Match the mode of dioxygen binding (column – II) to the proteins (column – I).Column – I Column – II i. Hemoglobin P. η1-end-on peroxo ii. Hemocyanin Q. η1-end-on superoxo iii. Hemerythrin R. μ−η1:η1-end-on peroxo iv. Hemosiderin S. μ−η2:η2-side-on peroxo T. μ−η2-oxo
i – Q , ii – S , iii – P , iv – T
The three natural oxygen carriers bind O2 in quite different ways, and the iron storage material hemosiderin contains oxo-bridged iron.
i. Hemoglobin: O2 binds end-on and bent to a single Fe; the Fe(III)–O2− description (ν(O–O) about 1105 cm−1) makes it η1-end-on superoxo (Q).
ii. Hemocyanin: two Cu(II) ions sandwich a peroxide bound side-on to both metals, μ-η2:η2-peroxo (S), ν(O–O) about 750 cm−1.
iii. Hemerythrin: O2 binds to only one Fe of the diiron site as a terminal hydroperoxide, i.e. η1-end-on peroxo (P), hydrogen-bonded to the μ-oxo bridge. iv. Hemosiderin, like ferritin, is a polymeric iron(III) oxide-hydroxide built from oxo-bridged iron, matching the μ-oxo entry (T).
Matches that assign the side-on peroxo to hemosiderin or the bridging end-on peroxo to hemocyanin confuse the structures; the μ-η1:η1 peroxo mode is found in synthetic dicopper or diiron complexes, not in these proteins.
i – Q , ii – S , iii – P , iv – T option is correct.
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