Poster Presentation The 48th Lorne Conference on Protein Structure and Function 2023

The structure of the complex between the arsenite oxidase from Pseudorhizobium banfieldiae sp. str. NT-26 and its native electron acceptor cytochrome c552. (#413)

Nilakhi Poddar 1 , Megan Maher 1 2 , Joanne Santini 3
  1. School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne, VIC, Australia
  2. Department of Biochemistry and Genetics,, La Trobe Institute for Molecular Science, La Trobe University,, Melbourne, Victoria, Australia
  3. Division of Biosciences, University College London, London, Bloomsbury, United kingdom

Arsenic, a toxic metalloid is naturally found in the environment but can exist as a harmful pollutant generated from industrial waste waters and gold mines. This poses a great threat to human health by contaminating the ground water system. Arsenic can exist in both organic and inorganic forms and in four oxidation states, arsines and methyl arsines (As3-), elemental arsenic (As0), arsenite (AsO33-) and arsenate (AsO43-). Although arsenic is toxic and hazardous to human health, some prokaryotes have developed unique mechanisms that utilize inorganic forms of arsenic, such as arsenite (AsO33-) and arsenate (AsO43-) for respiration.

The organism Psuedorhizobium sp. str. NT-26 respires with arsenite and employs the arsenite oxidase (AioAB) for its crucial respiratory activity, which catalyzes the oxidation of arsenite to arsenate. The AioAB enzyme consists of two subunits: AioA (contains a molybdenum center and 3Fe-4S cluster) and AioB (contains a Rieske [2Fe-2S] cluster). Arsenite is oxidized to arsenate at the Mo site, concomitantly reducing Mo(VI) to Mo(IV). The electrons are then passed to the 3Fe-4S cluster, the Rieske cluster in AioB and to an electron acceptor, which is cytochrome c552 (cytc552). The crystal structure of the AioAB/cytc552 electron transfer complex reveals two A2B2/(cytc552)2 assemblies per asymmetric unit. Three of the four cytc552 molecules in the asymmetric unit dock with AioAB in a cleft at the interface between the AioA and AioB subunits, with an edge-to-edge distance of 7.5 Å between the heme of cytc552 and the [2Fe-2S] Rieske cluster in the AioB subunit. The interface between the AioAB and cytc552 proteins features electrostatic and non-polar interactions and is stabilized by two salt-bridges. This presentation will discuss the transient and catalytically efficient nature of the AioAB/cytc552 complex that underpins the ability of this organism to respire using the arsenite present in contaminated environments.