J
Jongsun Kim
Researcher at California Institute of Technology
Publications - 10
Citations - 2350
Jongsun Kim is an academic researcher from California Institute of Technology. The author has contributed to research in topics: Azotobacter vinelandii & Nitrogenase. The author has an hindex of 7, co-authored 10 publications receiving 2237 citations.
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Journal ArticleDOI
Structural models for the metal centers in the nitrogenase molybdenum-iron protein
Jongsun Kim,Douglas C. Rees +1 more
TL;DR: Neither the FeMo-cofactor nor the P-clusters are exposed to the surface, suggesting that substrate entry, electron transfer, and product release must involve a carefully regulated sequence of interactions between the MoFe-protein and Fe-protein of nitrogenase.
Journal ArticleDOI
Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from azotobacter vinelandii.
Jongsun Kim,Douglas C. Rees +1 more
TL;DR: The crystal structure of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii has been determined and structural similarities are apparent between nitrogenase and other electron transfer systems, including hydrogenases and the photosynthetic reaction centre.
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The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures.
TL;DR: Findings indicate that a cavity exists in the interior of the FeMo-cofactor that could be involved in substrate binding and suggest that redox reactions at the P-cluster pair may be linked to transitions of two cluster-bound sulfurs between disulfide and sulfide oxidation states.
Journal ArticleDOI
Nitrogenase and biological nitrogen fixation.
Jongsun Kim,Douglas C. Rees +1 more
TL;DR: General features of the nitrogenase system, including conformational coupling of nucleotide hydrolysis, aspects of the cluster structures, and the general spatial organization of redox centers within the protein subunits, are relevant to a wide range of biochemical systems.
Journal ArticleDOI
X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution.
TL;DR: The crystal structure of the nitrogenase molybdenum-iron (MoFe) protein from Clostridium pasteurianum (Cp1) has been determined at 3.0-A resolution by a combination of isomorphous replacement, molecular replacement, and noncrystallographic symmetry averaging.