Year |
Citation |
Score |
2019 |
Burrows JE, Paulson MQ, Altman ER, Vukovic I, Machonkin TE. The role of halogen substituents and substrate pK in defining the substrate specificity of 2,6-dichlorohydroquinone 1,2-dioxygenase (PcpA). Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 31089822 DOI: 10.1007/S00775-019-01663-4 |
0.33 |
|
2015 |
Schofield JA, Brennessel WW, Urnezius E, Rokhsana D, Boshart MD, Juers DH, Holland PL, Machonkin TE. Metal-Halogen Secondary Bonding in a 2,5-Dichlorohydroquinonate Cobalt(II) Complex: Insight into Substrate Coordination in the Chlorohydroquinone Dioxygenase PcpA European Journal of Inorganic Chemistry. 2015: 4643-4647. DOI: 10.1002/Ejic.201500845 |
0.349 |
|
2014 |
Machonkin TE, Boshart MD, Schofield JA, Rodriguez MM, Grubel K, Rokhsana D, Brennessel WW, Holland PL. Structural and spectroscopic characterization of iron(II), cobalt(II), and nickel(II) ortho-dihalophenolate complexes: insights into metal-halogen secondary bonding. Inorganic Chemistry. 53: 9837-48. PMID 25167329 DOI: 10.1021/Ic501424E |
0.373 |
|
2011 |
Machonkin TE, Doerner AE. Substrate specificity of Sphingobium chlorophenolicum 2,6-dichlorohydroquinone 1,2-dioxygenase. Biochemistry. 50: 8899-913. PMID 21870805 DOI: 10.1021/Bi200855M |
0.335 |
|
2010 |
Rocks SS, Brennessel WW, Machonkin TE, Holland PL. Solution and structural characterization of iron(II) complexes with ortho-halogenated phenolates: insights into potential substrate binding modes in hydroquinone dioxygenases. Inorganic Chemistry. 49: 10914-29. PMID 21058671 DOI: 10.1021/Ic101377U |
0.366 |
|
2010 |
Machonkin TE, Holland PL, Smith KN, Liberman JS, Dinescu A, Cundari TR, Rocks SS. Determination of the active site of Sphingobium chlorophenolicum 2,6-dichlorohydroquinone dioxygenase (PcpA). Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 15: 291-301. PMID 19924449 DOI: 10.1007/S00775-009-0602-9 |
0.35 |
|
2009 |
Lin IJ, Xia B, King DS, Machonkin TE, Westler WM, Markley JL. Hyperfine-shifted (13)C and (15)N NMR signals from Clostridium pasteurianum rubredoxin: extensive assignments and quantum chemical verification. Journal of the American Chemical Society. 131: 15555-63. PMID 19799419 DOI: 10.1021/Ja905928X |
0.343 |
|
2009 |
Rocks SS, Brennessel WW, Machonkin TE, Holland PL. Solid-state and proton NMR characterization of an iron(II) complex of a tridentate, facially coordinating N,N,O donor ligand Inorganica Chimica Acta. 362: 1387-1390. DOI: 10.1016/J.Ica.2008.05.037 |
0.382 |
|
2005 |
Lin IJ, Gebel EB, Machonkin TE, Westler WM, Markley JL. Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants. Proceedings of the National Academy of Sciences of the United States of America. 102: 14581-6. PMID 16199518 DOI: 10.1073/Pnas.0505521102 |
0.315 |
|
2005 |
Machonkin TE, Westler WM, Markley JL. Paramagnetic NMR spectroscopy and density functional calculations in the analysis of the geometric and electronic structures of iron-sulfur proteins. Inorganic Chemistry. 44: 779-97. PMID 15859246 DOI: 10.1021/Ic048624J |
0.361 |
|
2004 |
Park IY, Eidsness MK, Lin IJ, Gebel EB, Youn B, Harley JL, Machonkin TE, Frederick RO, Markley JL, Smith ET, Ichiye T, Kang C. Crystallographic studies of V44 mutants of Clostridium pasteurianum rubredoxin: effects of side-chain size on reduction potential. Proteins. 57: 618-25. PMID 15382226 DOI: 10.1002/Prot.20243 |
0.329 |
|
2004 |
Machonkin TE, Westler WM, Markley JL. Strategy for the study of paramagnetic proteins with slow electronic relaxation rates by nmr spectroscopy: application to oxidized human [2Fe-2S] ferredoxin. Journal of the American Chemical Society. 126: 5413-26. PMID 15113213 DOI: 10.1021/Ja037077I |
0.333 |
|
2003 |
Lin IJ, Gebel EB, Machonkin TE, Westler WM, Markley JL. Correlation between hydrogen bond lengths and reduction potentials in Clostridium pasteurianum rubredoxin. Journal of the American Chemical Society. 125: 1464-5. PMID 12568591 DOI: 10.1021/Ja028710N |
0.313 |
|
2003 |
Machonkin TE, Westler WM, Markley JL. Structural determinants of electronic differences among classes of [2Fe2S] ferredoxins: Insights from paramagnetic NMR and electronic structure calculations Journal of Inorganic Biochemistry. 96: 184. DOI: 10.1016/S0162-0134(03)80699-2 |
0.309 |
|
2002 |
Machonkin TE, Westler WM, Markley JL. (13)C[(13)C] 2D NMR: a novel strategy for the study of paramagnetic proteins with slow electronic relaxation rates. Journal of the American Chemical Society. 124: 3204-5. PMID 11916393 DOI: 10.1021/Ja017733J |
0.307 |
|
2002 |
Machonkin TE, Mukherjee P, Henson MJ, Stack TDP, Solomon EI. The EPR spectrum of a Cu(II/II/III) cluster: Anisotropic exchange in a bent Cu(II)2O2 core Inorganica Chimica Acta. 341: 39-44. DOI: 10.1016/S0020-1693(02)01179-9 |
0.599 |
|
2001 |
Machonkin TE, Quintanar L, Palmer AE, Hassett R, Severance S, Kosman DJ, Solomon EI. Spectroscopy and reactivity of the type 1 copper site in Fet3p from Saccharomyces cerevisiae: correlation of structure with reactivity in the multicopper oxidases. Journal of the American Chemical Society. 123: 5507-17. PMID 11389633 DOI: 10.1021/Ja003975S |
0.651 |
|
2000 |
Machonkin TE, Solomon EI. The thermodynamics, kinetics, and molecular mechanism of intramolecular electron transfer in human ceruloplasmin Journal of the American Chemical Society. 122: 12547-12560. DOI: 10.1021/Ja002339R |
0.562 |
|
1999 |
Machonkin TE, Musci G, Zhang HH, Bonaccorsi di Patti MC, Calabrese L, Hedman B, Hodgson KO, Solomon EI. Investigation of the anomalous spectroscopic features of the copper sites in chicken ceruloplasmin: comparison to human ceruloplasmin. Biochemistry. 38: 11093-102. PMID 10460165 DOI: 10.1021/Bi990280Z |
0.589 |
|
1998 |
Machonkin TE, Zhang HH, Hedman B, Hodgson KO, Solomon EI. Spectroscopic and magnetic studies of human ceruloplasmin: identification of a redox-inactive reduced Type 1 copper site. Biochemistry. 37: 9570-8. PMID 9649340 DOI: 10.1021/Bi980434V |
0.577 |
|
1998 |
Solomon EI, Palmer AE, Sundaram UM, Machonkin TE. Spectroscopic Studies of O2 Intermediates in Copper Proteins: Electronic Structure Contributions to Function in Bioinorganic Chemistry Acs Symposium Series. 692: 423-452. |
0.589 |
|
1996 |
Solomon EI, Sundaram UM, Machonkin TE. Multicopper Oxidases and Oxygenases. Chemical Reviews. 96: 2563-2606. PMID 11848837 DOI: 10.1021/Cr950046O |
0.542 |
|
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