= Ruth E. Benesch
{c}
\b[Ruth E. Benesch] was a biochemist whose work with <Reinhold Benesch> investigated <hemoglobin> and its interaction with small-molecule regulators. Their jointly authored 1969 account connected <2,3-Bisphosphoglycerate> in <red blood cells> with lower oxygen affinity through preferential binding to <deoxyhemoglobin>. The published full byline uses Ruth E. Benesch; the middle initial is retained here.<Intracellular Organic Phosphates as Regulators of Oxygen Release by Haemoglobin by Reinhold Benesch and Ruth E. Benesch>[Publisher byline and abstract, Nature221, pp.618–622, 1969]{ref}
She was first author of a separate 1969 study of <hemoglobin> oxygenation in the presence of the same metabolite, with <Reinhold Benesch> and <Chi Irg Yu>. Its stated experimental variables were <temperature>, <pH>, <ionic strength> and hemoglobin concentration. Those variables matter because a ligand's effect is a property of the complete chemical equilibrium under specified conditions, not just the name of the ligand. The shared byline supports a collaborative contribution; it does not identify who performed every apparatus task.<Oxygenation of hemoglobin in the presence of 2,3-diphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration by Ruth E. Benesch and others>[Publisher title, byline and original June1969 issue information]{ref}
An original binding calculation illustrates why protein concentration belongs in such a comparison. In a deliberately simplified one-site model, let $H_T$ be the total concentration of binding sites, $B$ the free concentration of <2,3-Bisphosphoglycerate>, and $K_d$ its <dissociation constant>. The bound concentration is
$$
[HB]=H_T\frac{B}{K_d+B},\qquad B_T=B+[HB].
$$
At $H_T=1.0\,\mathrm{mM}$ and $B=K_d=0.10\,\mathrm{mM}$, half the sites are occupied: $[HB]=0.50\,\mathrm{mM}$. The total ligand concentration is $B_T=0.60\,\mathrm{mM}$, not $0.10\,\mathrm{mM}$. Substituting total concentration for free concentration would predict a different occupancy. These are stipulated numbers, not measured binding constants from her paper.
The biochemical insight extends beyond the small molecule: oxygenation and regulator binding are coupled properties of a <protein>. Their 1969 joint account describes one bound phosphate-metabolite molecule per hemoglobin tetramer, rather than one for every oxygen-binding subunit. This distinguishes regulatory stoichiometry from oxygen-carrying capacity.<Intracellular Organic Phosphates as Regulators of Oxygen Release by Haemoglobin by Reinhold Benesch and Ruth E. Benesch>[Abstract: preferential deoxyhaemoglobin binding and one molecule per tetramer]{ref}
The historical photograph below is explicitly identified by the Science History Institute and credited to Columbia University's Department of Biochemistry.<Reinhold and Ruth Benesch photograph at the Science History Institute>[Photograph caption and credit]{ref}
\Image[https://www.sciencehistory.org/wp-content/uploads/2023/04/benesch_reinhold_and_ruth_columbia_univ-640x500.jpg]
{title=<Ruth E. Benesch> with <Reinhold Benesch>, identified together by the Science History Institute}
{description=Historical photograph credited by the holding institution to the Department of Biochemistry, Columbia University. External image; no local copy.}
{width=360}
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