A bound reaction intermediate sheds light on the mechanism of nitrogenase
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Title
A bound reaction intermediate sheds light on the mechanism of nitrogenase
Authors
Keywords
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Journal
SCIENCE
Volume 359, Issue 6383, Pages 1484-1489
Publisher
American Association for the Advancement of Science (AAAS)
Online
2018-03-30
DOI
10.1126/science.aar2765
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- (2016) Dmitriy Lukoyanov et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement
- (2016) Thomas Spatzal et al. Nature Communications
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- (2015) J. B. Varley et al. PHYSICAL CHEMISTRY CHEMICAL PHYSICS
- Mechanism of Nitrogen Fixation by Nitrogenase: The Next Stage
- (2014) Brian M. Hoffman et al. CHEMICAL REVIEWS
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- (2014) Oliver Einsle JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
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- (2013) Brian M. Hoffman et al. ACCOUNTS OF CHEMICAL RESEARCH
- The global nitrogen cycle in the twenty-first century: introduction
- (2013) D. Fowler et al. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES
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- (2012) D. Lukoyanov et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Linking Crystallographic Model and Data Quality
- (2012) P. A. Karplus et al. SCIENCE
- REFMAC5 for the refinement of macromolecular crystal structures
- (2011) Garib N. Murshudov et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- 57Fe ENDOR Spectroscopy and ‘Electron Inventory’ Analysis of the Nitrogenase E4Intermediate Suggest the Metal-Ion Core of FeMo-Cofactor Cycles Through Only One Redox Couple
- (2011) Peter E. Doan et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- ENDOR/HYSCORE Studies of the Common Intermediate Trapped during Nitrogenase Reduction of N2H2, CH3N2H, and N2H4Support an Alternating Reaction Pathway for N2Reduction
- (2011) Dmitriy Lukoyanov et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
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- X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor
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- (2009) Lance C. Seefeldt et al. Annual Review of Biochemistry
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