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7: Ferrodoxins, Hydrogenases, and Nitrogenases - Metal-Sulfide Proteins

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    Transition-metal/sulfide sites, especially those containing iron, are present in all forms of life and are found at the active centers of a wide variety of redox and catalytic proteins. These proteins include simple soluble electron-transfer agents (the ferredoxins), membrane-bound components of electron-transfer chains, and some of the most complex metalloenzymes, such as nitrogenase, hydrogenase, and xanthine oxidase. In this chapter we first review the chemistry of the Fe-S sites that occur in relatively simple rubredoxins and ferredoxins, and make note of the ubiquity of these sites in other metalloenzymes. We use these relatively simple systems to show the usefulness of spectroscopy and model-system studies for deducing bioinorganic structure and reactivity. We then direct our attention to the hydrogenase and nitrogenase enzyme systems, both of which use transition-metalsulfur clusters to activate and evolve molecular hydrogen.

    III. Report on the Nitrogenase Crystal Structure378-381

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    Contributors and Attributions

    • Edward I. Stiefel (Exxon Research and Engineering Company)
    • Graham N. George (Exxon Research and Engineering Company)

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