Investigations on non-heme iron-oxygen proteins : II. The nature of the ESR signal at gav below 2 in hemerythrin
✍ Scribed by Ernst Bayer; Peter Krauss; Albert Röder; Peter Schretzmann
- Book ID
- 104106036
- Publisher
- Elsevier Science
- Year
- 1972
- Weight
- 438 KB
- Volume
- 1
- Category
- Article
- ISSN
- 0006-3061
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✦ Synopsis
During isolation and purification of oxyhemerythrin from the blood cells of Golfingia gouldii, some of the native oxygen adduct is transformed to a species, which liberates no more oxygen on lowering the 0 2 partial pressure . he amount of this aged species formed depends upon methods and duration of the purification process . he electronic spectrum of aged oxyhemerythrin is characterized by a strong absorption maximum at 360 nm-in contrast to the native oxygen complex which shows only a weak shoulder in this region . n the partially reduced state aged oxyhemerythrin displays an Ei signal similar to those of reduced non-heme iron-sulfur proteins, with gav < 2, (gil = 1 .85, rq~ = 1 .96) and a strong temperature dependence of the signal amplitude . he aged oxyhemerythrin is not denatured since it can be reconverted to oxyhemerythrin by full reduction and reoxygenation . t is supposed that the E active species contains a (Fe 02 Fe group with an odd electron delocalized over the whole non-heme ironoxygen center .
E D E activity of partially reduced aged oxyhemerythrin . arallels to reduced non-heme iron-sulfur proteins .