Mössbauer effect in synthetic analogs of rubredoxin
✍ Scribed by A. Kostikas; V. Petrouleas; A. Simopoulos; D. Coucouvanis; D.G. Holah
- Publisher
- Elsevier Science
- Year
- 1976
- Tongue
- English
- Weight
- 297 KB
- Volume
- 38
- Category
- Article
- ISSN
- 0009-2614
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✦ Synopsis
measurements have been performed on three recently synthesized i%(H) compkes with tetrahedral sulphur coordinatipn, simuIating the active center in reduced rubredoxin. One of the complcscs has virtually identical hfiissbsuor parameters with reduced rubredosin. A class of biomolecules particularly important in a variety of electron transfer processes are the nonhemq iron sulphur proteins [l f (NHISP). The electronic structures of the iron atoms in these proteins have been &died extensively. by a variety of physicaf techniques [2] _ Recently, X-ray crystallographic studies have been reported ok sevc:r3! of these moiecuies.
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📜 SIMILAR VOLUMES
## Abstract Studies are made of Mössbauer absorption of Fe^57^ in biotite. The asymmetric double peak spectrum is explained by quadrupole splitting; the energy levels are influenced by the presence of OH‐groups in the octahedral surrounding of the Fe‐ions.