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1. Mössbauer spectra were measured of adrenodoxin purified from porcine adrenal glands. They show similarities to the spectra of the plant ferredoxins. All of these proteins contain two atoms of iron and two of inorganic sulphide per molecule, and on reduction accept one electron. 2. As with the plant ferredoxins the adrenodoxin for these measurements was enriched with (57)Fe by reconstitution of the apo-protein, and subsequently was carefully purified and checked by a number of methods to ensure that it was in the same conformation as the native protein and contained no extraneous iron. 3. The Mössbauer spectra of oxidized adrenodoxin at temperatures from 4.2 degrees K to 197 degrees K show that the iron atoms are probably high-spin Fe(3+), and in similar environments, and experience little or no magnetic field from the electrons. 4. Mössbauer spectra of reduced adrenodoxin showed magnetic hyperfine structure at all temperatures from 1.7 degrees K to 244 degrees K, in contrast with the reduced plant ferredoxins, which showed it only at lower temperatures. This is a consequence of a longer electron-spin relaxation time in reduced adrenodoxin. 5. At 4.2 degrees K in a small magnetic field the spectrum of reduced adrenodoxin shows a sixline Zeeman pattern due to Fe(3+) superimposed upon a combined magnetic and quadrupole spectrum due to Fe(2+). 6. In a large magnetic field (30kG) each hyperfine pattern is further split into two. Analysis of these spectra at 4.2 degrees K and 1.7 degrees K shows that the effective fields at the Fe(3+) and Fe(2+) nuclei are in opposite directions. This agrees with the proposal, first made for the ferredoxins, that the iron atoms are antiferromagnetically coupled. 7. In accord with the model for the ferredoxins, it is proposed that the oxidized adrenodoxin contains two high-spin Fe(3+) atoms which are antiferromagnetically coupled; on reduction one iron atom becomes high-spin Fe(2+).

Mössbauer studies of adrenodoxin. The mechanism of electron transfer in a hydroxylase iron–sulphur protein