X-Ray Absorption Spectroscopic Evidence For A Unique Nickel Site In Clostridium-Thermoaceticum Carbon-Monoxide Dehydrogenase

INORGANIC CHEMISTRY(1987)

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ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTX-ray absorption spectroscopic evidence for a unique nickel site in Clostridium thermoaceticum carbon monoxide dehydrogenaseStephen P. Cramer, Marly K. Eidsness, W. H. Pan, Thomas A. Morton, Steve W. Ragsdale, Daniel V. DerVartanian, Lars G. Ljungdahl, and Robert A. ScottCite this: Inorg. Chem. 1987, 26, 15, 2477–2479Publication Date (Print):July 1, 1987Publication History Published online1 May 2002Published inissue 1 July 1987https://doi.org/10.1021/ic00262a027RIGHTS & PERMISSIONSArticle Views169Altmetric-Citations69LEARN 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 PDF (439 KB) Get e-AlertsSupporting Info (1)»Supporting Information Supporting Information Get e-Alerts
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nickel,x ray spectroscopy,bacteria,electron paramagnetic resonance,molecular structure,spectroscopy,chemical reaction,microorganisms,enzyme,chemical reactions,extended x ray absorption fine structure,oxidation,spectrum,carbon compounds,carbon monoxide,proteins,enzymes
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