Research Topics
Species | Russ HilleSummaryAffiliation: The Ohio State University Country: USA Publications
| Collaborators
|
Detail Information
Publications
Substrate Orientation and Catalysis at the Molybdenum Site in Xanthine Oxidase: CRYSTAL STRUCTURES IN COMPLEX WITH XANTHINE AND LUMAZINEJames M Pauff
Department of Biochemistry, University of California, Riverside, California 92521 and the Medical Scientist Program, The Ohio State University, Columbus, Ohio 43210, USA
J Biol Chem 284:8760-7. 2009..The mechanistic implications as to how the ensemble of active site functional groups in the active site work to accelerate reaction rate are discussed...
Molybdenum-containing hydroxylasesRuss Hille
Department of Molecular and Cellular Biochemistry, The Ohio State University, 333 Hamilton Hall, 1645 Neil Avenue, Columbus, OH 43210, USA
Arch Biochem Biophys 433:107-16. 2005..The present minireview summarizes recent mechanistic and structure/function studies of members of this large and growing family of enzymes...- Resonance Raman studies of xanthine oxidase: The reduced enzyme-product complex with violapterinCraig Hemann
Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA
J Phys Chem B 109:3023-31. 2005..Given the numerous modes involving the bridging oxygen, a side-on binding mode can be eliminated... - Spectroscopic and kinetic studies of Y114F and W116F mutants of Me2SO reductase from Rhodobacter capsulatusNathan Cobb
Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA
J Biol Chem 282:35519-29. 2007..This "redox-cycled" mutant exhibits a Me(2)SO reducing activity and overall reaction mechanism similar to that of wild-type enzyme but rapidly reverts to the inactive five-coordinate form in the course of turnover... - The role of arginine 310 in catalysis and substrate specificity in xanthine dehydrogenase from Rhodobacter capsulatusJames M Pauff
Department of Molecular and Cellular Biochemistry, Ohio State University, Columbus, Ohio 43210, USA
J Biol Chem 282:12785-90. 2007.... - Spectroscopic and kinetic studies of Arabidopsis thaliana sulfite oxidase: nature of the redox-active orbital and electronic structure contributions to catalysisCraig Hemann
Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA
J Am Chem Soc 127:16567-77. 2005..Electron occupancy of this Mo=O(eq) pi* redox orbital upon interaction with substrates would effectively labilize the Mo=O(eq) bond, providing the dominant contribution to lowering the activation energy for oxygen atom transfer... - Mechanistic studies of Rhodobacter sphaeroides Me2SO reductaseNathan Cobb
Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, Ohio 43210-1218, USA
J Biol Chem 280:11007-17. 2005.... - Oxidative half-reaction of arabidopsis thaliana sulfite oxidase: generation of superoxide by a peroxisomal enzymeRobert S Byrne
Department of Molecular and Cellular Biochemistry, University of California, Riverside, California 92521, USA
J Biol Chem 284:35479-84. 2009..The physiological implications of plant sulfite oxidase as a copious generator of superoxide are discussed... - Studies on the mechanism of action of xanthine oxidaseEun-Young Choi
Department of Molecular and Cellular Biochemistry, The Ohio State University, 333 Hamilton Hall, 1645 Neil Avenue, Columbus, OH 43210-1218, USA
J Inorg Biochem 98:841-8. 2004..Preliminary experiments with two such mutants are entirely consistent with the proposed catalytic roles of two active site glutamate residues... - Molybdenum and tungsten in biologyRuss Hille
Dept of Molecular and Cellular Biochemistry and The Protein Research Group, The Ohio State University, Columbus, OH 43210 1218, USA
Trends Biochem Sci 27:360-7. 2002..Together, these studies provide an increasingly detailed view of the reaction mechanisms and the correlation between the electronic structure of the active site and catalytic function, one of the fundamental goals in metallobiochemistry... - Reduced nonprotein thiols inhibit activation and function of MMP-9: implications for chemopreventionPing Pei
Department of Oral Maxillofacial Surgery and Pathology, College of Dentistry, The Ohio State University, Columbus, OH 43210, USA
Free Radic Biol Med 41:1315-24. 2006..Collectively, these data demonstrate that nonprotein thiols suppress MMP-9 activation and function and introduce the prospect for their use in chemopreventive applications... - The interaction of trimethylamine dehydrogenase and electron-transferring flavoproteinWeiwei Shi
Department of Molecular and Cellular Biochemistry, Ohio State University, Columbus, Ohio 43210 1218, USA
J Biol Chem 280:20239-46. 2005.... - Oxo, sulfido, and tellurido Mo-enedithiolate models for xanthine oxidase: understanding the basis of enzyme reactivityPredrag Ilich
Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA
J Am Chem Soc 124:6796-7. 2002.... - The active site of arsenite oxidase from Alcaligenes faecalisThomas Conrads
Department of Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA
J Am Chem Soc 124:11276-7. 2002.... - Ser170 of Bacillus thuringiensis Cry1Ab delta-endotoxin becomes anchored in a hydrophobic moiety upon insertion of this protein into Manduca sexta brush border membranesOscar Alzate
Biochemistry Department, The Ohio State University, Columbus, OH 43210, USA
BMC Biochem 10:25. 2009.... - Crystal structure and stability studies of C77S HiPIP: a serine ligated [4Fe-4S] clusterSheref S Mansy
Evans Laboratory of Chemistry, Ohio State University, 100 West 18th Avenue, Columbus, Ohio 43210, USA
Biochemistry 41:1195-201. 2002..Ser ligation ultimately results in decreased cluster stability due to increased sensitivity to proton mediated degradation... - Characterization of superoxide production from aldehyde oxidase: an important source of oxidants in biological tissuesTapan Kumar Kundu
Center for Biomedical EPR Spectroscopy and Imaging, The Davis Heart and Lung Research Institute, Division of Cardiovascular Medicine, Department of Internal Medicine, Ohio State University College of Medicine, Columbus, OH 43210, USA
Arch Biochem Biophys 460:113-21. 2007..In view of the ubiquitous distribution of aldehydes in tissues, aldehyde oxidase can be an important basal source of superoxide that would be enhanced in disease settings where cellular aldehyde levels are increased... - Molybdenum enzymes containing the pyranopterin cofactor: an overviewRuss Hille
Department of Molecular and Cellular Biochemistry, Ohio State University, Columbus, OH 43210-1218, USA
Met Ions Biol Syst 39:187-226. 2002 - The reaction mechanism of xanthine oxidase: evidence for two-electron chemistry rather than sequential one-electron stepsAmy L Stockert
Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA
J Am Chem Soc 124:14554-5. 2002..Our results provide additional support to current evidence for the favored two-electron reduction mechanism... - Iron-sulfur cluster biosynthesis: characterization of Schizosaccharomyces pombe Isa1Gong Wu
Evans Laboratory of Chemistry, Ohio State University, 100 West 18th Avenue, Columbus, OH 43210, USA
J Biol Inorg Chem 7:526-32. 2002..Electronic supplementary material to this paper, containing Mössbauer and UV-visible spectra for mutant Isa1 proteins, can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00775-001-0330-2... - The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenaseSilke Leimkuhler
Department of Plant Biology, Technical University Braunschweig, 38023 Braunschweig, Germany
J Biol Chem 279:40437-44. 2004..This result is fully consistent with the proposed role of this residue as an active site base that initiates catalysis... - Substrate orientation in xanthine oxidase: crystal structure of enzyme in reaction with 2-hydroxy-6-methylpurineJames M Pauff
Department of Biochemistry, University of California, Riverside, California 92521, USA
J Biol Chem 283:4818-24. 2008.... - The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibitionKen Okamoto
Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo 113-8602, Japan
Proc Natl Acad Sci U S A 101:7931-6. 2004..A water molecule usually seen in the active site of the enzyme is absent in the present structure, which probably accounts for the stability of this intermediate toward ligand displacement by hydroxide... - Electrochemical studies of arsenite oxidase: an unusual example of a highly cooperative two-electron molybdenum centerKevin R Hoke
Inorganic Chemistry Laboratory, Oxford University, South Parks Road, Oxford OX1 3QR, England
Biochemistry 43:1667-74. 2004..0 and 20 degrees C, that of the [3Fe-4S] center is approximately 260 mV and that of the Rieske center is approximately 130 mV... - Structure of tetrahydrobiopterin tunes its electron transfer to the heme-dioxy intermediate in nitric oxide synthaseChin Chuan Wei
Department of Immunology, The Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA
Biochemistry 42:1969-77. 2003..4) Faster electron transfer from 5-methyl-H(4)B may be due to increased radical stability afforded by the N-5 methyl group... - Structures of the Mo(V) forms of sulfite oxidase from Arabidopsis thaliana by pulsed EPR spectroscopyAndrei V Astashkin
Department of Chemistry, University of Arizona, 1306 East University Boulevard, Tucson, Arizona 85721 0041, USA
Biochemistry 44:13274-81. 2005..At high pH, the active site is in the "open form", and water can readily exchange into the site to generate the hpH SO... - Nature of the catalytically labile oxygen at the active site of xanthine oxidaseChristian J Doonan
Department of Geological Sciences, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E2, Canada
J Am Chem Soc 127:4518-22. 2005..These results support a mechanism initiated by base-assisted nucleophilic attack of the substrate by Mo-OH... - Plants have SOX: the structure of sulfite oxidase from Arabidopsis thalianaRuss Hille
Structure 11:1189-90. 2003 - Direct demonstration of the presence of coordinated sulfate in the reaction pathway of Arabidopsis thaliana sulfite oxidase using 33S labeling and ESEEM spectroscopyAndrei V Astashkin
Department of Chemistry, University of Arizona, Tucson, Arizona 85721 0041, USA
J Am Chem Soc 129:14800-10. 2007..The isotropic hfi constant of 33S determined in these experiments was about 3 MHz, which demonstrates the presence of coordinated sulfate in the sulfite-reduced low-pH form of the plant enzyme... - Catalytic reduction of a tetrahydrobiopterin radical within nitric-oxide synthaseChin Chuan Wei
Department of Pathobiology, The Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA
J Biol Chem 283:11734-42. 2008..These results, in light of existing NOS crystal structures, suggest a "through-heme" mechanism may operate for H(4)B radical reduction in NOS... - Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteinsRobielyn P Ilagan
Department of Pathobiology, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio 44195, USA
J Biol Chem 283:19603-15. 2008..We conclude that the set point and regulation of the FMN conformational equilibrium differ markedly in eNOSr and nNOSr and can explain the lower electron transfer activity of eNOSr... - Electron transfer within complex II. Succinate:ubiquinone oxidoreductase of Escherichia coliRobert F Anderson
Department of Chemistry, The University of Auckland, Auckland 1, New Zealand
J Biol Chem 280:33331-7. 2005.... - A tetrahydrobiopterin radical forms and then becomes reduced during Nomega-hydroxyarginine oxidation by nitric-oxide synthaseChin Chuan Wei
Department of Immunology, The Lerner Research Institute, Cleveland Clinic Foundation, 9500 Euclid Avenue, Cleveland, OH 44195, USA
J Biol Chem 278:46668-73. 2003..These redox roles are novel and expand our understanding of biopterin function in biology...