KOL | Britt HedmanStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, United States of America. Electronic address: ... |
KOL Resume for Britt Hedman
| Year | |
|---|---|
| 2022 | Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, United States of America. Electronic address: |
| 2021 | Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, California, 94025, United States |
| 2020 | Stanford University |
| 2019 | Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, 94025, USA |
| 2018 | Stanford Synchrotron Radiation Lightsource , SLAC National Accelerator Laboratory , Stanford University , California 94025 , USA . Email: ; Email: |
| 2017 | Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, 2575 Sand Hill Road, Menlo Park, CA 94025, USA. |
| 2016 | Stanford Synchrotron Radiation Lightsource, Stanford Linear Accelerator Center, Stanford University, Menlo Park, CA 94025 |
| 2015 | Stanford Synchrotron Radiation Lightsource, Stanford Linear Accelerator Center (SLAC) National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025; |
| 2014 | Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Menlo Park, California 94025, United States |
| 2013 | Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Stanford, CA 94309, USA |
| 2012 | Department of Chemistry, Stanford University, Stanford, CA 94305, USA Stanford Synchroton Radiation Lightsource, SLAC, Stanford University, Stanford, California 94309, United States |
| 2011 | Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Menlo Park, CA 94025, USA |
| 2010 | Radiation Lightsource, SLAC, Stanford University, Menlo Park, CA 94025, USA SLAC National Accelerator Laboratory. |
| 2009 | Department of Chemistry, Stanford University, Stanford, California 94305, Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Menlo Park, California 94025, and Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158 Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, 2575 Sand Hill Road, MS 69, Menlo Park, CA 94025-7015 |
| 2008 | Department of Chemistry, Stanford University, Stanford, California 94305, Stanford Synchrotron Radiation Laboratory, Stanford Linear Accelerator Center, Stanford University, Stanford, California 94309, and Department of Chemistry and Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana−Champaign, Urbana, Illinois 61801 Stanford Synchrotron Radiation Laboratory. |
| 2007 | Department of Chemistry, Stanford University, Stanford, California 94305-5080, Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900, and Stanford Synchrotron Radiation Laboratory, SLAC, Stanford University, 2575 Sand Hill Road, MS 69, Menlo Park, California 94025-7015 Stanford Synchrotron Radiation Laboratory, SLAC, Stanford University, United States |
| 2006 | Department of Chemistry, Stanford University, Stanford, California 94305, and Stanford Synchrotron Radiation Laboratory, SLAC, Stanford University, Stanford, California 94309 Stanford Synchrotron Radiation Laboratory, Stanford University, 2575 Sand Hill Road, MS 69, Menlo Park, CA 94025-7015 |
| 2005 | Department of Chemistry, Stanford University, Stanford, California 94305, Stanford Synchrotron Radiation Laboratory, SLAC, Menlo Park, California 94302, and Department of Chemistry, New York University, New York 10003 Stanford Synchrotron Radiation Laboratory, Stanford Linear Accelerator Center, Stanford University, CA 94309, USA. |
| 2004 | Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, Department of Chemistry, Stanford University, Stanford, California 94305, and Stanford Synchrotron Radiation Laboratory, SLAC, Stanford University, Stanford, California 94309 Stanford Synchrotron Radiation Laboratory, Stanford Linear Accelerator Center, Stanford University, Stanford, California 94305 |
Britt Hedman: Influence Statistics
| Concept | World rank |
|---|---|
| applicable standard hardware | #1 |
| ssrl smb xas | #1 |
| diffraction data acquisition | #1 |
| xas exafs | #1 |
| stream coolers | #1 |
| xas instrumentation | #1 |
| ln2 crystal coolers | #1 |
| crystal alignment beam | #1 |
| spear3 upgrade | #1 |
| crystal xas | #1 |
| canberra 30element detector | #1 |
| xas data collection | #1 |
| ssrl crystallography beamlines | #1 |
| wiggler station | #1 |
| xas edge | #1 |
| kappa goniometer | #1 |
| silica synchrotron rad | #2 |
| ascidian perophora | #2 |
| binding fe4s4 | #2 |
| metallopeptides hc4h2fe4s4ni | #2 |
| delocalization fe | #2 |
| homocitrate fe core | #2 |
| allferrous titaniumiii | #2 |
| techniques multielement arrays | #2 |
| lcysteine scans | #2 |
| cell sulfur | #2 |
| solution structure cuh2o52 | #2 |
| sulfurous products | #2 |
| 287 angstroms | #2 |
| finalstate type | #2 |
| fe4se4 cluster | #2 |
| nifh acid sequence | #2 |
| rigid protein scaffold | #2 |
| nitrogenase nmr | #2 |
| 252 fwhm width | #2 |
| lcluster facilitate investigations | #2 |
| vanadium−sulfate | #2 |
| 7 water molecules | #2 |
| identical sample preparation | #2 |
| molybdoenzymes dmso reductase | #2 |
| realistic operating conitions | #2 |
| order reset scheme | #2 |
| blood cell samples | #2 |
| fe8s9c precursor l‐cluster | #2 |
| watersulfur interaction | #2 |
| 92 fraction | #2 |
| copper−dioxygen isomers | #2 |
| wellresolved features | #2 |
| aryl ch activation | #2 |
| central thesis asymmetry | #2 |
Open the FULL List in Excel | |
Prominent publications by Britt Hedman
Low-temperature optical absorption, circular dichroism, magnetic circular dichroism, and sulfur K-edge X-ray absorption spectra have been measured for the green “blue” copper center (type 1) in Achromobacter cycloclastes nitrite reductase. Combined with density functional calculations, the results of these spectroscopies have been used to define the extremely “perturbed” electronic structure of this site relative to that of the prototypical “classic” site found in plastocyanin. ...
| Known for Nitrite Reductase | Electronic Structure | Spectroscopic Properties | Copper Site | Perturbed Blue |
Mo-nitrogenase catalyzes the reduction of dinitrogen to ammonia at the cofactor (i.e., FeMoco) site of its MoFe protein component. Biosynthesis of FeMoco involves NifEN, a scaffold protein that hosts the maturation of a precursor to a mature FeMoco before it is delivered to the target location in the MoFe protein. Previously, we have shown that the NifEN-bound precursor could be converted in vitro to a fully complemented "FeMoco" in the presence of 2 mM dithionite. However, such a ...
| Known for Femoco Maturation | Mofe Protein | Bound Precursor | Azotobacter Vinelandii | Models Molecular |
The electronic structure of the red copper site in nitrosocyanin is defined relative to that of the well understood blue copper site of plastocyanin by using low-temperature absorption, circular dichroism, magnetic circular dichroism, resonance Raman, EPR and X-ray absorption spectroscopies, combined with DFT calculations. These studies indicate that the principal electronic structure change in the red copper site is the sigma rather than the pi donor interaction of the cysteine sulfur ...
| Known for Copper Site | Electronic Structure | Density Functional | Resonance Raman | Circular Dichroism |
Molybdenum and tungsten oxotransferase and hydroxylase enzymes catalyze the generalized reaction X + H2O ↔ XO + 2H+ + 2e- involving substrate and product X/XO. All such enzymes contain one or two pterin dithiolene ligands bound to a molybdenum or tungsten atom in the enzyme cofactor. Recent investigations in these laboratories together with earlier work by others have afforded a set of 10 complexes, all structurally characterized by X-ray diffraction, that are relevant to the active ...
| Known for Dmso Reductase | Active Sites | Enzymes Molybdenum | Oxidation States | Substrate Product |
Laccase is a multicopper oxidase which contains four coppers, one type 1, one type 2, and a coupled binuclear type 3 pair, the type 2 and type 3 copper centers together forming a trinuclear copper cluster. The type 1 mercury derivative of laccase (T1Hg Lc) has the type 1 center substituted with a redox-inactive Hg2+ ion and an intact trinuclear copper cluster. Reaction of H2O2 with fully oxidized T1Hg Lc produces a peroxide adduct which has now been studied in detail. Peroxide is shown ...
| Known for Trinuclear Copper | Peroxide Adduct | Type 2 | Cluster Site | 3 Pair |
Nature of the Intermediate Formed in the Reduction of O2 to H2O at the Trinuclear Copper Cluster Active Site in Native Laccase
[ PUBLICATION ]
The multicopper oxidases contain at least four copper atoms and catalyze the four-electron reduction of O(2) to H(2)O at a trinuclear copper cluster. An intermediate, termed native intermediate, has been trapped by a rapid freeze-quench technique from Rhus vernicifera laccase when the fully reduced form reacts with dioxygen. This intermediate had been described as an oxygen-radical bound to the trinuclear copper cluster with one Cu site reduced. XAS, however, shows that all copper atoms ...
| Known for Trinuclear Copper Cluster | Copper Atoms | O2 Reduction | Resting Form | Native Intermediate |
Laccase is a multicopper oxidase which contains four coppers, one type 1, one type 2, and a coupled binuclear type 3 pair, the type 2 and type 3 copper centers together forming a trinuclear copper cluster. The type 1 mercury derivative of laccase (T1Hg Lc) has the type 1 center substituted with a redox inactive Hg2+ ion and an intact trinuclear copper cluster. Reaction of reduced T1Hg Lc with dioxygen produces an oxygen intermediate which has now been studied in detail. Isotope ratio ...
| Known for Multicopper Oxidases | Catalytic Mechanism | Dioxygen Water | Coppers Type | Circular Dichroism |
Hydrogen bonding (H-bonding) is generally thought to play an important role in tuning the electronic structure and reactivity of metal-sulfur sites in proteins. To develop a quantitative understanding of this effect, S K-edge X-ray absorption spectroscopy (XAS) has been employed to directly probe ligand-metal bond covalency, where it has been found that protein active sites are significantly less covalent than their related model complexes. Sulfur K-edge XAS data are reported here on a ...
| Known for Hydrogen Bonding | Dft Calculations | Electronic Structure | Model Complexes | Edge Xas |
X-ray absorption Fe−K edge data on ferrous and ferric model complexes have been studied to establish a detailed understanding of the 1s → 3d pre-edge feature and its sensitivity to the electronic structure of the iron site. The energy position and splitting, and intensity distribution, of the pre-edge feature were found to vary systematically with spin state, oxidation state, geometry, and bridging ligation (for binuclear complexes). A methodology for interpreting the energy splitting ...
| Known for Iron Complexes | 1s → | Multiplet Analysis | Edge Features | Excited States |
Superoxide reductase (SOR) is a non-heme iron enzyme that reduces superoxide to peroxide at a diffusion-controlled rate. Sulfur K-edge X-ray absorption spectroscopy (XAS) is used to investigate the ground-state electronic structure of the resting high-spin and CN- bound low-spin FeIII forms of the 1Fe SOR from Pyrococcus furiosus. A computational model with constrained imidazole rings (necessary for reproducing spin states), H-bonding interaction to the thiolate (necessary for ...
| Known for Superoxide Reductase | Cytochrome P450 | Absorption Spectroscopy | Axial Thiolate | Ground State |
Nitrogenase, the enzyme system responsible for biological nitrogen fixation, is believed to utilize two unique metalloclusters in catalysis. There is considerable interest in understanding how these metalloclusters are assembled in vivo. It has been presumed that immature iron-molybdenum cofactor-deficient nitrogenase MoFe proteins contain the P-cluster, although no biosynthetic pathway for the assembly of this complex cluster has been identified as yet. Through the comparison by iron ...
| Known for Mofe Protein | Ray Absorption | Azotobacter Vinelandii | Molybdenum Cofactor | Unique Metalloclusters |
Continual advancements in the development of synchrotron radiation sources have resulted in X-ray based spectroscopic techniques capable of probing the electronic and structural properties of numerous systems. This review gives an overview of the application of metal K-edge and L-edge X-ray absorption spectroscopy (XAS), as well as K resonant inelastic X-ray scattering (RIXS), to the study of electronic structure in transition metal sites with emphasis on experimentally quantifying 3d ...
| Known for Metal Sites | Ray Absorption | Orbital Covalency | Resonant Inelastic | Ledge Xas |
Spectroscopy and Kinetics of Wild-Type and Mutant Tyrosine Hydroxylase: Mechanistic Insight into O2 Activation
[ PUBLICATION ]
Tyrosine hydroxylase (TH) is a pterin-dependent nonheme iron enzyme that catalyzes the hydroxylation of L-tyr to L-DOPA in the rate-limiting step of catecholamine neurotransmitter biosynthesis. We have previously shown that the Fe(II) site in phenylalanine hydroxylase (PAH) converts from six-coordinate (6C) to five-coordinate (5C) only when both substrate + cofactor are bound. However, steady-state kinetics indicate that TH has a different co-substrate binding sequence (pterin + O(2) + ...
| Known for Tyrosine Hydroxylase | O2 Activation | Feii Site | Kinetics Models | Circular Dichroism |
The low spin ferric and low and high spin ferrous forms of myoglobin, bacterial cytochrome P-450-CAM, and chloroperoxidase have been examined by Fe-K x-ray absorption edge spectroscopy. The positions of the absorption edge and the shapes of preedge and edge regions of imidazole adducts of ferric P-450-CAM and chloroperoxidase are essentially the same when compared with thiolate-ligated ferric myoglobin. As these three protein derivatives all have six-coordinate, low spin, ferric hemes ...
| Known for Ray Absorption | Ferric Myoglobin | Proximal Ligand | Cytochrome P450cam | Ferrous State |
Sulfur K-Edge XAS and DFT Calculations on Nitrile Hydratase: Geometric and Electronic Structure of the Non-heme Iron Active Site
[ PUBLICATION ]
The geometric and electronic structure of the active site of the non-heme iron enzyme nitrile hydratase (NHase) is studied using sulfur K-edge XAS and DFT calculations. Using thiolate (RS(-))-, sulfenate (RSO(-))-, and sulfinate (RSO(2)(-))-ligated model complexes to provide benchmark spectral parameters, the results show that the S K-edge XAS is sensitive to the oxidation state of S-containing ligands and that the spectrum of the RSO(-) species changes upon protonation as the S-O bond ...
| Known for Dft Calculations | Active Site | Nitrile Hydratase | Electronic Structure | Chemical Models |
Key People For Electronic Structure
Britt Hedman:Expert Impact
Concepts for whichBritt Hedmanhas direct influence:Electronic structure, Ray absorption, Dft calculations, Active site, Oxo transfer, Absorption spectroscopy, Edge xas.
Britt Hedman:KOL impact
Concepts related to the work of other authors for whichfor which Britt Hedman has influence:Electronic structure, Active site, Ray absorption, Electron transfer, Nitric oxide, Dft calculations, Oxidation state.
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