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His more than 200 publications have established Mössbauer spectroscopy as a primary tool for studying proteins containing complex iron centers. Over the past thirty years, he has unraveled the electronic structures of metal clusters in numerous iron-sulfur proteins and iron-oxo enzymes and revealed the molecular mechanism by which many important enzymes activate molecular oxygen and catalyze reactions essential to life. He discovered the first example of a coupled chromophore assembly in the enzyme sulfite reductase, elucidated the structure of 3Fe-clusters, provided final spectroscopic proof for almost all molecular systems containing Fe(IV) known to present, and demonstrated the existence of double and antisymmetric exchange in molecular systems. Eckard Münck's inventive analyses have turned spin physics into a powerful tool for structure determination.
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