Interaction of copper(II) and manganese(II) with hemoglobin

Chiang, Scott C.; Sprecher, Richard F.; Schweighardt, F.K.; Li, Norman C.

doi:10.1016/0022-1902(75)80760-3

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1975

1977

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“…Other possible paramagnetic labels involve ions such as Cu2+ and Mn2+. They have been used much less extensively until now (Vanngard, 1972;Chiang et al, 1975;Armbrecht et al, 1976). The present work is concerned with a study of Cu2+ ions bound to met-myoglobin crystals.…”

Section: Introductionmentioning

confidence: 99%

Electron paramagnetic resonance of Cu2+:Mb single crystal. Conformational changes

Nascimento¹,

Ribeiro²,

Bemski³

1977

Biophysical Journal

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Copper introduced into met-myoglobin crystals occupies various sites as indicated by electron paramagnetic resonance parameters. Cu2+ (A) is probably liganded to histidine A10, lysine A14, and asparagine GH4 (Banaszak et al., 1965) and shows superhyperfine interaction with a single (imidazole) nitrogen. Cu2+ (B) and Cu2+ (C) correspond to other anisotropic sites described in less detail. Cu2+ (A) exhibits a transition to an isotropic form with a transition temperature of 40.5 degrees C. This transition indicates a conformational change in myoglobin and could correspond to a motion of A helix away from the GH section. The transition temperature is 7 degrees C higher than the one previously reported (Atanasov, 1971) for myoglobin in solution.

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Section: Introductionmentioning

confidence: 99%