Search

The traditional "leaky pipeline" plots are widely used to inform gender equality policy and practice. Herein, we demonstrate how a statistical phenomenon known as Simpson's paradox can obscure trends in gender "leaky pipeline" plots. Our approach has been to use Excel spreadsheets to generate hypothetical "leaky pipeline" plots of gender inequality within an organisation. The principal factors, which make up these hypothetical plots, can be input into the model so that a range of potential situations can be modelled. How the individual principal factors are then reflected in "leaky pipeline" plots is shown. We find that the effect of Simpson's paradox on leaky pipeline plots can be simply and clearly illustrated with the use of hypothetical modelling and our study augments the findings in other statistical reports of Simpson's paradox in clinical trial data and in gender inequality data. The findings in this paper, however, are presented in a way, which makes the paradox accessible to a wide range of people.

The traditional ‘leaky pipeline’ plots are widely used to inform gender equality policy and practice. Herein, we demonstrate how a statistical phenomenon known as Simpson’s paradox can obscure trends in gender ‘leaky pipeline’ plots. Our approach has been to use Excel spreadsheets to generate hypothetical ‘leaky pipeline’ plots of gender inequality within an organisation. The principal factors, which make up these hypothetical plots, can be input into the model so that a range of potential situations can be modelled. How the individual principal factors are then reflected in ‘leaky pipeline’ plots is shown. We find that the effect of Simpson’s paradox on leaky pipeline plots can be simply and clearly illustrated with the use of hypothetical modelling and our study augments the findings in other statistical reports of Simpson’s paradox in clinical trial data and in gender inequality data. The findings in this paper, however, are presented in a way, which makes the paradox accessible to a wide range of people.

Strategies for O2 activation by copper enzymes were recently expanded to include mononuclear Cu sites, with the discovery of the copper-dependent polysaccharide monooxygenases, also classified as auxiliary-activity enzymes 9-11 (AA9-11). These enzymes are finding considerable use in industrial biofuel production. Crystal structures of polysaccharide monooxygenases have emerged, but experimental studies are yet to determine the solution structure of the Cu site and how this relates to reactivity. From X-ray absorption near edge structure and extended X-ray absorption fine structure spectroscopies, we observed a change from four-coordinate Cu(ll) to three-coordinate Cu(l) of the active site in solution, where three protein-derived nitrogen ligands coordinate the Cu in both redox states, and a labile hydroxide ligand is lost upon reduction. The spectroscopic data allowed for density functional theory calculations of an enzyme active site model, where the optimized Cu(l) and (II) structures were consistent with the experimental data. The O2 reactivity of the Cu(l) site was probed by EPR and stopped-flow absorption spectroscopies, and a rapid one-electron reduction of O2 and regeneration of the resting Cu(ll) enzyme were observed. This reactivity was evaluated computationally, and by calibration to Cu-superoxide model complexes, formation of an end-on Cu-AA9-superoxide species was found to be thermodynamically favored. We discuss how this thermodynamically difficult one-electron reduction of O2 is enabled by the unique protein structure where two nitrogen ligands from His1 dictate formation of a T-shaped Cu(l) site, which provides an open coordination position for strong O2 binding with very little reorganization energy. [ABSTRACT FROM AUTHOR]

Strategies for O2 activation by copper enzymes were recently expanded to include mononuclear Cu sites, with the discovery of the copper-dependent polysaccharide monooxygenases, also classified as auxiliary-activity enzymes 9-11 (AA9-11). These enzymes are finding considerable use in industrial biofuel production. Crystal structures of polysaccharide monooxygenases have emerged, but experimental studies are yet to determine the solution structure of the Cu site and how this relates to reactivity. From X-ray absorption near edge structure and extended X-ray absorption fine structure spectroscopies, we observed a change from four-coordinate Cu(II) to three-coordinate Cu(I) of the active site in solution, where three protein-derived nitrogen ligands coordinate the Cu in both redox states, and a labile hydroxide ligand is lost upon reduction. The spectroscopic data allowed for density functional theory calculations of an enzyme active site model, where the optimized Cu(I) and (II) structures were consistent with the experimental data. The O2 reactivity of the Cu(I) site was probed by EPR and stopped-flow absorption spectroscopies, and a rapid one-electron reduction of O2 and regeneration of the resting Cu(II) enzyme were observed. This reactivity was evaluated computationally, and by calibration to Cu-superoxide model complexes, formation of an end-on Cu-AA9-superoxide species was found to be thermodynamically favored. We discuss how this thermodynamically difficult one-electron reduction of O2 is enabled by the unique protein structure where two nitrogen ligands from His1 dictate formation of a T-shaped Cu(I) site, which provides an open coordination position for strong O2 binding with very little reorganization energy.