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Cytochrome c Reductase is a Key Enzyme Involved in the Extracellular Electron Transfer Pathway towards Transition Metal Complexes in Pseudomonas Putida.


ABSTRACT: Mediator-based extracellular electron transfer (EET) pathways can balance the redox metabolism of microbes. However, such electro-biosynthesis processes are constrained by the unknown underlying EET mechanisms. In this paper, we studied Pseudomonas putida to systematically investigate its EET pathway to transition metal complexes (i.e. [Fe(CN) 6 ] 3-/4- and [Co(bpy) 3 ] 3+/2+ ) under anaerobic conditions. Comparative proteomics showed the aerobic respiratory components were upregulated in a bioelectrochemical system without oxygen, suggesting their potential contribution to EET. Further tests found inhibiting cytochrome c oxidase activity by NaN 3 and NADH dehydrogenase by rotenone did not significantly change the current output. However, the EET pathway was completely blocked, while cytochrome c reductase activity was inhibited by antimycin A. Although it cannot be excluded that cytochrome c and the periplasmic subunit of cytochrome c oxidase donate electrons to the transition metal complexes, these results strongly demonstrate that cytochrome c reductase is a key complex for the EET pathway.

SUBMITTER: Lai B 

PROVIDER: S-EPMC7589348 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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Cytochrome c Reductase is a Key Enzyme Involved in the Extracellular Electron Transfer Pathway towards Transition Metal Complexes in Pseudomonas Putida.

Lai Bin B   Bernhardt Paul V PV   Krömer Jens O JO  

ChemSusChem 20200817 19


Mediator-based extracellular electron transfer (EET) pathways can balance the redox metabolism of microbes. However, such electro-biosynthesis processes are constrained by the unknown underlying EET mechanisms. In this paper, Pseudomonas putida was studied to systematically investigate its EET pathway to transition metal complexes (i. e., [Fe(CN)<sub>6</sub> ]<sup>3-/4-</sup> and [Co(bpy)<sub>3</sub> ]<sup>3+/2+</sup> ; bpy=2,2'-bipyridyl) under anaerobic conditions. Comparative proteomics showe  ...[more]

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