Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated α-chain from human hemoglobin A

Tran, Anh-Tuyet T.; Kolczak, Urszula; Mar, Gerd N. La

doi:10.1016/s1570-9639(03)00202-4

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“…This conclusion is consistent with previous findings that heme pocket structure is well preserved in isolated subunits, based on far-UV (69,70) and near-UV CD (69 -72) and homonuclear NMR studies of ferrous and ferric ␣Hb (47,55,56,73,74). None of these data provide any hints as to why free ␣Hb is more prone to oxidation and subsequent rapid loss of the heme moiety and aggregation.…”

Section: Discussionsupporting

confidence: 92%

α-Hemoglobin-stabilizing Protein (AHSP) Perturbs the Proximal Heme Pocket of Oxy-α-hemoglobin and Weakens the Iron-Oxygen Bond

Dickson

Rich

d’Avigdor

et al. 2013

Journal of Biological Chemistry

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Background: ␣-Hemoglobin stabilizing protein (AHSP) is a hemoglobin chaperone. Results: AHSP causes a subtle perturbation of the proximal heme pocket of O 2 -␣-hemoglobin, lengthening the Fe-O 2 bond and enhancing O 2 dissociation. Conclusion: Pro-30 in wild-type AHSP promotes ␣Hb autooxidation by introducing strain into the proximal heme pocket. Significance: ␣Hb⅐AHSP complexes are intermediates in Hb assembly and achieve ␣Hb detoxification.

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