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. 1997 Oct 17;272(42):26627-33.
doi: 10.1074/jbc.272.42.26627.

N2 fixation by Streptomyces thermoautotrophicus involves a molybdenum-dinitrogenase and a manganese-superoxide oxidoreductase that couple N2 reduction to the oxidation of superoxide produced from O2 by a molybdenum-CO dehydrogenase

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N2 fixation by Streptomyces thermoautotrophicus involves a molybdenum-dinitrogenase and a manganese-superoxide oxidoreductase that couple N2 reduction to the oxidation of superoxide produced from O2 by a molybdenum-CO dehydrogenase

M Ribbe et al. J Biol Chem. .
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Abstract

N2 fixation by Streptomyces thermoautotrophicus follows the equation N2 + 4-12MgATP + 8H+ + 8e- --> 2NH3 + H2 + 4-12MgADP + 4-12Pi and exhibits features which are not obvious in the diazotrophic bacteria studied so far. The reaction is coupled to the oxidation of carbon monoxide (CO) by a molybdenum-containing CO dehydrogenase that transfers the electrons derived from CO oxidation to O2, thereby producing superoxide anion radicals (O-2). A manganese-containing superoxide oxidoreductase reoxidizes the O-2 anions to O2 and transfers the electrons to a MoFeS-dinitrogenase for the reduction of N2 to ammonium. Among the most striking properties of the S. thermoautotrophicus nitrogenase system are the dependence on O2 and O-2, the complete insensitivity of all components involved toward O2 and H2O2, the inability to reduce ethine or ethene, and a low MgATP requirement. In addition, the subunit structure of the S. thermoautotrophicus nitrogenase components and the polypeptides involved seem to be dissimilar from the known nitrogenases.

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