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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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發(fā)表于 2025-3-21 19:30:56 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
期刊全稱Biological Nitrogen Fixation for the 21st Century
期刊簡(jiǎn)稱Proceedings of the 1
影響因子2023C. Elmerich,A. Kondorosi,W. E. Newton
視頻videohttp://file.papertrans.cn/188/187425/187425.mp4
學(xué)科分類Current Plant Science and Biotechnology in Agriculture
圖書封面Titlebook: Biological Nitrogen Fixation for the 21st Century; Proceedings of the 1 C. Elmerich,A. Kondorosi,W. E. Newton Conference proceedings 1998 S
影響因子Nitrogen availability is one of the most critical factors that limits plant productivity. The largest reservoir of nitrogen is the atmosphere, but this gaseous molecular nitrogen only becomes available to plants through the biological nitrogen fixation process, which only prokaryotic cells have developed. The discovery that microbes were providing fixed nitrogen to legumes and the isolation of the first nitrogen-fixing bacteria occured at the end the 19th Century, in Louis Pasteur‘s time. We are now building on more than 100 years of research in this field and looking towards the 21st Century. The International Nitrogen Fixation Congress series Started more than 20 years ago. The format of this Congress is designed to gather scientists from very diverse origins, backgrounds, interests and scientific approaches and is a forum where fundamental knowledge is discussed alongside applied research. This confluence of perspectives is, we believe, extremely beneficial in raising new ideas, questions and concepts.
Pindex Conference proceedings 1998
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Een gemengde kleur aan de voeten,ajor success stories in the last five years have included the solution of the structures of the Fe protein (Georgiadis et al, 1992) and MoFe protein (Kim, Rees, 1992; Bolin et al, 1993; Peters et al., 1997). However, the three-dimensional structures of the MoFe protein have given rise to a major con
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Der neoinstitutionalistische Ansatz,olybdenum iron (MoFe-) protein. During substrate reduction, the two proteins associate to form a transient complex where electron transfer from the Fe-protein to the MoFe-protein is coupled to MgATP hydrolysis. Ultimately, electrons and protons are transferred to substrates bound to the active metal
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Der neoinstitutionalistische Ansatz,ere on this cluster, and by implication the corresponding clusters in the alternative V- and Fe-nitrogenases (Eady, 1991) are substrates bound and reduced? This review discusses this question in the light of the reactions of isolated FeMoco and of metal complexes, cluster or otherwise, which give im
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https://doi.org/10.1007/978-3-662-62195-0wn nitrogenases. No other Mo, V or Fe-containing enzyme is known to employ FeMo-co or its analogs and all known nitrogenases contain one of these cofactors. FeMo-co (MoFe.S.homocitrate) is found at the active site of the .-encoded, molybdenum nitrogenase, and its structure (Fig 1) was determined as
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