,Ferreira MR,Salgueiro CAdoi
10.1016/j.abb.2018.02.017subject
Has Abstractpub_date
2018-04-15 00:00:00pages
8-16eissn
0003-9861issn
1096-0384pii
S0003-9861(18)30067-5journal_volume
644pub_type
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