Titlebook: Biological Nitrogen Fixation for the 21st Century; Proceedings of the 1 C. Elmerich,A. Kondorosi,W. E. Newton Conference proceedings 1998 S

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Ossification

Fe Protein: MgATP Induced Conformational Change and Reduction to an all Ferrous Stateified three regions of the polypeptide, switch I, switch II and the highly conserved region that includes M156 and A157, as being important for this conformational change. An A157S Fe protein variant binds MgATP but is unable to undergo the conformational change and is inactive (N. Gavini, B.K. Burg

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使無效

debacle

The Fe-Only Nitrogenase from ,: 1. Catalytic and EPR-Spectroscopic Properties of the FeFe Proteinnase (Fe nitrogenase) from a . mutant strain (Δ., Δ.; provided by Prof. Dr. W. Klipp, Universit?t Bochum) has recently been developed (Schneider et al., 1994; Schneider et al., 1997). Based on this procedure, at Fe protein: FeFe protein molar ratios of approximately 40:1, the following, remarkably h

高腳酒杯

The Fe-Only Nitrogenase From ,: 2. The FeFe Protein Metal Centers Probed by EXAFS and M?ssbauer Specion procedure yielding highly active protein components (FeFe protein and Fe protein) has recently been established. The biochemical and EPR spectroscopic properties of this enzyme have been extensively studied (Schneider . this volume). We report here the first spectroscopic evidence for a high deg

GOAD

The Nitrogen Cycle Sustained by Prokaryotes: Reversing Dinitrogen Fixationion, nitrification, nitrate assimilation, ammonification, and denitrification (Fig. 1). A new reaction is now being studied by which nitrate is reduced to N. at the expense of oxidation of ammonia. The process has been termed . for .aerobic .onium oxidation (Mulder et al. 1995).