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Additional file 1: Figure S1. Alignment of the 49 sequences of DIRLs from bacteria and five selected plant DIRs sequences in clustal0 on Uniprot server (Align tools). The plant DIRs are F. intermedia FiDIR1, P. sativum DRR206, G. echinata PTS1, A. Thaliana atDIR5 and A. Thaliana atDIR6 (AtDIR6, DRR206 and PTS1 have a resolved 3D structures and FiDIR1 and AtDIR5 are also well characterized).

Additional file 2: Figure S2. Schematic representation of a part of the genome of 25 bacteria, Genomes are annotated manually in order to obtain genomic information around the genes encoding a potential DIRL. With the NCBI number of the bacteria genomes in the Table 1, the fasta sequence of the genome is obtain and zoomed on the DPL region. Softberry server is used to predict the -10 and -30 regulation zone before the ATG of each predicted gene. For the other DPL, or the DPL genes is not well positioned on the contigue or not found (the sequenced genome for these bacteria is not complete or in not operonique structure.

Combining a palladium-based complex with a laccase allows the oxidation of an alcohol substrate at room temperature and atmospheric pressure., The first example of a coupled catalytic system involving an enzyme and a palladium(ii) catalyst competent for the aerobic oxidation of alcohol in mild conditions is described. In the absence of dioxygen, the fungal laccase LAC3 is reduced by a palladium(0) species as evidenced by the UV/VIS and ESR spectra of the enzyme. During the oxidation of veratryl alcohol performed in water, at room temperature and atmospheric pressure, LAC3 regenerates the palladium catalyst, is reduced and catalyzes the four-electron reduction of dioxygen into water with no loss of enzyme activity. The association of a laccase with a water-soluble palladium complex results in a 7-fold increase in the catalytic efficiency of the complex. This is the first step in the design of a family of renewable palladium catalysts for aerobic oxidation.