Magnetically induced circular dichroism (MCD), is the differential absorption of left and right circularly polarized light in the presence of a magnetic field. In general, this means wrapping a circular dichrometer in a large electromagnet. If the magnet is water cooled, field strength of a couple tesla are common. With a supercooled magnet, field strengths can reach 5 tesla.
MCD measurements are made by taking a circular dichroism, or CD measurement, with the magnetization oriented in the positive sense, and then a CD measurement with the magnetization oriented in the negative sense. The two signals are then subtracted:
- Signal 1 = CD + MCD
- Signal 2 = CD - MCD
- Signal 1 - Signal 2 = 2 MCD
The physical processes that lead to MCD are substantively different than those of CD itself. At any given wavelength, MCD will not exist unless the molecule has an optical absorption at that wavelength. This is very unlike CD, which can have a measurable signal in ranges where no substantive optical absorption exists.
In the most common kind of MCD (the so called C spectra), the magnetic field breaks the degeneracy of excited state optical energy levels differing only in magnetic spin. This separation is small, leading to a tiny shift in frequency in otherwise nearly identical spectrum, that, because of different signs of the spin state, are opposite in sign. As a consequence, this kinds of MCD absorption (so called C spectra) are shaped like a frequency derivative of the underlying optical spectra, having a peak on one side of the related optical maximum and a trough on the other side.
In type A spectra, MCD absorption is a consequence of the magnetic field breaking the degeneracy of the ground state of the optical absorption. Unlike C spectra, the intensity of A spectra are affected by temperature, with stronger signals being observed as the sample is cooled. For samples exhibiting both A and C class spectra, taking the MCD as a function of temperature is a way to separate the relative contributions of these two effects.
In biology, metalloproteins are the most likely candidates for MCD measurements, as the presence of metals with degenerate energy levels leads to strong MCD signals. In the case of ferric hemoproteins, MCD is capable of determining both oxidation and spin state to a remarkably exquisite degree. In regular proteins, MCD is capable of stoichiometrically measuring the tryptophan content of proteins, assuming there are no other competing absorbers in the spectroscopic system.