Moessbauer and integer-spin EPR of the oxidized P-clusters of nitrogenase: POX is a non-Kramers system with a nearly degenerate ground doublet

Autor:	Eckard Münck, Michael P. Hendrich, Patricia D. Christie, Dirk Rottgardt, Kristene K. Surerus, William H. Orme-Johnson
Rok vydání:	1992
Předmět:	Chemistry Analytical chemistry General Chemistry Biochemistry Redox Catalysis law.invention Electron transfer Crystallography Colloid and Surface Chemistry law Mössbauer spectroscopy Cluster (physics) Diamagnetism Electron paramagnetic resonance Spin (physics) Hyperfine structure
Zdroj:	Journal of the American Chemical Society. 114:8579-8590
ISSN:	1520-5126 0002-7863
Popis:	The molybdenum-iron protein of nitrogenase contains 2 Mo atoms and ca. 28-30 Fe atoms. Approximately 16 Fe atoms belong to the P-clusters, a novel type of iron-sulfur cluster of unknown structure. Mossbauer studies have established that P-clusters are diamagnetic in the semireduced state, P N . Upon oxidation of the protein with redox dyes such as thionin the state P OX is attained. Previous studies have revealed that the low-temperature (≤4.2 K) Mossbauer spectra of P OX exhibit magnetic hyperfine patterns even in the absence of external magnetic fields
Databáze:	OpenAIRE
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