Richard H. Holm
Harvard University
580 Papers
13.5K Citations
Richard H. Holm is an academic researcher from Harvard University. The author has contributed to research in topics: Cubane & Chemistry. The author has an hindex of 87, co-authored 580 publications. Previous affiliations of Richard H. Holm include University of New Mexico & Stanford University.
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Papers
Fluorine-19 chemical shifts as structural probes of metal-sulfur clusters and the cofactor of nitrogenase
TL;DR: It was concluded that the essential Fe Mo-co cluster structure remains intact and a Fe atom is the probable thiolate binding site and the inclusion of a 19F NMR label in FeMo-co should prove of utility in further investigation of cofactor properties and reactions.
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Molecular Assemblies Containing Unsupported [Fe(III)-(m(2):eta(2)-RCO(2))-Cu(II)] Bridges.
TL;DR: An examination of Fe-Cu-carboxylate interactions is initiated by the synthesis of the first examples of [Fe(III)-(&mgr;(2):eta(2)-RCO(2))-Cu(II)] bridges.
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Reactions of site-differentiated [Fe4S4]2+, 1+ clusters with sulfonium cations: reactivity analogues of biotin synthase and other members of the S-adenosylmethionine enzyme family.
TL;DR: It is demonstrated that site-differentiated clusters sustain a high percentage of reductive cleavage, a necessary result in the context of biotin synthase activity preceding an investigation of the mode of binding of sulfonium substrates and inhibitors at the unique iron site.
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Sulfur K-Edge X-ray Absorption Spectroscopy and Density Functional Theory Calculations on Monooxo MoIV and Bisoxo MoVI Bis-dithiolenes: Insights into the Mechanism of Oxo Transfer in Sulfite Oxidase and Its Relation to the Mechanism of DMSO Reductase
TL;DR: Compared with previously studied dimethyl sulfoxide reductase (DMSOr) models, the presence of only one dithiolene at the enzyme active site selectively activates the equatorial oxo for transfer, and allows facile structural reorganization during turnover.