Isabel Moura

TL;DR: In this paper, the authors unraveled the mechanisms supporting the respiratory versatility of Desulfovibrio desulfuricans through the analysis of the proteome of the bacterium under different experimental conditions, showing that the most remarkable difference in the two-dimensional gel electrophoresis maps is the high number of spots exclusively represented in the nitrate medium.

TL;DR: Crystals of the fully oxidized form of desulfoferrodoxin were obtained by vapor diffusion from a solution containing 20% PEG 4000, 0.1 M HEPES buffer, pH 7.5, and 0.2 M CaCl2.

TL;DR: The orange-coloured protein (ORP) from Desulfovibrio gigas is a 12 kDa protein that contains a novel mixed-metal sulfide cluster of the type [S(2)MoS( 2)CuS(3)MoM(2), which has shown the versatility of the H2O/O2 mixture.

TL;DR: An enhanced cathodic signal for the activated enzyme was observed under turnover conditions, which is explained by the binding of nitrous oxide to CuZ0(4Cu1S), an intermediate species in the catalytic cycle.

TL;DR: In this article, a structural component of the hydrogenases isolated from Desulfovibrio gigas was shown to contain EPR nickel redox dependent signals, with g-values 2.31, 2.23 and 2.02 (see Fig. 1).