Book ChapterDOI
The Biochemistry of Molybdenum
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This article is published in Studies in Inorganic Chemistry.The article was published on 1994-01-01. It has received 3 citations till now. The article focuses on the topics: Molybdenum.read more
Citations
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Journal ArticleDOI
Authigenic molybdenum formation in marine sediments: A link to pore water sulfide in the Santa Barbara Basin
Yan Zheng,Yan Zheng,Yan Zheng,Robert F. Anderson,Robert F. Anderson,Alexander van Geen,James S. Kuwabara +6 more
TL;DR: Pore water and sediment Mo concentrations were measured in a suite of multicores collected at four sites along the northeastern flank of the Santa Barbara Basin to examine the connection between authigenic Mo formation and pore water sulfide concentration.
Journal ArticleDOI
Kupfer – ein “modernes” Bioelement
Wolfgang Kaim,Jochen Rall +1 more
TL;DR: In this paper, the authors describe the Funktionen von proteingebundenem Kupfer vor allem im Metabolismus von O2 and N/O-Verbindungen (NO2−, N2O) sowie seine haufige Assoziation with oxidierenden organischen and anorganischen Radikalen wie etwa Tyrosyl, Semichinonen, Superoxid-Ionen, Nitrosyls or NitroSyl-Radikalens.
Journal ArticleDOI
Crystal structure of the molybdate binding protein ModA.
TL;DR: The specificity exhibited by the molybdate binding protein ModA for molyBdate and tungstate reflects the size and ligands of the anion binding pocket.
References
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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 of the Nitrogenase Iron Protein from Azotobacter vinelandii
TL;DR: The crystal structure of the nitrogenase Fe-protein from Azotobacter vinelandii has been determined and it appears that interactions between the nucleotide and cluster sites must be indirectly coupled by allosteric changes occurring at the subunit interface.
Journal ArticleDOI
Metalloenzymes: the entatic nature of their active sites
Bert L. Vallee,R. J. P. Williams +1 more
Journal ArticleDOI
An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications
TL;DR: The structure of a recombinant human placenta aldose reductase is refined and it is revealed that the enzyme contains a parallel beta 8/alpha 8-barrel motif and establishes a new motif for NADP-binding oxidoreductases.