Abstract
THE geometry of the metal–oxygen linkage of myoglobin and haemoglobin has not been determined in detail. Recent studies of the reversible oxygen-carrying cobalt complexes, Co(acacen)(B)O21,2 (acacen = N,N′-ethylenebis(acetylacetoniminide), (CH3–C(O−) = CH–C(CH3) = NCH2–)2, B = base; py and so on) and coboglobin3, the cobalt analogue of haemoglobin, indicate that the binding of oxygen in haemoglobin is essentially the same as that in the model 1 : 1 cobalt complexes. We now report the structure of a cobalt oxygen complex, analogous to Co(acacen)(B)O2, that provides information on the metal–oxygen linkage, relevant to the structures of oxymyoglobin and oxyhaemoglobin. This structure of Co-(bzacen)(pyridine)O2 (bzacen = N,N′-ethylenebis (benzoylacetoniminide), (C6H5–C(O−) = CH–C(CH3) = NCH2–)2, is shown in Fig. 1. As indicated by X-ray studies on oxymyoglobin4 and infrared and electron spin resonance (ESR) studies of Co(acacen)(B)O2 (ref. 2), the oxygen molecule is bound to cobalt in an angular manner.
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RODLEY, G., ROBINSON, W. Structure of a Monomeric Oxygen-carrying Complex. Nature 235, 438–439 (1972). https://doi.org/10.1038/235438a0
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DOI: https://doi.org/10.1038/235438a0
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