Journal article
The structure of the complex between the arsenite oxidase from Pseudorhizobium banfieldiae sp. strain NT-26 and its native electron acceptor cytochrome c552
N Poddar, JM Santini, MJ Maher
Acta Crystallographica Section D Structural Biology | INT UNION CRYSTALLOGRAPHY | Published : 2023
Abstract
The arsenite oxidase (AioAB) from Pseudorhizobium banfieldiae sp. strain NT-26 catalyzes the oxidation of arsenite to arsenate and transfers electrons to its cognate electron acceptor cytochrome c552 (cytc552). This activity underpins the ability of this organism to respire using arsenite present in contaminated environments. 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 to 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 ..
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Awarded by University of Melbourne
Funding Acknowledgements
This research was supported by an Australian Research Council (ARC) Future Fellowship (FT180100397) to MJM and a Biotechnology and Biological Sciences Research Council (BBSRC) grant (BB/N012674/1) to JMS. NP was supported by a University of Melbourne Research Scholarship.