| Year |
Citation |
Score |
| 2024 |
Hille R. Molybdenum-containing CO dehydrogenase and formate dehydrogenases. Methods in Enzymology. 708: 257-274. PMID 39572142 DOI: 10.1016/bs.mie.2024.10.014 |
0.335 |
|
| 2024 |
Niks D, Hakopian S, Canchola A, Lin YH, Hille R. Mechanism of Action of Formate Dehydrogenases. Journal of the American Chemical Society. PMID 39382156 DOI: 10.1021/jacs.4c07376 |
0.395 |
|
| 2024 |
Nguyen D, Vigil W, Niks D, Hille R. The Rapid-reaction Kinetics of an Electron-Bifurcating Flavoprotein, the crotonyl-CoA-dependent NADH:ferredoxin oxidoreductase EtfAB:bcd. The Journal of Biological Chemistry. 107745. PMID 39236874 DOI: 10.1016/j.jbc.2024.107745 |
0.346 |
|
| 2023 |
Ortiz S, Niks D, Wiley S, Lubner CE, Hille R. Rapid-reaction kinetics of the bifurcating NAD-dependent NADPH:ferredoxin oxidoreductase NfnI from Pyrococcus furiosus. The Journal of Biological Chemistry. 299: 105403. PMID 38229399 DOI: 10.1016/j.jbc.2023.105403 |
0.324 |
|
| 2023 |
Ge X, Schut GJ, Tran J, Poole Ii FL, Niks D, Menjivar K, Hille R, Adams MWW. Characterization of the Membrane-Associated Electron-Bifurcating Flavoenzyme EtfABCX from the Hyperthermophilic Bacterium . Biochemistry. PMID 38061393 DOI: 10.1021/acs.biochem.3c00473 |
0.34 |
|
| 2023 |
Murray DT, Ge X, Schut GJ, Rosenberg DJ, Hammel M, Bierma JC, Hille R, Adams MWW, Hura GL. Correlating Conformational Equilibria with Catalysis in the Electron Bifurcating EtfABCX of . Biochemistry. PMID 38013433 DOI: 10.1021/acs.biochem.3c00472 |
0.325 |
|
| 2023 |
Harmer JR, Hakopian S, Niks D, Hille R, Bernhardt PV. Redox Characterization of the Complex Molybdenum Enzyme Formate Dehydrogenase from . Journal of the American Chemical Society. 145: 25850-25863. PMID 37967365 DOI: 10.1021/jacs.3c10199 |
0.394 |
|
| 2023 |
Kalimuthu P, Hakopian S, Niks D, Hille R, Bernhardt PV. The Reversible Electrochemical Interconversion of Formate and CO by Formate Dehydrogenase from . The Journal of Physical Chemistry. B. 127: 8382-8392. PMID 37728992 DOI: 10.1021/acs.jpcb.3c04652 |
0.384 |
|
| 2023 |
Vigil W, Nguyen D, Niks D, Hille R. Rapid-reaction kinetics of the butyryl-CoA dehydrogenase component of the electron-bifurcating crotonyl-CoA-dependent NADH:ferredoxin oxidoreductase from Megasphaera elsdenii. The Journal of Biological Chemistry. 104853. PMID 37220854 DOI: 10.1016/j.jbc.2023.104853 |
0.376 |
|
| 2022 |
Kusano T, Nishino T, Okamoto K, Hille R, Nishino T. The mechanism and significance of the conversion of xanthine dehydrogenase to xanthine oxidase in mammalian secretory gland cells. Redox Biology. 59: 102573. PMID 36525890 DOI: 10.1016/j.redox.2022.102573 |
0.301 |
|
| 2022 |
Kirk ML, Hille R. Spectroscopic Studies of Mononuclear Molybdenum Enzyme Centers. Molecules (Basel, Switzerland). 27. PMID 35956757 DOI: 10.3390/molecules27154802 |
0.317 |
|
| 2022 |
Hille R, Niks D. Application of EPR and related methods to molybdenum-containing enzymes. Methods in Enzymology. 666: 373-412. PMID 35465925 DOI: 10.1016/bs.mie.2022.02.006 |
0.371 |
|
| 2022 |
Hakopian S, Niks D, Hille R. The air-inactivation of formate dehydrogenase FdsDABG from Cupriavidus necator. Journal of Inorganic Biochemistry. 231: 111788. PMID 35313132 DOI: 10.1016/j.jinorgbio.2022.111788 |
0.375 |
|
| 2021 |
Vigil W, Niks D, Franz-Badur S, Chowdhury N, Buckel W, Hille R. Spectral deconvolution of redox species in the crotonyl-CoA-dependent NADH:ferredoxin oxidoreductase from Megasphaera elsdenii. A flavin-dependent bifurcating enzyme. Archives of Biochemistry and Biophysics. 108793. PMID 33587905 DOI: 10.1016/j.abb.2021.108793 |
0.307 |
|
| 2020 |
Young T, Niks D, Hakopian S, Tam TK, Yu X, Hille R, Blaha GM. Crystallographic and kinetic analyses of the FdsBG subcomplex of the cytosolic formate dehydrogenase FdsABG from Cupriavidus necator. The Journal of Biological Chemistry. PMID 32249211 DOI: 10.1074/Jbc.Ra120.013264 |
0.417 |
|
| 2020 |
Blaha G, Young T, Niks D, Hakopian S, Tam TK, Yu X, Hille R. The cytosolic formate dehydrogenase FdsABG from Cupriavidus necator . Crystal structure of the FdsBG fragment which is responsible for the oxidative half‐reaction. The Faseb Journal. 34: 1-1. DOI: 10.1096/Fasebj.2020.34.S1.09333 |
0.305 |
|
| 2019 |
Kalimuthu P, Petitgenet M, Niks D, Dingwall S, Harmer JR, Hille R, Bernhardt PV. The oxidation-reduction and electrocatalytic properties of CO dehydrogenase from Oligotropha carboxidovorans. Biochimica Et Biophysica Acta. Bioenergetics. 148118. PMID 31734195 DOI: 10.1016/J.Bbabio.2019.148118 |
0.481 |
|
| 2019 |
Walker LM, Li B, Niks D, Hille R, Elliott SJ. Deconvolution of reduction potentials of formate dehydrogenase from Cupriavidus necator. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 31463592 DOI: 10.1007/S00775-019-01701-1 |
0.486 |
|
| 2019 |
Bender D, Kaczmarek AT, Niks D, Hille R, Schwarz G. Mechanism of nitrite-dependent NO synthesis by human sulfite oxidase. The Biochemical Journal. PMID 31167903 DOI: 10.1042/Bcj20190143 |
0.496 |
|
| 2019 |
Yu X, Niks D, Ge X, Liu H, Hille R, Mulchandani A. Synthesis of Formate from CO Gas Catalyzed by an O-tolerant NAD-Dependent Formate Dehydrogenase and Glucose Dehydrogenase. Biochemistry. PMID 30839197 DOI: 10.1021/Acs.Biochem.8B01301 |
0.453 |
|
| 2019 |
Niks D, Hille R. Molybdenum-Containing Enzymes. Methods in Molecular Biology (Clifton, N.J.). 1876: 55-63. PMID 30317474 DOI: 10.1007/978-1-4939-8864-8_4 |
0.422 |
|
| 2018 |
Niks D, Hille R. Reductive activation of CO by formate dehydrogenases. Methods in Enzymology. 613: 277-295. PMID 30509470 DOI: 10.1016/Bs.Mie.2018.10.013 |
0.415 |
|
| 2018 |
Niks D, Hille R. Molybdenum- and tungsten-containing formate dehydrogenases and formylmethanofuran dehydrogenases: structure, mechanism and cofactor insertion. Protein Science : a Publication of the Protein Society. PMID 30120799 DOI: 10.1002/Pro.3498 |
0.407 |
|
| 2018 |
Peters JW, Beratan DN, Bothner B, Dyer RB, Harwood CS, Heiden ZM, Hille R, Jones AK, King PW, Lu Y, Lubner CE, Minteer SD, Mulder DW, Raugei S, Schut GJ, et al. A new era for electron bifurcation. Current Opinion in Chemical Biology. 47: 32-38. PMID 30077080 DOI: 10.1016/J.Cbpa.2018.07.026 |
0.416 |
|
| 2018 |
Pacheco J, Niks D, Hille R. Kinetic and spectroscopic characterization of tungsten-substituted DMSO reductase from Rhodobacter sphaeroides. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 29299674 DOI: 10.1007/S00775-017-1531-7 |
0.476 |
|
| 2017 |
Watson C, Niks D, Hille R, Vieira M, Schoepp-Cothenet B, Marques AT, Romão MJ, Santos-Silva T, Santini JM. Electron transfer through arsenite oxidase: Insights into Rieske interaction with cytochrome c. Biochimica Et Biophysica Acta. PMID 28801050 DOI: 10.1016/J.Bbabio.2017.08.003 |
0.472 |
|
| 2017 |
Yu X, Niks D, Mulchandani A, Hille R. Efficient reduction of CO2 by the molybdenum-containing formate dehydrogenase from Cupriavidus necator (Ralstonia eutropha). The Journal of Biological Chemistry. PMID 28784661 DOI: 10.1074/Jbc.M117.785576 |
0.46 |
|
| 2016 |
Dingwall S, Wilcoxen J, Niks D, Hille R. Studies of carbon monoxide dehydrogenase from Oligotropha carboxidovorans Journal of Molecular Catalysis B: Enzymatic. 134: 317-322. DOI: 10.1016/J.Molcatb.2016.10.007 |
0.8 |
|
| 2015 |
Niks D, Duvvuru J, Escalona M, Hille R. Spectroscopic and Kinetic Properties of the Molybdenum-Containing, NAD+-Dependent Formate Dehydrogenase from Ralstonia eutropha. The Journal of Biological Chemistry. PMID 26553877 DOI: 10.1074/Jbc.M115.688457 |
0.512 |
|
| 2015 |
Wang J, Krizowski S, Fischer-Schrader K, Niks D, Tejero J, Sparacino-Watkins C, Wang L, Ragireddy V, Frizzell S, Kelley EE, Zhang Y, Basu P, Hille R, Schwarz G, Gladwin MT. Sulfite Oxidase Catalyzes Single-Electron Transfer at Molybdenum Domain to Reduce Nitrite to Nitric Oxide. Antioxidants & Redox Signaling. 23: 283-94. PMID 25314640 DOI: 10.1089/ars.2013.5397 |
0.462 |
|
| 2015 |
Hille R, Dingwall S, Wilcoxen J. The aerobic CO dehydrogenase from Oligotropha carboxidovorans. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 20: 243-51. PMID 25156151 DOI: 10.1007/S00775-014-1188-4 |
0.766 |
|
| 2014 |
Hall J, Reschke S, Cao H, Leimkühler S, Hille R. The reductive half-reaction of xanthine dehydrogenase from Rhodobacter capsulatus: the role of Glu232 in catalysis. The Journal of Biological Chemistry. 289: 32121-30. PMID 25258317 DOI: 10.1074/Jbc.M114.603456 |
0.617 |
|
| 2014 |
Lee MC, Velayutham M, Komatsu T, Hille R, Zweier JL. Measurement and characterization of superoxide generation from xanthine dehydrogenase: a redox-regulated pathway of radical generation in ischemic tissues. Biochemistry. 53: 6615-23. PMID 25243829 DOI: 10.1021/Bi500582R |
0.367 |
|
| 2014 |
Cao H, Pauff JM, Hille R. X-ray crystal structure of a xanthine oxidase complex with the flavonoid inhibitor quercetin. Journal of Natural Products. 77: 1693-9. PMID 25060641 DOI: 10.1021/Np500320G |
0.358 |
|
| 2014 |
Anderson RF, Shinde SS, Hille R, Rothery RA, Weiner JH, Rajagukguk S, Maklashina E, Cecchini G. Electron-transfer pathways in the heme and quinone-binding domain of complex II (succinate dehydrogenase). Biochemistry. 53: 1637-46. PMID 24559074 DOI: 10.1021/Bi401630M |
0.431 |
|
| 2014 |
Hille R, Hall J, Basu P. The mononuclear molybdenum enzymes. Chemical Reviews. 114: 3963-4038. PMID 24467397 DOI: 10.1021/Cr400443Z |
0.592 |
|
| 2014 |
Cao H, Hall J, Hille R. Substrate orientation and specificity in xanthine oxidase: crystal structures of the enzyme in complex with indole-3-acetaldehyde and guanine. Biochemistry. 53: 533-41. PMID 24397336 DOI: 10.1021/Bi401465U |
0.603 |
|
| 2014 |
Schwarz G, Krizowski S, Wang J, Niks D, Sparacino-Watkins C, Hille R, Gladwin M. Intramolecular electron transfer controls nitrite reduction in molybdenum-containing sulfite oxidase Nitric Oxide. 42: 113. DOI: 10.1016/J.Niox.2014.09.045 |
0.355 |
|
| 2013 |
Wilcoxen J, Hille R. The hydrogenase activity of the molybdenum/copper-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans. The Journal of Biological Chemistry. 288: 36052-60. PMID 24165123 DOI: 10.1074/Jbc.M113.522441 |
0.785 |
|
| 2013 |
Reschke S, Niks D, Wilson H, Sigfridsson KG, Haumann M, Rajagopalan KV, Hille R, Leimkühler S. Effect of exchange of the cysteine molybdenum ligand with selenocysteine on the structure and function of the active site in human sulfite oxidase. Biochemistry. 52: 8295-303. PMID 24147957 DOI: 10.1021/Bi4008512 |
0.441 |
|
| 2013 |
Shanmugam M, Wilcoxen J, Habel-Rodriguez D, Cutsail GE, Kirk ML, Hoffman BM, Hille R. (13)C and (63,65)Cu ENDOR studies of CO dehydrogenase from Oligotropha carboxidovorans. Experimental evidence in support of a copper-carbonyl intermediate. Journal of the American Chemical Society. 135: 17775-82. PMID 24147852 DOI: 10.1021/Ja406136F |
0.755 |
|
| 2013 |
Pushie MJ, Cotelesage JJ, Lyashenko G, Hille R, George GN. X-ray absorption spectroscopy of a quantitatively Mo(V) dimethyl sulfoxide reductase species. Inorganic Chemistry. 52: 2830-7. PMID 23445435 DOI: 10.1021/Ic301660E |
0.4 |
|
| 2013 |
Hille R. The molybdenum oxotransferases and related enzymes. Dalton Transactions (Cambridge, England : 2003). 42: 3029-42. PMID 23318732 DOI: 10.1039/C2Dt32376A |
0.489 |
|
| 2013 |
Wang J, Krizowski S, Fischer K, Niks D, Tejero J, Wang L, Sparacino-Watkins C, Ragireddy P, Frizzell S, Kelley EE, Shiva S, Zhang Y, Basu P, Hille R, Schwarz G, et al. P62 Nitric Oxide. 31: S39-S40. DOI: 10.1016/J.Niox.2013.02.064 |
0.474 |
|
| 2013 |
Hille R. The molybdenum hydroxylases: Xanthine oxidase and related enzymes Molybdenum: Its Biological and Coordination Chemistry and Industrial Applications. 271-300. |
0.301 |
|
| 2012 |
Lambeck IC, Fischer-Schrader K, Niks D, Roeper J, Chi JC, Hille R, Schwarz G. Molecular mechanism of 14-3-3 protein-mediated inhibition of plant nitrate reductase. The Journal of Biological Chemistry. 287: 4562-71. PMID 22170050 DOI: 10.1074/Jbc.M111.323113 |
0.454 |
|
| 2011 |
Wilcoxen J, Snider S, Hille R. Substitution of silver for copper in the binuclear Mo/Cu center of carbon monoxide dehydrogenase from Oligotropha carboxidovorans. Journal of the American Chemical Society. 133: 12934-6. PMID 21774528 DOI: 10.1021/Ja205073J |
0.78 |
|
| 2011 |
Cao H, Hall J, Hille R. X-ray crystal structure of arsenite-inhibited xanthine oxidase: μ-sulfido,μ-oxo double bridge between molybdenum and arsenic in the active site. Journal of the American Chemical Society. 133: 12414-7. PMID 21761899 DOI: 10.1021/Ja2050265 |
0.577 |
|
| 2011 |
Mtei RP, Lyashenko G, Stein B, Rubie N, Hille R, Kirk ML. Spectroscopic and electronic structure studies of a dimethyl sulfoxide reductase catalytic intermediate: implications for electron- and atom-transfer reactivity. Journal of the American Chemical Society. 133: 9762-74. PMID 21648481 DOI: 10.1021/Ja109178Q |
0.411 |
|
| 2011 |
Hille R, Nishino T, Bittner F. Molybdenum enzymes in higher organisms. Coordination Chemistry Reviews. 255: 1179-1205. PMID 21516203 DOI: 10.1016/J.Ccr.2010.11.034 |
0.424 |
|
| 2011 |
Wilcoxen J, Zhang B, Hille R. Reaction of the molybdenum- and copper-containing carbon monoxide dehydrogenase from Oligotropha carboxydovorans with quinones. Biochemistry. 50: 1910-6. PMID 21275368 DOI: 10.1021/Bi1017182 |
0.769 |
|
| 2011 |
Havelius KG, Reschke S, Horn S, Döring A, Niks D, Hille R, Schulzke C, Leimkühler S, Haumann M. Structure of the molybdenum site in YedY, a sulfite oxidase homologue from Escherichia coli. Inorganic Chemistry. 50: 741-8. PMID 21190337 DOI: 10.1021/Ic101291J |
0.422 |
|
| 2011 |
Service RJ, Yano J, McConnell I, Hwang HJ, Niks D, Hille R, Wydrzynski T, Burnap RL, Hillier W, Debus RJ. Participation of glutamate-354 of the CP43 polypeptide in the ligation of manganese and the binding of substrate water in photosystem II. Biochemistry. 50: 63-81. PMID 21114287 DOI: 10.1021/Bi1015937 |
0.36 |
|
| 2011 |
Tejero J, Biswas A, Haque MM, Wang ZQ, Hemann C, Varnado CL, Novince Z, Hille R, Goodwin DC, Stuehr DJ. Mesohaem substitution reveals how haem electronic properties can influence the kinetic and catalytic parameters of neuronal NO synthase. The Biochemical Journal. 433: 163-74. PMID 20950274 DOI: 10.1042/Bj20101353 |
0.473 |
|
| 2010 |
Wahl B, Reichmann D, Niks D, Krompholz N, Havemeyer A, Clement B, Messerschmidt T, Rothkegel M, Biester H, Hille R, Mendel RR, Bittner F. Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes. The Journal of Biological Chemistry. 285: 37847-59. PMID 20861021 DOI: 10.1074/Jbc.M110.169532 |
0.418 |
|
| 2010 |
Shanmugam M, Zhang B, McNaughton RL, Kinney RA, Hille R, Hoffman BM. The structure of formaldehyde-inhibited xanthine oxidase determined by 35 GHz 2H ENDOR spectroscopy. Journal of the American Chemical Society. 132: 14015-7. PMID 20860357 DOI: 10.1021/Ja106432H |
0.344 |
|
| 2010 |
Cao H, Pauff JM, Hille R. Substrate orientation and catalytic specificity in the action of xanthine oxidase: the sequential hydroxylation of hypoxanthine to uric acid. The Journal of Biological Chemistry. 285: 28044-53. PMID 20615869 DOI: 10.1074/Jbc.M110.128561 |
0.437 |
|
| 2010 |
Duval S, Santini JM, Nitschke W, Hille R, Schoepp-Cothenet B. The small subunit AroB of arsenite oxidase: lessons on the [2Fe-2S] Rieske protein superfamily. The Journal of Biological Chemistry. 285: 20442-51. PMID 20421651 DOI: 10.1074/Jbc.M110.113811 |
0.321 |
|
| 2010 |
Zhang B, Hemann CF, Hille R. Kinetic and spectroscopic studies of the molybdenum-copper CO dehydrogenase from Oligotropha carboxidovorans. The Journal of Biological Chemistry. 285: 12571-8. PMID 20178978 DOI: 10.1074/Jbc.M109.076851 |
0.504 |
|
| 2010 |
Cecchini G, Maklashina E, Shinde SS, Anderson RF, Hille R. Electron transfer activity through the quinone-binding site of complex II (succinate: Quinone reductase) Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1797: 111. DOI: 10.1016/J.Bbabio.2010.04.334 |
0.376 |
|
| 2009 |
Hille R. The reaction mechanism of the molybdenum hydroxylase xanthine oxidoreductase: evidence against the formation of intermediates having metal-carbon bonds. Metal Ions in Life Sciences. 6: 395-416. PMID 20877801 DOI: 10.1039/9781847559333-00395 |
0.427 |
|
| 2009 |
Byrne RS, Hänsch R, Mendel RR, Hille R. Oxidative half-reaction of arabidopsis thaliana sulfite oxidase: generation of superoxide by a peroxisomal enzyme. The Journal of Biological Chemistry. 284: 35479-84. PMID 19875441 DOI: 10.1074/Jbc.M109.067355 |
0.524 |
|
| 2009 |
Spiegelhauer O, Dickert F, Mende S, Niks D, Hille R, Ullmann M, Dobbek H. Kinetic characterization of xenobiotic reductase A from Pseudomonas putida 86. Biochemistry. 48: 11412-20. PMID 19839648 DOI: 10.1021/Bi901370U |
0.51 |
|
| 2009 |
Wagener N, Pierik AJ, Ibdah A, Hille R, Dobbek H. The Mo-Se active site of nicotinate dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. 106: 11055-60. PMID 19549881 DOI: 10.1073/Pnas.0902210106 |
0.376 |
|
| 2009 |
Pauff JM, Hille R. Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin. Journal of Natural Products. 72: 725-31. PMID 19388706 DOI: 10.1021/Np8007123 |
0.392 |
|
| 2009 |
Pauff JM, Cao H, Hille R. Substrate Orientation and Catalysis at the Molybdenum Site in Xanthine Oxidase: CRYSTAL STRUCTURES IN COMPLEX WITH XANTHINE AND LUMAZINE. The Journal of Biological Chemistry. 284: 8760-7. PMID 19109252 DOI: 10.1074/Jbc.M804517200 |
0.464 |
|
| 2008 |
Ilagan RP, Tiso M, Konas DW, Hemann C, Durra D, Hille R, Stuehr DJ. Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins. The Journal of Biological Chemistry. 283: 19603-15. PMID 18487202 DOI: 10.1074/Jbc.M802914200 |
0.478 |
|
| 2008 |
Wei CC, Wang ZQ, Tejero J, Yang YP, Hemann C, Hille R, Stuehr DJ. Catalytic reduction of a tetrahydrobiopterin radical within nitric-oxide synthase. The Journal of Biological Chemistry. 283: 11734-42. PMID 18283102 DOI: 10.1074/Jbc.M709250200 |
0.405 |
|
| 2008 |
Pauff JM, Zhang J, Bell CE, Hille R. Substrate orientation in xanthine oxidase: crystal structure of enzyme in reaction with 2-hydroxy-6-methylpurine. The Journal of Biological Chemistry. 283: 4818-24. PMID 18063585 DOI: 10.1074/Jbc.M707918200 |
0.496 |
|
| 2007 |
Astashkin AV, Johnson-Winters K, Klein EL, Byrne RS, Hille R, Raitsimring AM, Enemark JH. Direct demonstration of the presence of coordinated sulfate in the reaction pathway of Arabidopsis thaliana sulfite oxidase using 33S labeling and ESEEM spectroscopy. Journal of the American Chemical Society. 129: 14800-10. PMID 17983221 DOI: 10.1021/Ja0704885 |
0.39 |
|
| 2007 |
Cobb N, Hemann C, Polsinelli GA, Ridge JP, McEwan AG, Hille R. Spectroscopic and kinetic studies of Y114F and W116F mutants of Me2SO reductase from Rhodobacter capsulatus. The Journal of Biological Chemistry. 282: 35519-29. PMID 17921142 DOI: 10.1074/Jbc.M704458200 |
0.488 |
|
| 2007 |
Kundu TK, Hille R, Velayutham M, Zweier JL. Characterization of superoxide production from aldehyde oxidase: an important source of oxidants in biological tissues. Archives of Biochemistry and Biophysics. 460: 113-21. PMID 17353002 DOI: 10.1016/J.Abb.2006.12.032 |
0.387 |
|
| 2007 |
Pauff JM, Hemann CF, Jünemann N, Leimkühler S, Hille R. The role of arginine 310 in catalysis and substrate specificity in xanthine dehydrogenase from Rhodobacter capsulatus. The Journal of Biological Chemistry. 282: 12785-90. PMID 17327224 DOI: 10.1074/Jbc.M700364200 |
0.485 |
|
| 2006 |
Hille R. Structure and function of xanthine oxidoreductase European Journal of Inorganic Chemistry. 1913-1926. DOI: 10.1002/Ejic.200600087 |
0.44 |
|
| 2005 |
Hemann C, Ilich P, Stockert AL, Choi EY, Hille R. Resonance Raman studies of xanthine oxidase: The reduced enzyme-product complex with violapterin. The Journal of Physical Chemistry. B. 109: 3023-31. PMID 16851316 DOI: 10.1021/Jp046636K |
0.783 |
|
| 2005 |
Hemann C, Hood BL, Fulton M, Hänsch R, Schwarz G, Mendel RR, Kirk ML, Hille R. Spectroscopic and kinetic studies of Arabidopsis thaliana sulfite oxidase: nature of the redox-active orbital and electronic structure contributions to catalysis. Journal of the American Chemical Society. 127: 16567-77. PMID 16305246 DOI: 10.1021/Ja0530873 |
0.697 |
|
| 2005 |
Stuehr DJ, Wei CC, Wang Z, Hille R. Exploring the redox reactions between heme and tetrahydrobiopterin in the nitric oxide synthases. Dalton Transactions (Cambridge, England : 2003). 3427-35. PMID 16234921 DOI: 10.1039/B506355H |
0.422 |
|
| 2005 |
Astashkin AV, Hood BL, Feng C, Hille R, Mendel RR, Raitsimring AM, Enemark JH. Structures of the Mo(V) forms of sulfite oxidase from Arabidopsis thaliana by pulsed EPR spectroscopy. Biochemistry. 44: 13274-81. PMID 16201753 DOI: 10.1021/Bi051220Y |
0.643 |
|
| 2005 |
Anderson RF, Hille R, Shinde SS, Cecchini G. Electron transfer within complex II. Succinate:ubiquinone oxidoreductase of Escherichia coli. The Journal of Biological Chemistry. 280: 33331-7. PMID 16085649 DOI: 10.1074/Jbc.M506002200 |
0.4 |
|
| 2005 |
Doonan CJ, Stockert A, Hille R, George GN. Nature of the catalytically labile oxygen at the active site of xanthine oxidase. Journal of the American Chemical Society. 127: 4518-22. PMID 15783235 DOI: 10.1021/Ja042500O |
0.783 |
|
| 2005 |
Shi W, Mersfelder J, Hille R. The interaction of trimethylamine dehydrogenase and electron-transferring flavoprotein. The Journal of Biological Chemistry. 280: 20239-46. PMID 15760891 DOI: 10.1074/Jbc.M500582200 |
0.752 |
|
| 2005 |
Cobb N, Conrads T, Hille R. Mechanistic studies of Rhodobacter sphaeroides Me2SO reductase. The Journal of Biological Chemistry. 280: 11007-17. PMID 15649898 DOI: 10.1074/Jbc.M412050200 |
0.533 |
|
| 2005 |
Wei CC, Wang ZQ, Durra D, Hemann C, Hille R, Garcin ED, Getzoff ED, Stuehr DJ. The three nitric-oxide synthases differ in their kinetics of tetrahydrobiopterin radical formation, heme-dioxy reduction, and arginine hydroxylation. The Journal of Biological Chemistry. 280: 8929-35. PMID 15632185 DOI: 10.1074/Jbc.M409737200 |
0.455 |
|
| 2005 |
Hille R. Molybdenum-containing hydroxylases. Archives of Biochemistry and Biophysics. 433: 107-16. PMID 15581570 DOI: 10.1016/J.Abb.2004.08.012 |
0.396 |
|
| 2004 |
Leimkühler S, Stockert AL, Igarashi K, Nishino T, Hille R. The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenase. The Journal of Biological Chemistry. 279: 40437-44. PMID 15265866 DOI: 10.1074/Jbc.M405778200 |
0.789 |
|
| 2004 |
Okamoto K, Matsumoto K, Hille R, Eger BT, Pai EF, Nishino T. The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition. Proceedings of the National Academy of Sciences of the United States of America. 101: 7931-6. PMID 15148401 DOI: 10.1073/Pnas.0400973101 |
0.476 |
|
| 2004 |
Choi EY, Stockert AL, Leimkühler S, Hille R. Studies on the mechanism of action of xanthine oxidase. Journal of Inorganic Biochemistry. 98: 841-8. PMID 15134930 DOI: 10.1016/J.Jinorgbio.2003.11.010 |
0.823 |
|
| 2004 |
Hoke KR, Cobb N, Armstrong FA, Hille R. Electrochemical studies of arsenite oxidase: an unusual example of a highly cooperative two-electron molybdenum center. Biochemistry. 43: 1667-74. PMID 14769044 DOI: 10.1021/Bi0357154 |
0.49 |
|
| 2004 |
Okamoto K, Matsumoto K, Yamaguchi Y, Matsumura T, Hille R, Eger B, Pai EF, Nishino T. 3SC54 Intermediate structure and hydroxylation mechanism of xanthine oxidoreductase Seibutsu Butsuri. 44: S28. DOI: 10.2142/Biophys.44.S28_4 |
0.301 |
|
| 2003 |
Lu X, Nikolic D, Mitchell DJ, van Breemen RB, Mersfelder JA, Hille R, Silverman RB. A mechanism for substrate-Induced formation of 6-hydroxyflavin mononucleotide catalyzed by C30A trimethylamine dehydrogenase. Bioorganic & Medicinal Chemistry Letters. 13: 4129-32. PMID 14592522 DOI: 10.1016/J.Bmcl.2003.07.032 |
0.733 |
|
| 2003 |
Wei CC, Wang ZQ, Hemann C, Hille R, Stuehr DJ. A tetrahydrobiopterin radical forms and then becomes reduced during Nomega-hydroxyarginine oxidation by nitric-oxide synthase. The Journal of Biological Chemistry. 278: 46668-73. PMID 14504282 DOI: 10.1074/Jbc.M307682200 |
0.488 |
|
| 2003 |
Wei CC, Wang ZQ, Arvai AS, Hemann C, Hille R, Getzoff ED, Stuehr DJ. Structure of tetrahydrobiopterin tunes its electron transfer to the heme-dioxy intermediate in nitric oxide synthase. Biochemistry. 42: 1969-77. PMID 12590583 DOI: 10.1021/Bi026898H |
0.38 |
|
| 2003 |
Hille R. The reaction mechanism of xanthine oxidase Journal of Inorganic Biochemistry. 96: 52. DOI: 10.1016/S0162-0134(03)80492-0 |
0.339 |
|
| 2002 |
Stockert AL, Shinde SS, Anderson RF, Hille R. The reaction mechanism of xanthine oxidase: evidence for two-electron chemistry rather than sequential one-electron steps. Journal of the American Chemical Society. 124: 14554-5. PMID 12465963 DOI: 10.1021/Ja027388D |
0.801 |
|
| 2002 |
Conrads T, Hemann C, George GN, Pickering IJ, Prince RC, Hille R. The active site of arsenite oxidase from Alcaligenes faecalis. Journal of the American Chemical Society. 124: 11276-7. PMID 12236735 DOI: 10.1021/Ja027684Q |
0.498 |
|
| 2002 |
Hille R. Molybdenum and tungsten in biology. Trends in Biochemical Sciences. 27: 360-7. PMID 12114025 DOI: 10.1016/S0968-0004(02)02107-2 |
0.415 |
|
| 2002 |
Ilich P, Hille R. Oxo, sulfido, and tellurido Mo-enedithiolate models for xanthine oxidase: understanding the basis of enzyme reactivity. Journal of the American Chemical Society. 124: 6796-7. PMID 12059179 DOI: 10.1021/Ja011957K |
0.51 |
|
| 2002 |
Wu G, Mansy SS, Hemann C, Hille R, Surerus KK, Cowan JA. Iron-sulfur cluster biosynthesis: characterization of Schizosaccharomyces pombe Isa1. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 7: 526-32. PMID 11941510 DOI: 10.1007/S00775-001-0330-2 |
0.301 |
|
| 2002 |
Hille R. Molybdenum enzymes containing the pyranopterin cofactor: an overview. Metal Ions in Biological Systems. 39: 187-226. PMID 11913126 |
0.341 |
|
| 2002 |
Wang J, Gosztola D, Ruffle SV, Hemann C, Seibert M, Wasielewski MR, Hille R, Gustafson TL, Sayre RT. Functional asymmetry of photosystem II D1 and D2 peripheral chlorophyll mutants of Chlamydomonas reinhardtii. Proceedings of the National Academy of Sciences of the United States of America. 99: 4091-6. PMID 11904453 DOI: 10.1073/Pnas.062056899 |
0.568 |
|
| 2001 |
Wang ZQ, Wei CC, Ghosh S, Meade AL, Hemann C, Hille R, Stuehr DJ. A conserved tryptophan in nitric oxide synthase regulates heme-dioxy reduction by tetrahydrobiopterin. Biochemistry. 40: 12819-25. PMID 11669618 DOI: 10.1021/Bi011182S |
0.372 |
|
| 2001 |
Yoon KS, Bobst C, Hemann CF, Hille R, Tabita FR. Spectroscopic and functional properties of novel 2[4Fe-4S] cluster-containing ferredoxins from the green sulfur bacterium Chlorobium tepidum. The Journal of Biological Chemistry. 276: 44027-36. PMID 11568186 DOI: 10.1074/Jbc.M107852200 |
0.371 |
|
| 2001 |
Manikandan P, Choi EY, Hille R, Hoffman BM. 35 GHz ENDOR characterization of the "very rapid" signal of xanthine oxidase reacted with 2-hydroxy-6-methylpurine (13C8): evidence against direct Mo-C8 interaction. Journal of the American Chemical Society. 123: 2658-63. PMID 11456936 DOI: 10.1021/Ja003894W |
0.557 |
|
| 2001 |
Mitchell DJ, Nikolic D, Jang MH, van Breemen RB, Hille R, Silverman RB. Inactivation of C30A trimethylamine dehydrogenase by N-cyclopropyl-alpha-methylbenzylamine, 1-phenylcyclopropylamine, and phenylhydrazine. Biochemistry. 40: 8523-30. PMID 11456490 DOI: 10.1021/Bi0105126 |
0.354 |
|
| 2001 |
Hille R, Anderson RF. Coupled electron/proton transfer in complex flavoproteins: Solvent kinetic isotope effect studies of electron transfer in xanthine oxidase and trimethylamine dehydrogenase Journal of Biological Chemistry. 276: 31193-31201. PMID 11395485 DOI: 10.1074/jbc.M100673200 |
0.339 |
|
| 2001 |
Ellis PJ, Conrads T, Hille R, Kuhn P. Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 Å and 2.03 Å Structure. 9: 125-132. PMID 11250197 DOI: 10.1016/S0969-2126(01)00566-4 |
0.357 |
|
| 2001 |
Hille R. Molybdenum enzymes. Sub-Cellular Biochemistry. 35: 445-85. PMID 11192730 DOI: 10.1007/0-306-46828-x_13 |
0.325 |
|
| 2001 |
Wei CC, Wang ZQ, Wang Q, Meade AL, Hemann C, Hille R, Stuehr DJ. Rapid kinetic studies link tetrahydrobiopterin radical formation to heme-dioxy reduction and arginine hydroxylation in inducible nitric-oxide synthase Journal of Biological Chemistry. 276: 315-319. PMID 11020389 DOI: 10.1074/Jbc.M008441200 |
0.342 |
|
| 2000 |
Anderson RF, Jang MH, Hille R. Radiolytic studies of trimethylamine dehydrogenase. Spectral deconvolution of the neutral and anionic flavin semiquinone, and determination of rate constants for electron transfer in the one-electron reduced enzyme Journal of Biological Chemistry. 275: 30781-30786. PMID 10859304 DOI: 10.1074/jbc.M001256200 |
0.431 |
|
| 2000 |
Jang MH, Scrutton NS, Hille R. Formation of W3A1 electron-transferring flavoprotein (ETF) hydroquinone in the trimethylamine dehydrogenase-ETF protein complex Journal of Biological Chemistry. 275: 12546-12552. PMID 10777543 DOI: 10.1074/jbc.275.17.12546 |
0.314 |
|
| 1999 |
Jones RM, Inscore FE, Hille R, Kirk ML. Freeze-Quench Magnetic Circular Dichroism Spectroscopic Study of the "Very Rapid" Intermediate in Xanthine Oxidase. Inorganic Chemistry. 38: 4963-4970. PMID 11671238 DOI: 10.1021/Ic990154J |
0.503 |
|
| 1999 |
Roberts P, Basran J, Wilson EK, Hille R, Scrutton NS. Redox cycles in trimethylamine dehydrogenase and mechanism of substrate inhibition Biochemistry. 38: 14927-14940. PMID 10555975 DOI: 10.1021/Bi9914098 |
0.467 |
|
| 1999 |
Yoon KS, Hille R, Hemann C, Tabita FR. Rubredoxin from the green sulfur bacterium Chlorobium tepidum functions as an electron acceptor for pyruvate ferredoxin oxidoreductase. The Journal of Biological Chemistry. 274: 29772-8. PMID 10514453 DOI: 10.1074/Jbc.274.42.29772 |
0.456 |
|
| 1999 |
Basran J, Sutcliffe MJ, Hille R, Scrutton NS. Reductive half-reaction of the H172Q mutant of trimethylamine dehydrogenase: Evidence against a carbanion mechanism and assignment of kinetically influential ionizations in the enzyme-substrate complex Biochemical Journal. 341: 307-314. PMID 10393087 DOI: 10.1042/0264-6021:3410307 |
0.472 |
|
| 1999 |
Brody MS, Hille R. The kinetic behavior of chicken liver sulfite oxidase Biochemistry. 38: 6668-6677. PMID 10350486 DOI: 10.1021/Bi9902539 |
0.405 |
|
| 1999 |
Basran J, Jang MH, Sutcliffe MJ, Hille R, Scrutton NS. The role of Tyr-169 of trimethylamine dehydrogenase in substrate oxidation and magnetic interaction between FMN cofactor and the 4Fe/4S center Journal of Biological Chemistry. 274: 13155-13161. PMID 10224070 DOI: 10.1074/jbc.274.19.13155 |
0.382 |
|
| 1999 |
Jang MH, Basran J, Scrutton NS, Hille R. The reaction of trimethylamine dehydrogenase with trimethylamine Journal of Biological Chemistry. 274: 13147-13154. PMID 10224069 DOI: 10.1074/Jbc.274.19.13147 |
0.492 |
|
| 1999 |
Scrutton NS, Basran J, Wilson EK, Chohan KK, Jang MH, Sutcliffe MJ, Hille R. Electron transfer in trimethylamine dehydrogenase and electron-transferring flavoprotein Biochemical Society Transactions. 27: 196-201. PMID 10093733 DOI: 10.1042/Bst0270196 |
0.332 |
|
| 1999 |
Huang L, Abu-Soud HM, Hille R, Stuehr DJ. Nitric oxide-generated P420 nitric oxide synthase: Characterization and roles for tetrahydrobiopterin and substrate in protecting against or reversing the P420 conversion Biochemistry. 38: 1912-1920. PMID 10026272 DOI: 10.1021/Bi981954T |
0.379 |
|
| 1999 |
Xia M, Dempski R, Hille R. The reductive half-reaction of xanthine oxidase. Reaction with aldehyde substrates and identification of the catalytically labile oxygen Journal of Biological Chemistry. 274: 3323-3330. PMID 9920873 DOI: 10.1074/jbc.274.6.3323 |
0.43 |
|
| 1999 |
Roberts P, Basran J, Mewies M, Hille R, Scrutton NS. Substrate inhibition in wild-type and mutant trimethylamine dehydrogenases Biochemical Society Transactions. 27: A46-A46. DOI: 10.1042/Bst027A046 |
0.316 |
|
| 1999 |
Ilich P, Hille R. Mechanism of formamide hydroxylation catalyzed by a molybdenum-dithiolene complex: A model for xanthine oxidase reactivity Journal of Physical Chemistry B. 103: 5406-5412. DOI: 10.1021/Jp9904825 |
0.437 |
|
| 1998 |
Hille R, Rétey J, Bartlewski-Hof U, Reichenbecher W. Mechanistic aspects of molybdenum-containing enzymes. Fems Microbiology Reviews. 22: 489-501. PMID 10189201 DOI: 10.1111/J.1574-6976.1998.Tb00383.X |
0.517 |
|
| 1998 |
Michaud AL, Herrick JA, Duplain JE, Manson JL, Hemann C, Ilich P, Donohoe RJ, Hille R, Oertling WA. FTIR characterization of heterocycles lumazine and violapterin in solution: effects of solvent on anionic forms Biospectroscopy. 4: 235-256. PMID 9706383 DOI: 10.1002/(Sici)1520-6343(1998)4:4<235::Aid-Bspy3>3.0.Co;2-1 |
0.312 |
|
| 1998 |
Conrads T, Hemann C, Hille R. Formation of a tyrosyl radical in xanthine oxidase. Biochemistry. 37: 7787-91. PMID 9601039 DOI: 10.1021/Bi972387X |
0.425 |
|
| 1998 |
Hille R. Reply to further comments on enzymes of the xanthine oxidase family Jbic Journal of Biological Inorganic Chemistry. 3: 559-560. DOI: 10.1007/S007750050268 |
0.367 |
|
| 1997 |
Babu CR, Arudchandran A, Hille R, Gross EL, Bullerjahn GS. Reconstitution and characterization of a divergent plastocyanin from the photosynthetic prokaryote, Prochlorothrix hollandica, expressed in Escherichia coli Biochemical and Biophysical Research Communications. 235: 631-635. PMID 9207210 DOI: 10.1006/Bbrc.1997.6846 |
0.372 |
|
| 1997 |
Mewies M, Basran J, Packman LC, Hille R, Scrutton NS. Involvement of a flavin iminoquinone methide in the formation of 6-hydroxyflavin mononucleotide in trimethylamine dehydrogenase: a rationale for the existence of 8alpha-methyl and C6-linked covalent flavoproteins. Biochemistry. 36: 7162-8. PMID 9188716 DOI: 10.1021/Bi970621D |
0.459 |
|
| 1997 |
Wilson EK, Huang L, Sutcliffe MJ, Mathews FS, Hille R, Scrutton NS. An exposed tyrosine on the surface of trimethylamine dehydrogenase facilitates electron transfer to electron transferring flavoprotein: Kinetics of transfer in wild-type and mutant complexes Biochemistry. 36: 41-48. PMID 8993316 DOI: 10.1021/Bi961224Q |
0.437 |
|
| 1997 |
Ilich P, Hille R. Tautomerization of the substrate heterocycle in the course of the reaction of xanthine oxidase Inorganica Chimica Acta. 263: 87-93. DOI: 10.1016/S0020-1693(97)05654-5 |
0.482 |
|
| 1997 |
Hille R. Mechanistic aspects of the mononuclear molybdenum enzymes Jbic Journal of Biological Inorganic Chemistry. 2: 804-809. DOI: 10.1007/S007750050199 |
0.44 |
|
| 1996 |
Hille R. The Mononuclear Molybdenum Enzymes. Chemical Reviews. 96: 2757-2816. PMID 11848841 |
0.324 |
|
| 1996 |
Bian S, Hemann CF, Hille R, Cowan JA. Characterization of an autoreduction pathway for the [Fe4S4]3+ cluster of mutant Chromatium vinosum high-potential iron proteins. Site-directed mutagenesis studies to probe the role of phenylalanine 66 in defining the stability of the [Fe4S4] center provide evidence for oxidative degradation via a [Fe3S4] cluster Biochemistry. 35: 14544-14552. PMID 8931551 DOI: 10.1021/Bi961658L |
0.341 |
|
| 1996 |
Huber R, Hof P, Duarte RO, Moura JJ, Moura I, Liu MY, LeGall J, Hille R, Archer M, Romão MJ. A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes. Proceedings of the National Academy of Sciences of the United States of America. 93: 8846-51. PMID 8799115 DOI: 10.1073/Pnas.93.17.8846 |
0.448 |
|
| 1996 |
Huang L, Scrutton NS, Hille R. Reaction of the C30A mutant of trimethylamine dehydrogenase with diethylmethylamine. The Journal of Biological Chemistry. 271: 13401-6. PMID 8662829 DOI: 10.1074/Jbc.271.23.13401 |
0.483 |
|
| 1996 |
Sun J, Kahlow MA, Kaysser TM, Osborne JP, Hill JJ, Rohlfs RJ, Hille R, Gennis RB, Loehr TM. Resonance Raman spectroscopic identification of a histidine ligand of b595 and the nature of the ligation of chlorin d in the fully reduced Escherichia coli cytochrome bd oxidase. Biochemistry. 35: 2403-12. PMID 8652583 DOI: 10.1021/Bi9518252 |
0.324 |
|
| 1996 |
Kim JH, Ryan MG, Knaut H, Hille R. The reductive half-reaction of xanthine oxidase. The involvement of prototropic equilibria in the course of the catalytic sequence. The Journal of Biological Chemistry. 271: 6771-80. PMID 8636099 DOI: 10.1074/Jbc.271.12.6771 |
0.468 |
|
| 1996 |
Brody MS, Hille R. The reaction of chicken liver sulfite oxidase with dimethylsulfite. Biochimica Et Biophysica Acta. 1253: 133-5. PMID 8519792 DOI: 10.1016/0167-4838(95)00194-4 |
0.488 |
|
| 1996 |
Hille R. Structure and function of mononuclear molybdenum enzymes Jbic Journal of Biological Inorganic Chemistry. 1: 397-404. DOI: 10.1007/S007750050071 |
0.43 |
|
| 1995 |
Rohlfs RJ, Huang L, Hille R. Prototropic control of intramolecular electron transfer in trimethylamine dehydrogenase. The Journal of Biological Chemistry. 270: 22196-207. PMID 7673198 DOI: 10.1074/Jbc.270.38.22196 |
0.423 |
|
| 1995 |
Ryan MG, Ratnam K, Hille R. The molybdenum centers of xanthine oxidase and xanthine dehydrogenase. Determination of the spectral change associated with reduction from the Mo(VI) to the Mo(IV) state. The Journal of Biological Chemistry. 270: 19209-12. PMID 7642590 DOI: 10.1074/Jbc.270.33.19209 |
0.364 |
|
| 1995 |
Huang L, Rohlfs RJ, Hille R. The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein. The Journal of Biological Chemistry. 270: 23958-65. PMID 7592591 DOI: 10.1074/Jbc.270.41.23958 |
0.45 |
|
| 1995 |
Anderson RF, Hille R, Patel KB. Inactivation of xanthine oxidase by oxidative radical attack International Journal of Radiation Biology. 68: 535-541. PMID 7490503 DOI: 10.1080/09553009514551521 |
0.383 |
|
| 1995 |
Hille R, Nishino T. Xanthine oxidase and xanthine dehydrogenase The Faseb Journal. 9: 995-1003. DOI: 10.1096/Fasebj.9.11.7649415 |
0.479 |
|
| 1995 |
Vitale M, Lee KK, Hemann CF, Hille R, Gustafson TL, Bursten BE. Resonance raman studies of [CpFe(CO)2]2 and [Cp*Fe(CO)2]2: A probe of photoreactive states and intermediates Journal of the American Chemical Society. 117: 2286-2296. DOI: 10.1021/Ja00113A017 |
0.547 |
|
| 1995 |
Schultz BE, Hille R, Holm RH. Direct oxygen atom transfer in the mechanism of action of Rhodobacter sphaeroides dimethyl sulfoxide reductase Journal of the American Chemical Society. 117: 827-828. DOI: 10.1021/Ja00107A031 |
0.304 |
|
| 1994 |
Lorigan GA, Britt RD, Kim JH, Hille R. Electron spin echo envelope modulation spectroscopy of the molybdenum center of xanthine oxidase. Biochimica Et Biophysica Acta. 1185: 284-94. PMID 8180233 DOI: 10.1016/0005-2728(94)90243-7 |
0.544 |
|
| 1994 |
Hille R. The reaction mechanism of oxomolybdenum enzymes. Biochimica Et Biophysica Acta. 1184: 143-69. PMID 8130250 DOI: 10.1016/0005-2728(94)90220-8 |
0.448 |
|
| 1994 |
Kim JH, Hille R. Studies of the substrate binding to xanthine oxidase using a spin-labeled analog. Journal of Inorganic Biochemistry. 55: 295-303. PMID 7964716 DOI: 10.1016/0162-0134(94)85013-5 |
0.464 |
|
| 1993 |
Hille R, Kim JH, Hemann C. Reductive half-reaction of xanthine oxidase: mechanistic role of the species giving rise to the "rapid type 1" molybdenum(V) electron paramagnetic resonance signal. Biochemistry. 32: 3973-80. PMID 8385992 DOI: 10.1021/Bi00066A018 |
0.477 |
|
| 1991 |
Hille R, Massey V. The kinetic behavior of xanthine oxidase containing chemically modified flavins. The Journal of Biological Chemistry. 266: 17401-8. PMID 1894627 |
0.724 |
|
| 1991 |
Hille R. Electron transfer within xanthine oxidase: a solvent kinetic isotope effect study. Biochemistry. 30: 8522-9. PMID 1888720 DOI: 10.1021/Bi00099A004 |
0.444 |
|
| 1991 |
Anderson GL, Hille R. Characterization and rapid kinetics of arsenite oxidase; A molybdenum-containing enzyme with unusual properties Journal of Inorganic Biochemistry. 43: 577. DOI: 10.1016/0162-0134(91)84550-S |
0.457 |
|
| 1991 |
McWhirter RB, Hille R. The reductive half-reaction of xanthine oxidase: Spectral intermediates in the hydroxylation of 2-hydroxy-6-methylpurine Journal of Inorganic Biochemistry. 43: 576. DOI: 10.1016/0162-0134(91)84549-O |
0.375 |
|
| 1991 |
Rohlfs RJ, Hille R. Intramolecular electron transfer in trimethylamine dehydrogenase from W3A1 Journal of Inorganic Biochemistry. 43: 115. DOI: 10.1016/0162-0134(91)84111-L |
0.353 |
|
| 1989 |
Zeller HD, Hille R, Jorns MS. Bacterial sarcosine oxidase: identification of novel substrates and a biradical reaction intermediate. Biochemistry. 28: 5145-54. PMID 2475174 DOI: 10.1021/Bi00438A035 |
0.523 |
|
| 1989 |
Hille R, George GN, Eidsness MK, Cramer SP. EXAFS analysis of xanthine oxidase complexes with alloxanthine, violapterin, and 6-pteridylaldehyde Inorganic Chemistry. 28: 4018-4022. DOI: 10.1021/Ic00320A016 |
0.328 |
|
| 1986 |
Anderson RF, Hille R, Massey V. The radical chemistry of milk xanthine oxidase as studied by radiation chemistry techniques. The Journal of Biological Chemistry. 261: 15870-6. PMID 3782094 |
0.704 |
|
| 1986 |
Hille R, Massey V. The equilibration of reducing equivalents within milk xanthine oxidase. The Journal of Biological Chemistry. 261: 1241-7. PMID 3753700 |
0.663 |
|
| 1985 |
Stewart RC, Hille R, Massey V. The reaction of arsenite-complexed xanthine oxidase with oxygen. Evidence for an oxygen-reactive molybdenum center. The Journal of Biological Chemistry. 260: 8892-904. PMID 3839506 |
0.706 |
|
| 1984 |
Stewart RC, Hille R, Massey V. Characterization of arsenite-complexed xanthine oxidase at room temperature. Spectral properties and pH-dependent redox behavior of the molybdenum-arsenite center. The Journal of Biological Chemistry. 259: 14426-36. PMID 6094556 |
0.692 |
|
| 1983 |
Hille R, Stewart RC, Fee JA, Massey V. The interaction of arsenite with xanthine oxidase. The Journal of Biological Chemistry. 258: 4849-56. PMID 6300101 |
0.71 |
|
| 1982 |
Nishino T, Tsushima K, Hille R, Massey V. Inhibition of milk xanthine oxidase by fluorodinitrobenzene. The Journal of Biological Chemistry. 257: 7348-53. PMID 6806272 |
0.708 |
|
| 1982 |
Hille R, Massey V. The presence of a reducible disulfide bond in milk xanthine oxidase. The Journal of Biological Chemistry. 257: 8898-901. PMID 6284747 |
0.725 |
|
| 1981 |
Hille R, Massey V. Tight binding inhibitors of xanthine oxidase. Pharmacology & Therapeutics. 14: 249-63. PMID 6895556 DOI: 10.1016/0163-7258(81)90063-2 |
0.73 |
|
| 1981 |
Hille R, Massey V. Studies on the oxidative half-reaction of xanthine oxidase. The Journal of Biological Chemistry. 256: 9090-5. PMID 6894924 |
0.726 |
|
| 1981 |
Hille R, Fee JA, Massey V. Equilibrium properties of xanthine oxidase containing FAD analogs of varying oxidation-reduction potential. The Journal of Biological Chemistry. 256: 8933-40. PMID 6894923 |
0.624 |
|
| 1979 |
Hille R, Olson JS, Palmer G. Spectral transitions of nitrosyl hemes during ligand binding to hemoglobin. The Journal of Biological Chemistry. 254: 12110-20. PMID 40990 |
0.605 |
|
| 1977 |
Hille R, Palmer G, Olson JS. Chain equivalence in reaction of nitric oxide with hemoglobin. The Journal of Biological Chemistry. 252: 403-5. PMID 188812 |
0.645 |
|
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