A5048736279- Metalloenzymes and iron-sulfur proteins
- Electrocatalysts for Energy Conversion
- Photosynthetic Processes and Mechanisms
- Hydrogen Storage and Materials
- Electrochemical Analysis and Applications
- Metal-Catalyzed Oxygenation Mechanisms
- Catalysis for Biomass Conversion
- Advanced Chemical Physics Studies
- Biodiesel Production and Applications
- Microbial metabolism and enzyme function
- Microbial Metabolic Engineering and Bioproduction
- Protein Structure and Dynamics
- Mass Spectrometry Techniques and Applications
- Molecular Junctions and Nanostructures
- Catalytic Processes in Materials Science
- Algal biology and biofuel production
- Thermal and Kinetic Analysis
- Asymmetric Hydrogenation and Catalysis
- Advanced Electron Microscopy Techniques and Applications
- Nanocluster Synthesis and Applications
- Thermal Analysis in Power Transmission
- Heat Transfer and Boiling Studies
- Hemoglobin structure and function
- Inorganic and Organometallic Chemistry
- Malaria Research and Control
Lawrence Berkeley National Laboratory
2000-2020
Berkeley College
2018
Savitribai Phule Pune University
2011
University of Georgia
1987-2000
University of California, Davis
2000
University of California, Santa Cruz
2000
University of Delaware
2000
University of Wisconsin–Madison
2000
University of Nebraska–Lincoln
2000
University of Washington
2000
L-edge X-ray absorption spectroscopy has been used to study, under a variety of conditions, the electronic structure Ni in Ni−Fe hydrogenases from Desulfovibrio gigas, baculatus, and Pyrococcus furiosus. The status enzyme films for these measurements was monitored by FT-IR spectroscopy. spectra were interpreted ligand field multiplet simulations comparison with data model complexes. spectrum D. gigas "form A" is consistent covalent Ni(III) species. In contrast, all reduced samples exhibited...
The abbreviations used are: (NiFe) hydrogenase, hydrogenase containing nickel and non-heme iron; (NiFeSe) equivalent amounts of selenium plus GSH, glutathione; SDS, sodium dodecyl sulfate;
The heats of alcoholysis in isopropyl alcohol the d0 Ti or Zr compounds MR4(R = Me3SiCH2, Me3CCH2, PhCH2), M(NR′2)4(R′= Me Et), and MCl4(and some Hf analogues) have been measured, as well solution Pr1OH M(OPri)4, RH, R′2NH, HCl; from these subsidiary data standard formation thermochemical mean bond energy terms derived [M–X kcal mol–1: Ti–Cneopentyl,44; Ti–C,63; Ti–N, 81; Ti–O, 115; Zr–Cneopentyl, 54; Zr–C, 74; Zr–N, 90; Zr–O, 132; Hf–Cneopentyl, 58; Hf–N, 95; Hf–O, 137].
The periplasmic hydrogenase of Desulfovibrio vulgaris (Hildenbourough NCIB 8303) belongs to the category [Fe] which contains only iron-sulfur clusters as its prosthetic groups. Amino acid analyses were performed on purified D. hydrogenase. amino composition obtained compared very well with result derived from nucleotide sequence structural gene (Voordouw, G., Brenner, S. (1985) Eur. J. Biochem. 148, 515-520). Detailed EPR reductive titration studies characterize metal centers in this In...
Benzene dioxygenase from Pseudomonas putida comprises three components, namely a flavoprotein (NADH:ferredoxin oxidoreductase; Mr 81000), an intermediate electron-transfer protein, or ferredoxin (Mr 12000) with [2Fe-2S] cluster, and terminal containing two iron-sulphur clusters 215000), which requires additional Fe2+ atoms/molecule for oxygenase activity. The the give e.s.r. signals in reduced state rhombic symmetry average g values of 1.92 1.896 respectively. mid-point redox potentials were...
Using EPR spectroscopy to monitor the integrity of enzyme, conditions have been established which allow specific immunoprecipitation succinate dehydrogenase complex Escherichia coli. The enzyme precipitated from Lubrol PX-solubilized membranes by monospecific antiserum in presence a cocktail protease inhibitors contains four polypeptides apparent MrS 71,000, 26,000, 17,000, and 15,000. 71-kDa flavopeptide is readily susceptible proteolysis, shows unusual facile dissociation. Spectroscopic...
Conference Article| June 01 1985 Electron-spin-resonance/electron-paramagnetic-resonance spectroscopy of iron-sulphur enzymes RICHARD CAMMACK; CAMMACK *Department Plant Sciences, King's College, 68 Half Moon Lane, London SE24 9JF, U.K. Search for other works by this author on: This Site PubMed Google Scholar DAULAT S. PATIL; PATIL VICTOR M. FERNANDEZ †Instituto de Catalisis CSIC, Serrano 119, Madrid, Spain Biochem Soc Trans (1985) 13 (3): 572–578. https://doi.org/10.1042/bst0130572 Views...
The [NiFe] hydrogenase isolated from Desulfovibrio gigas was poised at different redox potentials and studied by Mossbauer spectroscopy. data firmly establish that this contains four prosthetic groups: one nickel center, [3Fe-xS], two [4Fe-4S] clusters. In the native enzyme, both [3Fe-xS] cluster are EPR-active. At low temperature (4.2 K), exhibits a paramagnetic spectrum typical for oxidized higher temperatures (greater than 20 collapses into quadrupole doublet with parameters magnitude of...
Carbon monoxide dehydrogenase from Clostridium thermoaceticum (Ct-CODH) is a nickel-containing enzyme that catalyzes acetyl-CoA synthesis and CO oxidation at two separate Ni sites, the A-cluster C-cluster, respectively. Rhodospirillum rubrum (Rr-CODH) contains only C-type cluster oxidation. We have used L-edge X-ray absorption spectroscopy to study electronic structure of these enzymes. The spectra indicate most in as-isolated Ct-CODH low-spin Ni(II). Upon treatment, fraction nickel...
Two electrophoretic forms of the large subunit soluble periplasmic [NiFe] hydrogenase from Desulfovibrio gigas have been detected by Western analysis. The faster moving form co‐migrates with purified, active enzyme. Amino acid sequence and composition C‐terminal tryptic peptide purified revealed that it is 15 amino acids shorter than predicted nucleotide sequence. Processing nascent occurs cleavage between His 536 Val 537 , residues which are highly conserved among hydrogenases. Mutagenesis...
According to L-edge sum rules, the number of 3d vacancies at a transition metal site is directly proportional integrated intensity X-ray absorption spectrum (XAS) for corresponding complex.
Low‐temperature electron spin resonance spectroscopy has been used to study the biophysical properties of succinate dehydrogenase from gram‐positive bacterium Micrococcus luteus . The paramagnetic redox centres enzyme were identified in a succinate‐dehydrogenase–antigen complex, which had purified with aid monospecific serum membranes solubilized Triton X‐100. characterized further detail using membrane‐bound and Triton‐solubilized forms enzyme. These studies distinguished two types...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTA reversible photoconversion between the carbon monoxide-induced axial 2.06 and rhombic 2.10 ESR signals of periplasmic hydrogenase from Desulfovibrio vulgarisDaulat S. Patil, . Huynh Boi Hanh, Shao H. He, Harry D. Peck, Daniel V. DerVartanian, Jean. LeGallCite this: J. Am. Chem. Soc. 1988, 110, 25, 8533–8534Publication Date (Print):December 1, 1988Publication History Published online1 May 2002Published inissue 1 December...
Succinate dehydrogenase was purified from the particulate fraction of Desulfobulbus . The enzyme catalysed both fumarate reduction and succinate oxidation but rate 8‐times less than that oxidation. Quantitative analysis showed presence 1 mol covalently bound flavin cytochrome b per dehydrogenase. contained three subunits with molecular mass 68.5, 27.5 22 kDa. EPR spectroscopy indicated at least two iron sulfur clusters. 2‐Heptyl‐4‐hydroxy‐quinoline‐ N ‐oxide inhibited electron‐transfer...