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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https://doi.org/10.1007/978-3-642-61404-0 (MoFe protein) is not clear and the mechanism of charge separation following electron transfer against the potential from Av2 (Fe protein) to Av1 is unknown. One of the most promising ways of gaining this information appears to be photoreduction of nitrogenase over a microsecond range. An alternati

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https://doi.org/10.1007/978-3-642-61404-0e site for substrate reduction of nitrogenase (Hoover et al, 1989; Kim, Rees, 1992). The products of at least six nitrogen fixation (.) genes, including ., ., ., ., . and ., are required for the biosynthesis of FeMo-co. It has been suggested that NifNE protein might serve as a scaffold for FeMo-co b

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Luftfeuchtigkeit und Wasserverdunstung,ry of its subsequent reduction remain unresolved. One reason for this is that only reduced states of the enzyme react with substrates and these can only be generated as mixtures of transient species. Another is the lack of an effective spectroscopic probe of the dinitrogen . and its chemistry subseq

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https://doi.org/10.1007/978-3-662-56778-4(lo-CO; . = 2.09, 1.97, 1.93) at low pressure (0.08 atm) and the other (hi-CO; . = 2.06, 2.06, 2.17) at high pressure (0.5 atm). Using .C and .Fe Q-band ENDOR spectroscopy with . nitrogenase, we recently showed (Pollock et al, 1995; Christie et al, 1996) that these signals arise from CO bound to the

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https://doi.org/10.1007/978-3-7091-4502-9nase (Fe nitrogenase) from a . mutant strain (Δ., Δ.; provided by Prof. Dr. W. Klipp, Universität 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

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Nachhaltige Unternehmensorganisationion 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

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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).

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