= Reinhold Benesch
{c}
\b[Reinhold Benesch] was a biochemist who investigated <hemoglobin> function in collaboration with <Ruth E. Benesch>. Their 1969 account of intracellular organic phosphates explained a mechanism by which <2,3-Bisphosphoglycerate> changes oxygen affinity: the regulator binds preferentially to <deoxyhemoglobin>, making oxygen release more favourable at a specified oxygen <partial pressure>. This identifies a chemical regulator of oxygen transport, rather than treating hemoglobin affinity as an immutable property of the isolated <protein>.<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}
The discovery is an example of <allostery>: ligand binding at one part of a molecular system affects binding elsewhere. A short equilibrium argument shows why the effect is reciprocal. Consider an original four-state model with one oxygen ligand $O$ and one regulator $B$, allowing states $H$, $HO$, $HB$ and $HOB$. Define <dissociation constants>
$$
K_O=\frac{[H][O]}{[HO]},\quad K_B=\frac{[H][B]}{[HB]},\quad
K_{O\mid B}=\frac{[HB][O]}{[HOB]},\quad
K_{B\mid O}=\frac{[HO][B]}{[HOB]}.
$$
Multiplying around the two possible binding paths gives
$$
\boxed{K_O K_{B\mid O}=K_B K_{O\mid B}.}
$$
Thus, if regulator binding makes oxygen ten times harder to bind in this model, $K_{O\mid B}/K_O=10$, oxygen binding must likewise increase the regulator's dissociation constant tenfold. An equilibrium coupling cannot act in only one direction. The four-state construction is an illustrative reduction, not a claim that the four oxygen-binding subunits of real hemoglobin behave as one physical site.
This reasoning motivates a controlled measurement: compare oxygen-equilibrium curves for matched <hemoglobin> preparations with different regulator concentrations, while controlling <pH>, <temperature> and solution composition. Measuring regulator binding as well tests the reciprocal side of the proposed mechanism. His coauthored 1969 paper with <Ruth E. Benesch> and <Chi Irg Yu> explicitly examined how several of these conditions enter the oxygenation problem.<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 and byline]{ref}
The scientific contribution is collective in these sources. Their joint paper does not establish a separate personal allocation of the chemical preparation, measurements and interpretation. The photograph below is the institutionally identified joint image, 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=<Reinhold Benesch> and <Ruth E. 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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