Bioinformatic Analysis of Oxygen Sensitivity in Arcobacter bivalviorum's Pyruvate:Ferredoxin Oxidoreductase (PFOR)

Abdulmajeed Alqurashi

Abstract


Background: Arcobacter bivalviorum is an emerging foodborne pathogen particularly found in shellfish and other bivalves. This bacterium's metabolic versatility is highlighted by its possession of both the Pyruvate Dehydrogenase Complex (PDC) and Pyruvate:Ferredoxin Oxidoreductase (PFOR). The PFOR enzyme is crucial for linking glycolysis to the citric acid cycle. Previous studies of PFOR enzyme reveal its susceptibility to oxygen damage due to its reliance on Fe-S clusters for electron transfer.

Methods: The current study employs bioinformatic approaches to explore the oxygen sensitivity of A. bivalviorum's PFOR, comparing it with Desulfovibrio africanus and Moorella thermoacetica. The UniProt database was used to obtain the sequences of PFOR from D. africanus (CAA70873), A. bivalviorum (AXH11209), and M. thermoacetica (Q2RMD6). This comparative analysis sheds light on the structural similarities and differences between the enzymes, providing a deeper understanding of their functional mechanisms.

Result: PFOR enzyme is a heterodimer, with its functional subunits containing three [4Fe-4S]²⁺ clusters. Its exposed Fe-S clusters are vulnerable to oxygen and ROS, leading to enzyme inactivation. A comparison of PFOR sequences from D. africanus, M. thermoacetica, and A. bivalviorum reveals a crucial difference: the final 43 residues at the C-terminal of D. africanus are missing in the other two enzymes, depriving the M. thermoacetica and A. bivalviorum enzymes of a self-protective mechanism.

Conclusion: Pyruvate:ferredoxin oxidoreductase (PFOR) in A. bivalviorum lacks protection from oxidative damage due to the absence of the final 43 amino acids at the C-terminal.

Keywords: PFOR; Homology modeling; oxygen sensitivity; Foodborne pathogen 


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DOI: http://dx.doi.org/10.62940/als.v11i4.3142

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