Titlebook: Metallocofactors that Activate Small Molecules; With Focus on Bioino Markus W. Ribbe Book 2019 Springer Nature Switzerland AG 2019 Nitrogen

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Mechanism of Ni,Fe-Containing Carbon Monoxide Dehydrogenases,eria and archaea living under anaerobic conditions employ different classes of Ni,Fe-containing carbon monoxide dehydrogenases to use CO as an energy source or to contribute in converting CO. to acetyl-CoA..The active site of carbon monoxide dehydrogenases contains a unique [NiFe.S.]-cluster, the on

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Mechanism of Ni,Fe-Containing Carbon Monoxide Dehydrogenases, CO and CO., in which it is supported by an electrophilic Fe ion placed in . to the heterocubane cluster..This review gives an overview on current ideas how Ni,Fe-containing carbon monoxide dehydrogenases reversibly oxidize CO to CO., with a focus on recent structural studies of the enzymes.

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Book 2019evelopment in these areas from the perspective of bioinorganic chemistry.?.Metallocofactors are essential for all forms of life and include a variety of metals, such as iron, molybdenum, vanadium, and nickel. Structurally fascinating metallocofactors featuring these metals are present in many bacter

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0081-5993 chanistic understanding of metallocofactors.Multi-authored vThis volume highlights recent progress on the fundamental chemistry and mechanistic understanding of metallocofactors, with an emphasis on the major development in these areas from the perspective of bioinorganic chemistry.?.Metallocofactor

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The Catalytic Mechanisms of the Molybdenum and Tungsten Enzymes,gen atom transferase redox chemistry, with the metal cycling between M(VI) and M(IV) formal oxidation states during the catalytic cycle. We discuss the range of reactions and what is known of mechanism for both oxo-transferase and non-oxo-transferase molybdenum and tungsten enzymes.

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Looking at Nitrogenase: Insights from Modern Structural Approaches,r atoms. The activity-based methods provide a framework for accessing non-resting states of the cofactor and introduce new questions surrounding the controlled binding and release of substrates. In the following, we discuss recent structural advances in the field and the novel directions for future activity-based research.

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Andrew M. Crawford,Julien J. H. Cotelesage,Roger C. Prince,Graham N. George