59 results match your criteria: "Massachusetts Institute of Technology 77 Massachusetts Avenue[Affiliation]"
A Short Copper-Copper Distance in a (µ-1,2-Peroxo)dicopper(II) Complex Having a 1,8-Naphthyridine Unit as an Additional Bridge This work was supported by grants from the National Science Foundation and the National Institutes of Health. We thank A. M. Barrios for help in acquiring resonance Raman spectra. X-ray absorption spectroscopic data were measured at SSRL. SSRL is funded by the Department of Energy, Office of Basic Energy Science. The SSRL Structural Molecular Biology Program is supported by the National Institute of Health, National Center for Research Resources, Biomedical Technology Program, and by the Department of Energy, Office of Biological and Environmental Research.
Angew Chem Int Ed Engl
April 2001
Department of Chemistry, Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge, MA 02139 (USA).
A Short Copper-Copper Distance in a (μ-1,2-Peroxo)dicopper(II) Complex Having a 1,8-Naphthyridine Unit as an Additional Bridge.
Angew Chem Int Ed Engl
April 2001
Department of Chemistry, Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge, MA 02139 (USA) Fax: (+1) 617-258-8150.
A copper-copper separation of about 2.84 Å is determined by extended X-ray absorption fine structure studies for the (μ-1,2-peroxo)dicopper(II) species 1, which has only a 1,8-naphthyridine unit as an additional bridge. Complex 1 was prepared by the reaction of O with a dicopper(I) complex formed from BPMAN.
View Article and Find Full Text PDFAdsorption-Mediated Electrochemical Sensing of Halides We gratefully acknowledge financial support from the Office of Naval Research through their Young Investigator Program. We thank D. Kong for various helpful discussions and the Austrian Science Fund for an Erwin Schrödinger Fellowship to R.M.
Angew Chem Int Ed Engl
March 2001
Department of Chemical Engineering Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge, MA 02139 (USA).
Adsorption-Mediated Electrochemical Sensing of Halides.
Angew Chem Int Ed Engl
March 2001
Department of Chemical Engineering Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge, MA 02139 (USA) Fax: (+1) 617-258-5042.
A new strategy for detecting halides is presented that employs gold electrodes plated to expose a monolayer of silver atoms. Cl , Br , and I ions each adsorb onto this surface and stochastically produce electrochemical changes (see picture; upd=underpotentially deposited) in the stripping characteristic of the silver layer that reflect the identity and surface coverage of these halides. The latter provides measurements that relate to the solution concentrations of the halides.
View Article and Find Full Text PDFUranium Hexakisamido Complexes This work was supported by the National Science Foundation (CAREER Award CHE-9501992), the Alfred P. Sloan Foundation, the National Science Board (1998 Alan T. Waterman award to C.C.C.), and the Packard Foundation. K.M. thanks the Deutsche Forschungsgemeinschaft for a postdoctoral fellowship.
Angew Chem Int Ed Engl
September 2000
Department of Chemistry, Room 2-227 Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge, MA 02139-4307 (USA).
Metal-Based NO Sensing by Selective Ligand Dissociation This work was supported by a grant from the National Science Foundation and a fellowship to N.S. from the Undergraduate Research Opportunity Program (MIT). We thank Prof. Roger Tsien for valuable discussions at the inception of this project.
Angew Chem Int Ed Engl
June 2000
Department of Chemistry Massachusetts Institute of Technology 77 Massachusetts Avenue Cambridge, MA 02139 (USA).
Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function.
Proc Natl Acad Sci U S A
March 1999
Departments of Biology and Chemistry, Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
The disulfide bond between Cys-110 and Cys-187 in the intradiscal domain is required for correct folding in vivo and function of mammalian rhodopsin. Misfolding in rhodopsin, characterized by the loss of ability to bind 11-cis-retinal, has been shown to be caused by an intradiscal disulfide bond different from the above native disulfide bond. Further, naturally occurring single mutations of the intradiscal cysteines (C110F, C110Y, and C187Y) are associated with retinitis pigmentosa (RP).
View Article and Find Full Text PDFStructure and function in rhodopsin: kinetic studies of retinal binding to purified opsin mutants in defined phospholipid-detergent mixtures serve as probes of the retinal binding pocket.
Proc Natl Acad Sci U S A
March 1999
Departments of Biology and Chemistry, Massachusetts Institute of Technology 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
In the current standard procedure for preparation of mammalian rhodopsin mutants, transfected COS-1 cells expressing the mutant opsin genes are treated with 5 microM 11-cis-retinal before detergent solubilization for purification. We found that binding of 11-cis-retinal to opsin mutants with single amino acid changes at Trp-265 (W265F,Y,A) and a retinitis pigmentosa mutant (A164V) was far from complete and required much higher concentrations of 11-cis-retinal. By isolation of the expressed opsins in a stable form, kinetic studies of retinal binding to the opsins in vitro have been carried out by using defined phospholipid-detergent mixtures.
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