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Mechanism of Molybdenum Nitrogenase

Barbara K. Burgess and,David J. Lowe

Nitrogenase

Citation

Library science

1996

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMechanism of Molybdenum NitrogenaseBarbara K. Burgess and David J. LoweView Author Information Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92717-3900, and Nitrogen Fixation Laboratory, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, U.K. Cite this: Chem. Rev. 1996, 96, 7, 2983–3012Publication Date (Web):November 7, 1996Publication History Received28 March 1996Revised15 August 1996Published online7 November 1996Published inissue 1 January 1996https://doi.org/10.1021/cr950055xCopyright © 1996 American Chemical SocietyRIGHTS & PERMISSIONSArticle Views13116Altmetric-Citations1481LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit Read OnlinePDF (861 KB) Get e-AlertsSUBJECTS:Cluster chemistry,FeMo cofactor,Metal organic frameworks,Peptides and proteins,Redox reactions Get e-Alerts

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“Mechanism of Molybdenum Nitrogenase” is a paper by Barbara K. Burgess and David J. Lowe published in 1996. It has an Open Access status of “closed”. You can read and download a PDF Full Text of this paper here.