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Thomas M. Loehr - Publications

Affiliations: 
Oregon Health and Science University, Portland, OR 
Area:
Biochemistry, Molecular Biology, General Biophysics
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33 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2001 Taoka S, Green EL, Loehr TM, Banerjee R. Mercuric chloride-induced spin or ligation state changes in ferric or ferrous human cystathionine beta-synthase inhibit enzyme activity. Journal of Inorganic Biochemistry. 87: 253-9. PMID 11744063 DOI: 10.1016/S0162-0134(01)00336-1  0.386
2001 Baldwin J, Voegtli WC, Khidekel N, Moënne-Loccoz P, Krebs C, Pereira AS, Ley BA, Huynh BH, Loehr TM, Riggs-Gelasco PJ, Rosenzweig AC, Bollinger JM. Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a self-hydroxylating monooxygenase. Journal of the American Chemical Society. 123: 7017-30. PMID 11459480 DOI: 10.1021/Ja002114G  0.413
2001 Hirst J, Wilcox SK, Ai J, Moënne-Loccoz P, Loehr TM, Goodin DB. Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 2. Effects on heme coordination and function. Biochemistry. 40: 1274-83. PMID 11170453 DOI: 10.1021/Bi002090Q  0.412
2000 Fee JA, Chen Y, Todaro TR, Bren KL, Patel KM, Hill MG, Gomez-Moran E, Loehr TM, Ai J, Thöny-Meyer L, Williams PA, Stura E, Sridhar V, McRee DE. Integrity of thermus thermophilus cytochrome c552 synthesized by Escherichia coli cells expressing the host-specific cytochrome c maturation genes, ccmABCDEFGH: biochemical, spectral, and structural characterization of the recombinant protein. Protein Science : a Publication of the Protein Society. 9: 2074-84. PMID 11152119 DOI: 10.1110/Ps.9.11.2074  0.328
2000 Lyle KS, Möenne-Loccoz P, Ai J, Sanders-Loehr J, Loehr TM, Fox BG. Resonance Raman studies of the stoichiometric catalytic turnover of a substrate-stearoyl-acyl carrier protein delta(9) desaturase complex. Biochemistry. 39: 10507-13. PMID 10956041 DOI: 10.1021/Bi000965V  0.386
2000 Youngs HL, Moënne-Loccoz P, Loehr TM, Gold MH. Formation of a bis(histidyl) heme iron complex in manganese peroxidase at high pH and restoration of the native enzyme structure by calcium. Biochemistry. 39: 9994-10000. PMID 10933820 DOI: 10.1021/Bi000679J  0.595
1999 Moënne-Loccoz P, Krebs C, Herlihy K, Edmondson DE, Theil EC, Huynh BH, Loehr TM. The ferroxidase reaction of ferritin reveals a diferric mu-1,2 bridging peroxide intermediate in common with other O2-activating non-heme diiron proteins. Biochemistry. 38: 5290-5. PMID 10220314 DOI: 10.1021/Bi990095L  0.467
1999 Liu Y, Moënne-Loccoz P, Hildebrand DP, Wilks A, Loehr TM, Mauk AG, Ortiz De Montellano PR. Replacement of the proximal histidine iron ligand by a cysteine or tyrosine converts heme oxygenase to an oxidase Biochemistry. 38: 3733-3743. PMID 10090762 DOI: 10.1021/Bi982707S  0.494
1997 Cohen JD, Bao W, Renganathan V, Subramaniam SS, Loehr TM. Resonance Raman spectroscopic studies of cellobiose dehydrogenase from Phanerochaete chrysosporium. Archives of Biochemistry and Biophysics. 341: 321-8. PMID 9169022 DOI: 10.1006/Abbi.1997.9987  0.422
1997 Liu Y, Moënne-Loccoz P, Loehr TM, Ortiz De Montellano PR. Heme oxygenase-1, intermediates in verdoheme formation and the requirement for reduction equivalents Journal of Biological Chemistry. 272: 6909-6917. PMID 9054378 DOI: 10.1074/Jbc.272.11.6909  0.38
1997 Andrew CR, Han J, Den Blaauwen T, Van Pouderoyen G, Vijgenboom E, Canters GW, Loehr TM, Sanders-Loehr J. Cysteine ligand vibrations are responsible for the complex resonance Raman spectrum of azurin Journal of Biological Inorganic Chemistry. 2: 98-107. DOI: 10.1007/S007750050111  0.425
1997 Ai J, Broadwater JA, Loehr TM, Sanders-Loehr J, Fox BG. Azide adducts of stearoyl-ACP desaturase: A model for μ-1,2 bridging by dioxygen in the binuclear iron active site Journal of Biological Inorganic Chemistry. 2: 37-45. DOI: 10.1007/S007750050104  0.471
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  0.415
1995 Sun J, Osborne JP, Kahlow MA, Kaysser TM, Hil JJ, Gennis RB, Loehr TM. Resonance Raman studies of Escherichia coli cytochrome bd oxidase. Selective enhancement of the three heme chromophores of the "as-isolated" enzyme and characterization of the cyanide adduct. Biochemistry. 34: 12144-51. PMID 7547954 DOI: 10.1021/Bi00038A007  0.41
1993 Loehr TM, Sanders-Loehr J. Techniques for obtaining resonance Raman spectra of metalloproteins. Methods in Enzymology. 226: 431-70. PMID 8277876 DOI: 10.1016/0076-6879(93)26020-A  0.323
1993 Kahlow MA, Loehr TM, Zuberi TM, Gennis RB. The oxygenated complex of cytochrome d terminal oxidase: direct evidence for iron-oxygen coordination in a chlorin-containing enzyme by resonance Raman spectroscopy Journal of the American Chemical Society. 115: 5845-5846. DOI: 10.1021/Ja00066A071  0.414
1993 Han J, Loehr TM, Lu Y, Valentine JS, Averill BA, Sanders-Loehr J. Resonance raman excitation profiles indicate multiple cys → Cu charge transfer transitions in type 1 copper proteins Journal of the American Chemical Society. 115: 4256-4263. DOI: 10.1021/Ja00063A048  0.344
1993 Andersson LA, Mylrajan M, Loehr TM, Chang CK. Vibrational spectra of isomeric copper(II)-dimethyl-octaethylisobacteriochlorin complexes: effects of non-conjugated substituents Spectrochimica Acta Part a: Molecular and Biomolecular Spectroscopy. 49: 2105-2116. DOI: 10.1016/S0584-8539(09)91020-0  0.371
1992 Han J, Blackburn NJ, Loehr TM. Identification of the Cyanide Stretching Frequency in the Cyano Derivative of Copper/Zinc-Superoxide Dismutase by Ir and Raman Spectroscopy Inorganic Chemistry. 31: 3223-3229. DOI: 10.1021/Ic00041A011  0.379
1992 Loehr TM. Detection of conserved structural elements in ferredoxins and cupredoxins by resonance Raman spectroscopy Journal of Raman Spectroscopy. 23: 531-537. DOI: 10.1002/Jrs.1250231005  0.4
1990 Sahlin M, Sjöberg BM, Backes G, Loehr T, Sanders-Loehr J. Activation of the iron-containing B2 protein of ribonucleotide reductase by hydrogen peroxide. Biochemical and Biophysical Research Communications. 167: 813-8. PMID 2182022 DOI: 10.1016/0006-291X(90)92098-K  0.344
1990 Mylrajan M, Valli K, Wariishi H, Gold MH, Loehr TM. Resonance Raman spectroscopic characterization of compound III of lignin peroxidase. Biochemistry. 29: 9617-9623. PMID 2176851 DOI: 10.1021/Bi00493A016  0.41
1990 Andersson LA, Loehr TM, Wu WS, Chang CK, Timkovich R. Modelling heme d1. The spectral properties of copper(II) porphyrindiones. Febs Letters. 267: 285-8. PMID 2116325 DOI: 10.1016/0014-5793(90)80946-G  0.384
1988 Nocek JM, Kurtz DM, Sage JT, Xia YM, Debrunner P, Shiemke AK, Sanders-Loehr J, Loehr TM. Nitric oxide adducts of the binuclear iron site of hemerythrin: spectroscopy and reactivity. Biochemistry. 27: 1014-24. PMID 3365363 DOI: 10.1021/Bi00403A026  0.447
1988 Ahmad S, McCallum JD, Shiemke AK, Appelman EH, Loehr TM, Sanders-Loehr J. Raman spectroscopic evidence for side-on binding of peroxide ion to ferric EDTA Inorganic Chemistry. 27: 2230-2233. DOI: 10.1021/Ic00286A006  0.318
1987 Ainscough EW, Bingham AG, Brodie AM, Ellis WR, Gray HB, Loehr TM, Plowman JE, Norris GE, Baker EN. Spectrochemical studies on the blue copper protein azurin from Alcaligenes denitrificans. Biochemistry. 26: 71-82. PMID 3030404 DOI: 10.1021/Bi00375A011  0.462
1986 Sibbett SS, Loehr TM, Hurst JK. Resonance raman spectroscopic evidence for perturbation of vinyl modes in copper(I)-protoheme π-complexes Inorganic Chemistry. 25: 307-313. DOI: 10.1021/Ic00223A016  0.372
1985 Plowman JE, Loehr TM, Schauer CK, Anderson OP. CRYSTAL AND MOLECULAR STRUCTURE OF THE (μ-OXO)BIS(AQUOBIS(PHENANTHROLINE)IRON(III)) COMPLEX, A RAMAN SPECTROSCOPIC MODEL FOR THE BINUCLEAR IRON SITE IN HEMERYTHRIN AND RIBONUCLEOTIDE REDUCTASE Cheminform. 16. DOI: 10.1002/Chin.198507054  0.398
1984 Lukat GS, Kurtz DM, Shiemke AK, Loehr TM, Sanders-Loehr J. Sulfide-bridged derivatives of the binuclear iron site of hemerythrin at both met and semi-met oxidation levels. Biochemistry. 23: 6416-22. PMID 6529557 DOI: 10.1021/Bi00321A021  0.435
1984 Plowman JE, Loehr TM, Schauer CK, Anderson OP. Crystal and molecular structure of the (μ-oxo)bis[aquobis(phenanthroline)iron(III)] complex, a Raman spectroscopic model for the binuclear iron site in hemerythrin and ribonucleotide reductase Inorganic Chemistry. 23: 3553-3559. DOI: 10.1021/Ic00190A024  0.365
1977 Keyes WE, Dunn JBR, Loehr TM. A water-stable copper(III) complex Journal of the American Chemical Society. 99: 4527-4529. DOI: 10.1021/Ja00455A065  0.32
1977 Keyes WE, Dunn JBR, Loehr TM. A water-stable copper(III) complex Cheminform. 8. DOI: 10.1002/Chin.197739325  0.32
1969 Loehr TM, Plane RA. Raman spectra of arsenic trichloride in water and alcohols and the spectrum of arsenic tribromide Inorganic Chemistry. 8: 73-78. DOI: 10.1021/Ic50071A018  0.306
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