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Experimental Mössbauer parameters [isomer shift (IS) and quadruple splitting (QS)] ascribed to native and substrate-bound forms of Fe2+–hARD and the difference between the two spectral Fe2+ components (Δ) in Fe–hARD–ACI. The signal assigned to Fe3+ is not reported in the table because it is not related to an active form of the holoenzyme.
| Fe2+–hARD | Fe2+–hARD–ACI | |||
|---|---|---|---|---|
| red | red | dark-red | Δ | |
| IS [mm s−1] | 1.215(3) | 1.217(7) | 1.15(2) | −0.06(1) |
| QS [mm s−1] | 3.165(5) | 3.105(12) | 2.66(10) | −0.45(10) |
