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. Author manuscript; available in PMC: 2020 Jul 20.
Published in final edited form as: Subcell Biochem. 2020;94:345–382. doi: 10.1007/978-3-030-41769-7_14

Fig. 14.9.

Fig. 14.9

Superposed structures of T (blue), R (magenta), R3 (yellow), RR2 (green), R2 (black), and RR3 (salmon) on their α1β1 dimers. αArg141 participates in inter-subunit salt-bridge interaction with αAsp126 (as well as αLys127—not shown) in deoxygenated Hb stabilizing the low-affinity T state and facilitating O2 release. At higher pH, this interaction is broken increasing the mobility of αArg141, which facilitates the T → R transition, and increase Hb oxygen affinity