Year |
Citation |
Score |
2014 |
Jancura D, Stanicova J, Palmer G, Fabian M. How hydrogen peroxide is metabolized by oxidized cytochrome c oxidase Biochemistry. 53: 3564-3575. PMID 24840065 DOI: 10.1021/Bi401078B |
0.392 |
|
2012 |
da Silva GF, Shinkarev VP, Kamensky YA, Palmer G. Spectroscopic evidence of the role of an axial ligand histidinate in the mechanism of adrenal cytochrome b561. Biochemistry. 51: 8730-42. PMID 23088392 DOI: 10.1021/Bi301127K |
0.381 |
|
2011 |
Tsai AL, Wu G, Rogge CE, Lü JM, Peng S, Van Der Donk WA, Palmer G, Gerfen GJ, Kulmacz RJ. Structural comparisons of arachidonic acid-induced radicals formed by prostaglandin H synthase-1 and -2 Journal of Inorganic Biochemistry. 105: 366-374. PMID 21421123 DOI: 10.1016/J.Jinorgbio.2010.11.012 |
0.32 |
|
2011 |
Sato H, Higashimoto Y, Sakamoto H, Sugishima M, Shimokawa C, Harada J, Palmer G, Noguchi M. Reduction of oxaporphyrin ring of CO-bound α-verdoheme complexed with heme oxygenase-1 by NADPH-cytochrome P450 reductase. Journal of Inorganic Biochemistry. 105: 289-96. PMID 21194630 DOI: 10.1016/J.Jinorgbio.2010.11.010 |
0.386 |
|
2010 |
Parul D, Palmer G, Fabian M. Ligand trapping by cytochrome c oxidase: implications for gating at the catalytic center. The Journal of Biological Chemistry. 285: 4536-43. PMID 20037139 DOI: 10.1074/Jbc.M109.078618 |
0.349 |
|
2008 |
Higashimoto Y, Sugishima M, Sato H, Sakamoto H, Fukuyama K, Palmer G, Noguchi M. Mass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase. Biochemical and Biophysical Research Communications. 367: 852-8. PMID 18194664 DOI: 10.1016/J.Bbrc.2008.01.016 |
0.311 |
|
2007 |
Sato H, Higashimoto Y, Sakamoto H, Sugishima M, Takahashi K, Palmer G, Noguchi M. Electrochemical reduction of ferrous alpha-verdoheme in complex with heme oxygenase-1. Journal of Inorganic Biochemistry. 101: 1394-9. PMID 17644182 DOI: 10.1016/J.Jinorgbio.2007.05.016 |
0.369 |
|
2007 |
Kamensky Y, Liu W, Tsai AL, Kulmacz RJ, Palmer G. Axial ligation and stoichiometry of heme centers in adrenal cytochrome b561. Biochemistry. 46: 8647-58. PMID 17602662 DOI: 10.1021/Bi700054G |
0.343 |
|
2007 |
Wu G, Rogge CE, Wang JS, Kulmacz RJ, Palmer G, Tsai AL. Oxyferryl heme and not tyrosyl radical is the likely culprit in prostaglandin H synthase-1 peroxidase inactivation. Biochemistry. 46: 534-42. PMID 17209563 DOI: 10.1021/Bi061859H |
0.35 |
|
2006 |
Higashimoto Y, Sato H, Sakamoto H, Takahashi K, Palmer G, Noguchi M. The reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase. Electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN. The Journal of Biological Chemistry. 281: 31659-67. PMID 16928691 DOI: 10.1074/Jbc.M606163200 |
0.394 |
|
2006 |
Jancura D, Antalik M, Berka V, Palmer G, Fabian M. Filling the catalytic site of cytochrome c oxidase with electrons. Reduced CuB facilitates internal electron transfer to heme a3. The Journal of Biological Chemistry. 281: 20003-10. PMID 16704969 DOI: 10.1074/Jbc.M602066200 |
0.383 |
|
2006 |
Fabian M, Jancura D, Bona M, Musatov A, Baran M, Palmer G. Influence of reduction of heme a and Cu(A) on the oxidized catalytic center of cytochrome c oxidase: insight from organic solvents. Biochemistry. 45: 4277-83. PMID 16566602 DOI: 10.1021/Bi052632+ |
0.321 |
|
2005 |
Antalik M, Jancura D, Palmer G, Fabian M. A role for the protein in internal electron transfer to the catalytic center of cytochrome c oxidase. Biochemistry. 44: 14881-9. PMID 16274235 DOI: 10.1021/Bi050824Z |
0.338 |
|
2005 |
Higashimoto Y, Sakamoto H, Hayashi S, Sugishima M, Fukuyama K, Palmer G, Noguchi M. Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductase. The Journal of Biological Chemistry. 280: 729-37. PMID 15516695 DOI: 10.1074/Jbc.M406203200 |
0.313 |
|
2004 |
Sakamoto H, Higashimoto Y, Hayashi S, Sugishima M, Fukuyama K, Palmer G, Noguchi M. Hydroxylamine and hydrazine bind directly to the heme iron of the heme-heme oxygenase-1 complex. Journal of Inorganic Biochemistry. 98: 1223-8. PMID 15219989 DOI: 10.1016/J.Jinorgbio.2004.02.028 |
0.377 |
|
2004 |
Berka V, Wu G, Yeh HC, Palmer G, Tsai AL. Three different oxygen-induced radical species in endothelial nitric-oxide synthase oxygenase domain under regulation by L-arginine and tetrahydrobiopterin. The Journal of Biological Chemistry. 279: 32243-51. PMID 15166218 DOI: 10.1074/Jbc.M404044200 |
0.339 |
|
2004 |
Liu W, Rogge CE, Bambai B, Palmer G, Tsai AL, Kulmacz RJ. Characterization of the heme environment in Arabidopsis thaliana fatty acid alpha-dioxygenase-1. The Journal of Biological Chemistry. 279: 29805-15. PMID 15100225 DOI: 10.1074/Jbc.M401779200 |
0.368 |
|
2004 |
McMahon BH, Fabian M, Tomson F, Causgrove TP, Bailey JA, Rein FN, Dyer RB, Palmer G, Gennis RB, Woodruff WH. FTIR studies of internal proton transfer reactions linked to inter-heme electron transfer in bovine cytochrome c oxidase. Biochimica Et Biophysica Acta. 1655: 321-31. PMID 15100047 DOI: 10.1016/J.Bbabio.2004.01.007 |
0.374 |
|
2004 |
Fabian M, Skultety L, Jancura D, Palmer G. Implications of ligand binding studies for the catalytic mechanism of cytochrome c oxidase. Biochimica Et Biophysica Acta. 1655: 298-305. PMID 15100045 DOI: 10.1016/J.Bbabio.2003.07.008 |
0.339 |
|
2004 |
Fabian M, Jancura D, Palmer G. Two sites of interaction of anions with cytochrome a in oxidized bovine cytochrome c oxidase. The Journal of Biological Chemistry. 279: 16170-7. PMID 14766756 DOI: 10.1074/Jbc.M311834200 |
0.335 |
|
2002 |
Kamensky Y, Kulmacz RJ, Palmer G. Composition of the heme centers in chromaffin granule cytochrome b(561). Annals of the New York Academy of Sciences. 971: 450-3. PMID 12438163 DOI: 10.1111/J.1749-6632.2002.Tb04507.X |
0.35 |
|
2002 |
Tsai AL, Palmer G, Wu G, Peng S, Okeley NM, van der Donk WA, Kulmacz RJ. Structural characterization of arachidonyl radicals formed by aspirin-treated prostaglandin H synthase-2. The Journal of Biological Chemistry. 277: 38311-21. PMID 12167656 DOI: 10.1074/Jbc.M206961200 |
0.317 |
|
2001 |
Morgan JE, Verkhovsky MI, Palmer G, Wikström M. Role of the PR intermediate in the reaction of cytochrome c oxidase with O2. Biochemistry. 40: 6882-92. PMID 11389603 DOI: 10.1021/Bi010246W |
0.32 |
|
2001 |
Fabian M, Skultety L, Brunel C, Palmer G. Cyanide stimulated dissociation of chloride from the catalytic center of oxidized cytochrome c oxidase Biochemistry. 40: 6061-6069. PMID 11352742 DOI: 10.1021/Bi010059Y |
0.358 |
|
2001 |
Fabian M, Palmer G. Proton involvement in the transition from the "peroxy" to the ferryl intermediate of cytochrome c oxidase Biochemistry. 40: 1867-1874. PMID 11327850 DOI: 10.1021/Bi002373I |
0.315 |
|
2001 |
Kamensky YA, Palmer G. Chromaffin granule membranes contain at least three heme centers: Direct evidence from EPR and absorption spectroscopy Febs Letters. 491: 119-122. PMID 11226432 DOI: 10.1016/S0014-5793(01)02173-1 |
0.367 |
|
2000 |
Sakamoto H, Omata Y, Adachi Y, Palmer G, Noguchi M. Separation and identification of the regioisomers of verdoheme by reversed-phase ion-pair high-performance liquid chromatography, and characterization of their complexes with heme oxygenase Journal of Inorganic Biochemistry. 82: 113-121. PMID 11132617 DOI: 10.1016/S0162-0134(00)00149-5 |
0.322 |
|
2000 |
Shi W, Hoganson CW, Espe M, Bender CJ, Babcock GT, Palmer G, Kulmacz RJ, Tsai Al. Electron paramagnetic resonance and electron nuclear double resonance spectroscopic identification and characterization of the tyrosyl radicals in prostaglandin H synthase 1. Biochemistry. 39: 4112-21. PMID 10747802 DOI: 10.1021/Bi992561C |
0.59 |
|
1999 |
Tsai AL, Wu G, Palmer G, Bambai B, Koehn JA, Marshall PJ, Kulmacz RJ. Rapid kinetics of tyrosyl radical formation and heme redox state changes in prostaglandin H synthase-1 and -2 Journal of Biological Chemistry. 274: 21695-21700. PMID 10419480 DOI: 10.1016/S0090-6980(99)90355-6 |
0.302 |
|
1999 |
Sakamoto H, Omata Y, Palmer G, Noguchi M. Ferric α-hydroxyheme bound to heme oxygenase can be converted to verdoheme by dioxygen in the absence of added reducing equivalents Journal of Biological Chemistry. 274: 18196-18200. PMID 10373419 DOI: 10.1074/Jbc.274.26.18196 |
0.37 |
|
1999 |
Fabian M, Palmer G. Redox state of peroxy and ferryl intermediates in cytochrome c oxidase catalysis Biochemistry. 38: 6270-6275. PMID 10320356 DOI: 10.1021/Bi982541V |
0.351 |
|
1998 |
Tsai AL, Berka V, KulMacZ RJ, Wu G, Palmer G. An improved sample packing device for rapid freeze-trap electron paramagnetic resonance spectroscopy kinetic measurements Analytical Biochemistry. 264: 165-171. PMID 9866678 DOI: 10.1006/Abio.1998.2774 |
0.304 |
|
1998 |
Liao GL, Palmer G. Diazene - A not so innocent ligand for the binuclear center of cytochrome C oxidase Biochemistry. 37: 15583-15592. PMID 9799523 DOI: 10.1021/Bi981476M |
0.359 |
|
1998 |
Berka V, Palmer G, Chen PF, Tsai AL. Effects of various imidazole ligands on heme conformation in endothelial nitric oxide synthase Biochemistry. 37: 6136-6144. PMID 9558353 DOI: 10.1021/Bi980133L |
0.329 |
|
1997 |
Xiao G, Tsai AL, Palmer G, Boyar WC, Marshall PJ, Kulmacz RJ. Analysis of hydroperoxide-induced tyrosyl radicals and lipoxygenase activity in aspirin-treated human prostaglandin H synthase-2 Biochemistry. 36: 1836-1845. PMID 9048568 DOI: 10.1021/Bi962476U |
0.311 |
|
1996 |
Chang KT, Palmer G. Formate bound to cytochrome oxidase can be removed by cyanide and by reduction Biochimica Et Biophysica Acta - Bioenergetics. 1277: 237-242. PMID 8982389 DOI: 10.1016/S0005-2728(96)00105-3 |
0.356 |
|
1996 |
Tsai AL, Berka V, Chen PF, Palmer G. Characterization of endothelial nitric-oxide synthase and its reaction with ligand by electron paramagnetic resonance spectroscopy Journal of Biological Chemistry. 271: 32563-32571. PMID 8955082 DOI: 10.1074/Jbc.271.51.32563 |
0.358 |
|
1996 |
Liao GL, Palmer G. The reduced minus oxidized difference spectra of cytochromes a and a3 Biochimica Et Biophysica Acta - Bioenergetics. 1274: 109-111. PMID 8664303 DOI: 10.1016/0005-2728(96)00014-X |
0.339 |
|
1995 |
Fabian M, Palmer G. The reaction of cyanide with peroxidatic forms of cytochrome oxidase Biochemistry. 34: 1534-1540. PMID 7849012 DOI: 10.1021/Bi00005A009 |
0.33 |
|
1995 |
Tsai AL, Kulmacz RJ, Palmer G. Spectroscopic evidence for reaction of prostaglandin H synthase-1 tyrosyl radical with arachidonic acid Journal of Biological Chemistry. 270: 10503-10508. PMID 7737984 DOI: 10.1074/Jbc.270.18.10503 |
0.319 |
|
1994 |
Palmer G, Esposti MD. Application of exciton coupling theory to the structure of mitochondrial cytochrome b Biochemistry. 33: 176-185. PMID 8286337 DOI: 10.1021/Bi00167A023 |
0.303 |
|
1994 |
Kulmacz RJ, Palmer G, Wei C, Tsai AL. Reaction and free radical kinetics of prostaglandin H synthase with manganese protoporphyrin IX as the prosthetic group Biochemistry. 33: 5428-5439. PMID 8180166 DOI: 10.1021/Bi00184A011 |
0.337 |
|
1993 |
Day EP, Peterson J, Sendova MS, Schoonover J, Palmer G. Magnetization of fast and slow oxidized cytochrome c oxidase Biochemistry. 32: 7855-7860. PMID 8394118 DOI: 10.1021/Bi00082A003 |
0.355 |
|
1993 |
Palmer G. Current issues in the chemistry of cytochrome c oxidase Journal of Bioenergetics and Biomembranes. 25: 145-151. PMID 8389747 DOI: 10.1007/Bf00762856 |
0.339 |
|
1993 |
Li W, Palmer G. Spectroscopic characterization of the interaction of azide and thiocyanate with the binuclear center of cytochrome oxidase: Evidence for multiple ligand sites Biochemistry. 32: 1833-1843. PMID 8382524 DOI: 10.1021/Bi00058A018 |
0.308 |
|
1993 |
Fato R, Cavazzoni M, Castellucio C, Parenti Castelli G, Palmer G, Degli Esposti M, Lenaz G. Steady-state kinetics of ubiquinol-cytochrome c reductase in bovine heart submitochondrial particles: Diffusional effects Biochemical Journal. 290: 225-236. PMID 8382478 DOI: 10.1042/Bj2900225 |
0.341 |
|
1991 |
Kulmacz RJ, Palmer G, Tsai AL. Prostaglandin H synthase: Perturbation of the tyrosyl radical as a probe of anticyclooxygenase agents Molecular Pharmacology. 40: 833-837. PMID 1658613 DOI: 10.1007/978-1-4899-0727-1_38 |
0.308 |
|
1991 |
Palmer G. Reaction of formate with the fast form of cytochrome oxidase: A model for the fast to slow conversion Biochemistry®. 30: 7541-7550. PMID 1649633 DOI: 10.1021/Bi00244A025 |
0.393 |
|
1991 |
Palmer G, Reedijk J. Nonmenclature of electron-transfer proteins. Recommendations 1989 Bba - Bioenergetics. 1060: vii-xix. DOI: 10.1016/S0005-2728(05)80311-1 |
0.311 |
|
1990 |
Kulmacz RJ, Ren Y, Tsai AL, Palmer G. Prostaglandin H synthase: Spectroscopic studies of the interaction with hydroperoxides and with indomethacin Biochemistry. 29: 8760-8771. PMID 2176834 DOI: 10.1021/Bi00489A037 |
0.369 |
|
1989 |
Myers D, Palmer G. The kinetic mechanism(s) of cytochrome oxidase. Techniques for their analysis and criteria for their validation Annals of the New York Academy of Sciences. 550: 85-97. PMID 2854414 DOI: 10.1111/J.1749-6632.1988.Tb35325.X |
0.314 |
|
1989 |
Simpkin D, Palmer G, Devlin FJ, McKenna MC, Jensen GM, Stephens PJ. The axial ligands of heme in cytochromes: a near-infrared magnetic circular dichroism study of yeast cytochromes c, c1, and b and spinach cytochrome f. Biochemistry. 28: 8033-9. PMID 2557894 DOI: 10.1021/Bi00446A010 |
0.392 |
|
1989 |
Peterson J, Schoonover JR, Palmer G, Dat EP. Oxidized cyctochrome c oxidase: Saturation magnetization of ‘fast’ and ‘slow’ preparations Journal of Inorganic Biochemistry. 36: 266. DOI: 10.1016/0162-0134(89)84353-3 |
0.317 |
|
1988 |
Gaul DF, Davidson MW, Palmer G, Shaw RW, Knaff DB. Spectroscopic and ligand-binding properties of an oxygen-binding heme protein from Chromatium vinosum Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 953: 226-231. PMID 3355839 DOI: 10.1016/0167-4838(88)90029-5 |
0.336 |
|
1988 |
Schoonover JR, Dyer RB, Woodruff WH, Baker GM, Noguchi M, Palmer G. A comparison of the resonance Raman properties of the fast and slow forms of cytochrome oxidase Biochemistry. 27: 5433-5440. PMID 2846036 DOI: 10.1021/Bi00415A008 |
0.359 |
|
1988 |
Hartzell CR, Beinert H, Babcock GT, Chan SI, Palmer G, Scott RA. Heterogeneity in an isolated membrane protein. Has the 'authentic cytochrome oxidase' been identified? Febs Letters. 236: 1-4. PMID 2841158 DOI: 10.1016/0014-5793(88)80273-4 |
0.604 |
|
1987 |
Baker GM, Palmer G. Effect of high pH on the spectral and catalytic properties of beef heart cytochrome oxidase. Biochemistry. 26: 3038-44. PMID 3038174 DOI: 10.1021/Bi00385A014 |
0.358 |
|
1987 |
Telser J, Hoffman BM, LoBrutto R, Ohnishi T, Tsai AL, Simpkin D, Palmer G. Evidence for N coordination to Fe in the [2Fe-2S] center in yeast mitochondrial complex III Comparison with similar findings for analogous bacterial [2Fe-2S] proteins Febs Letters. 214: 117-121. PMID 3032676 DOI: 10.1016/0014-5793(87)80024-8 |
0.322 |
|
1987 |
Gaul DF, Ondrias MR, Findsen EW, Palmer G, Olson JS, Davidson MW, Knaff DB. Spectroscopic and kinetic properties of an oxygen-binding heme protein from Chromatium vinosum Journal of Biological Chemistry. 262: 1144-1147. PMID 3027081 |
0.613 |
|
1986 |
Degli Esposti M, Tsai AL, Palmer G, Lenaz G. On the oxidation pathways of the mitochondrial bc1 complex from beef heart. Effects of various inhibitors European Journal of Biochemistry. 160: 547-555. PMID 3023079 DOI: 10.1111/J.1432-1033.1986.Tb10073.X |
0.361 |
|
1986 |
Yu L, Yang FD, Yu CA, Tsai AL, Palmer G. Identification of ubiquinone-binding proteins in yeast mitochondrial ubiquinol-cytochrome c reductase using an azido-ubiquinone derivative. Biochimica Et Biophysica Acta. 848: 305-11. PMID 3004577 DOI: 10.1016/0005-2728(86)90204-5 |
0.325 |
|
1985 |
Babcock GT, Jean JM, Johnston LN, Woodruff WH, Palmer G. Flow-flash, time-resolved resonance Raman spectroscopy of the oxidation of reduced and of mixed valence cytochrome oxidase by dioxygen. Journal of Inorganic Biochemistry. 23: 243-51. PMID 2991463 DOI: 10.1016/0162-0134(85)85031-5 |
0.587 |
|
1985 |
Tsai AL, Kauten R, Palmer G. The interaction of yeast Complex III with some respiratory inhibitors. Biochimica Et Biophysica Acta. 806: 418-26. PMID 2982396 DOI: 10.1016/0005-2728(85)90249-X |
0.342 |
|
1984 |
Babcock GT, Jean JM, Johnston LN, Palmer G, Woodruff WH. Time-resolved resonance Raman spectroscopy of transient species formed during the oxidation of cytochrome oxidase by dioxygen Journal of the American Chemical Society. 106: 8305-8306. DOI: 10.1021/Ja00338A056 |
0.573 |
|
1983 |
T'sai AL, Palmer G. Potentiometric studies on yeast complex III. Biochimica Et Biophysica Acta. 722: 349-63. PMID 6301554 DOI: 10.1016/0005-2728(83)90083-X |
0.312 |
|
1983 |
Palmer G, Carithers R, Carter K, Kojima N, Young L, Kent T, Münck E. Aspects of the chemistry of the two heme centers of cytochrome oxide Inorganica Chimica Acta. 79: 74-75. DOI: 10.1016/S0020-1693(00)95104-1 |
0.363 |
|
1983 |
Hosein B, Palmer G. The kinetics and mechanism of oxidation of reduced spinach ferredoxin by molecular oxygen and its reduced products Biochimica Et Biophysica Acta. 723: 383-390. DOI: 10.1016/0005-2728(83)90045-2 |
0.308 |
|
1982 |
T'sai AL, Palmer G. Purification and characterization of highly purified cytochrome b from complex III of baker's yeast. Biochimica Et Biophysica Acta. 681: 484-95. PMID 6289886 DOI: 10.1016/0005-2728(82)90191-8 |
0.346 |
|
1982 |
de la Rosa FF, Palmer G. Anomalous reduction of cytochrome b in highly purified complex III from baker's yeast. Zeitschrift Fur Naturforschung. Section C, Biosciences. 37: 445-7. PMID 6287753 DOI: 10.1515/Znc-1982-5-615 |
0.338 |
|
1982 |
Siedow JN, Miller S, Palmer G. The partially reduced species present in purified cytochrome oxidase from baker's yeast is cytochrome a. Journal of Bioenergetics and Biomembranes. 13: 171-9. PMID 6273396 DOI: 10.1007/Bf00763838 |
0.379 |
|
1981 |
Carter KR, Antalis TM, Palmer G, Ferris NS, Woodruff WH. Spectroscopic characterization of compound C and related derivatives of cytochrome oxidase Proceedings of the National Academy of Sciences of the United States of America. 78: 1652-1655. PMID 6262822 DOI: 10.1073/Pnas.78.3.1652 |
0.629 |
|
1981 |
Woodruff WH, Dallinger RF, Antalis TM, Palmer G. Resonance Raman spectroscopy of cytochrome oxidase using Soret excitation: selective enhancement, indicator bands, and structural significance for cytochromes a and a3. Biochemistry. 20: 1332-8. PMID 6261789 DOI: 10.1021/Bi00508A045 |
0.63 |
|
1980 |
Mackler B, Haynes B, Person R, Palmer G. Electron transport systems of Candida utilis: purification and properties of the respiratory chain-linked external NADH dehydrogenase. Biochimica Et Biophysica Acta. 591: 289-97. PMID 7190438 DOI: 10.1016/0005-2728(80)90160-7 |
0.345 |
|
1980 |
Power S, Palmer G. Electron transfer reactions of cytochrome c confined within erythrocyte ghosts Bba - Bioenergetics. 593: 400-413. PMID 6263324 DOI: 10.1016/0005-2728(80)90076-6 |
0.35 |
|
1978 |
Beinert H, Orme-Johnson WH, Palmer G. Special techniques for the preparation of samples for low-temperature EPR spectroscopy. Methods in Enzymology. 54: 111-32. PMID 215872 DOI: 10.1016/S0076-6879(78)54013-5 |
0.669 |
|
1978 |
Palmer G. [16] Complex III from bakers' yeast Methods in Enzymology. 53: 113-121. PMID 213674 DOI: 10.1016/S0076-6879(78)53019-X |
0.369 |
|
1978 |
Babcock GT, Vickery LE, Palmer G. The electronic state of heme in cytochrome oxidase II. Oxidation-reduction potential interactions and heme iron spin state behavior observed in reductive titrations. The Journal of Biological Chemistry. 253: 2400-11. PMID 204649 |
0.528 |
|
1978 |
Vickery LE, Palmer G, Wharton DC. Heme c - heme d1 interaction in Pseudomonas cytochrome oxidase (nitrite reductase): A reappraisal of the spectroscopic evidence Biochemical and Biophysical Research Communications. 80: 458-463. PMID 203287 DOI: 10.1016/0006-291X(78)90699-X |
0.374 |
|
1976 |
Babcock GT, Vickery LE, Palmer G. Electronic state of heme in cytochrome oxidase. I. Magnetic circular dichroism of the isolated enzyme and its derivatives. The Journal of Biological Chemistry. 251: 7907-19. PMID 187599 |
0.534 |
|
1976 |
Chen JS, Mortenson LE, Palmer G. The iron-sulfur centers and the function of hydrogenase from Clostridium pasteurianum. Advances in Experimental Medicine and Biology. 74: 68-82. PMID 183483 DOI: 10.1007/978-1-4684-3270-1_6 |
0.337 |
|
1976 |
Yamamoto T, Palmer G, Crespi H. Resonance raman studies of a c type algal cytochrome. Deuterium shifts and a comparison with mammalian cytochrome c. Biochimica Et Biophysica Acta. 439: 232-9. PMID 182237 DOI: 10.1016/0005-2795(76)90178-1 |
0.373 |
|
1976 |
Palmer G, Babcock GT, Vickery LE. A model for cytochrome oxidase. Proceedings of the National Academy of Sciences of the United States of America. 73: 2206-10. PMID 181747 DOI: 10.1073/Pnas.73.7.2206 |
0.585 |
|
1975 |
Strickland S, Palmer G, Massey V. Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data. The Journal of Biological Chemistry. 250: 4048-52. PMID 1126943 |
0.446 |
|
1975 |
Power SD, Choucair A, Palmer G. Is lysine 79 a ligand for iron hexacyanides bound to cytochrome c? Biochemical and Biophysical Research Communications. 66: 103-7. PMID 240356 DOI: 10.1016/S0006-291X(75)80300-7 |
0.305 |
|
1974 |
Olson JS, Ballou DP, Palmer G, Massey V. The mechanism of action of xanthine oxidase. The Journal of Biological Chemistry. 249: 4363-82. PMID 4367215 |
0.647 |
|
1974 |
Olson JS, Ballow DP, Palmer G, Massey V. The reaction of xanthine oxidase with molecular oxygen. The Journal of Biological Chemistry. 249: 4350-62. PMID 4367214 |
0.573 |
|
1974 |
Ballou DP, Palmer GA. Practical rapid quenching instrument for the study of reaction mechanisms by electron paramagnetic resonance spectroscopy Analytical Chemistry. 46: 1248-1253. DOI: 10.1021/Ac60345A034 |
0.542 |
|
1973 |
Edmondson D, Ballou D, Van Heuvelen A, Palmer G, Massey V. Kinetic studies on the substrate reduction of xanthine oxidase. The Journal of Biological Chemistry. 248: 6135-44. PMID 4353632 |
0.45 |
|
1973 |
Salmeen I, Rimai L, Gill D, Yamamoto T, Palmer G, Hartzell CR, Beinert H. Resonance Raman spectroscopy of cytochrome c oxidase and electron transport particles with excitation near the Soret band. Biochemical and Biophysical Research Communications. 52: 1100-7. PMID 4351046 DOI: 10.1016/0006-291X(73)91051-6 |
0.58 |
|
1973 |
Mortenson LE, Zumpft WG, Palmer G. Electron paramagnetic resonance studies on nitrogenase. 3. Function of magnesium adenosine 5'-triphosphate and adenosine 5'-diphosphate in catalysis by nitrogenase. Biochimica Et Biophysica Acta. 292: 422-35. PMID 4349920 DOI: 10.1016/0005-2728(73)90048-0 |
0.364 |
|
1973 |
Zumft WG, Palmer G, Mortenson LE. Electron paramagnetic resonance studies on nitrogenase. II. Interaction of adenosine 5'-triphosphate with azoferredoxin. Biochimica Et Biophysica Acta. 292: 413-21. PMID 4349919 DOI: 10.1016/0005-2728(73)90047-9 |
0.324 |
|
1972 |
Salmeen I, Palmer G. Contact-shifted NMR of spinach ferredoxin: additional resonances and partial assignments. Archives of Biochemistry and Biophysics. 150: 767-73. PMID 5044052 DOI: 10.1016/0003-9861(72)90096-3 |
0.392 |
|
1972 |
Massey V, Edmondson D, Palmer G, Beacham LM, Elion GB. The separation of functional and non-functional xanthine oxidase by affinity chromatography. The Biochemical Journal. 127: 10P-11P. PMID 4672853 DOI: 10.1042/Bj1270010P |
0.453 |
|
1972 |
Palmer G, Multani JS, Cretney WC, Zumft WG, Mortenson LE. Electron paramagnetic resonance studies on nitrogenase. I. The properties of molybdoferredoxin and azoferredoxin. Archives of Biochemistry and Biophysics. 153: 325-332. PMID 4346635 DOI: 10.1016/0003-9861(72)90452-3 |
0.316 |
|
1972 |
Zumft WG, Cretney WC, Huang TC, Mortenson LE, Palmer G. On the structure and function of nitrogenase from Clostridium pasteurianum W5. Biochemical and Biophysical Research Communications. 48: 1525-32. PMID 4342714 DOI: 10.1016/0006-291X(72)90887-X |
0.341 |
|
1972 |
Edmondson D, Massey V, Palmer G, Beacham LM, Elion GB. The resolution of active and inactive xanthine oxidase by affinity chromatography. The Journal of Biological Chemistry. 247: 1597-604. PMID 4335003 |
0.421 |
|
1971 |
Massey V, Williams CH, Palmer G. The presence of S degrees-containing impurities in commercial samples of oxidized glutathione and their catalytic effect on the reduction of cytochrome c. Biochemical and Biophysical Research Communications. 42: 730-8. PMID 5543955 DOI: 10.1016/0006-291X(71)90548-1 |
0.628 |
|
1971 |
Palmer G, Dunham WR, Fee JA, Sands RH, Iizuka T, Yonetani T. The magnetic susceptibility of spinach ferredoxin from 77-250°K: A measurement of the antiferromagnetic coupling between the two iron atoms Bba - Bioenergetics. 245: 201-207. PMID 5132472 DOI: 10.1016/0005-2728(71)90022-3 |
0.309 |
|
1971 |
Dunham WR, Palmer G, Sands RH, Bearden AJ, Beinert H, Orme-Johnson WH. Comments on "the interpretation of the EPR and Mössbauer spectra of two-iron, one-electron iron-sulfur proteins". Biochemical and Biophysical Research Communications. 45: 1119-26. PMID 4332592 DOI: 10.1016/0006-291X(71)90135-5 |
0.678 |
|
1971 |
Dunham WR, Palmer G, Sands RH, Bearden AJ. On the structure of the iron-sulfur complex in the two-iron ferredoxins. Biochimica Et Biophysica Acta. 253: 373-84. PMID 4332306 DOI: 10.1016/0005-2728(71)90041-7 |
0.322 |
|
1971 |
Fee JA, Palmer G. The properties of parsley ferredoxin and its selenium-containing homolog Bba - Bioenergetics. 245: 175-195. PMID 4332097 DOI: 10.1016/0005-2728(71)90020-X |
0.365 |
|
1971 |
Eaton WA, Palmer G, Fee JA, Kimura T, Lovenberg W. Tetrahedral iron in the active center of plant ferredoxins and beef adrenodoxin Proceedings of the National Academy of Sciences of the United States of America. 68: 3015-3020. PMID 4332004 DOI: 10.1073/Pnas.68.12.3015 |
0.332 |
|
1971 |
Dunham WR, Bearden AJ, Salmeen IT, Palmer G, Sands RH, Orme-Johnson WH, Beinert H. The two-iron ferredoxins in spinach, parsley, pig adrenal cortex, Azotobacter vinelandii, and Clostridium pasteurianum: studies by magnetic field Mössbauer spectroscopy. Biochimica Et Biophysica Acta. 253: 134-52. PMID 4331269 DOI: 10.1016/0005-2728(71)90240-4 |
0.693 |
|
1971 |
Fritz J, Anderson R, Fee J, Palmer G, Sands RH, Tsibris JC, Gunsalus IC, Orme-Johnson WH, Beinert H. The iron electron-nuclear double resonance (ENDOR) of two-iron ferredoxins from spinach, parsley, pig adrenal cortex and Pseudomonas putida. Biochimica Et Biophysica Acta. 253: 110-33. PMID 4331268 DOI: 10.1016/0005-2728(71)90239-8 |
0.655 |
|
1970 |
Massey V, Komai H, Palmer G, Elion GB. On the mechanism of inactivation of xanthine oxidase by allopurinol and other pyrazolo[3,4-d]pyrimidines. The Journal of Biological Chemistry. 245: 2837-44. PMID 5467924 |
0.398 |
|
1970 |
Massey V, Komai H, Palmer G, Elion GB. The existence of nonfunctional active sites in milk xanthine oxidase: reaction with functional active site inhibitors. Vitamins and Hormones. 28: 505-31. PMID 4335890 DOI: 10.1016/S0083-6729(08)60909-7 |
0.443 |
|
1970 |
Müller F, Hemmerich P, Ehrenberg A, Palmer G, Massey V. The chemical and electronic structure of the neutral flavin radical as revealed by electron spin resonance spectroscopy of chemically and isotopically substituted derivatives. European Journal of Biochemistry / Febs. 14: 185-96. PMID 4315843 DOI: 10.1111/J.1432-1033.1970.Tb00277.X |
0.541 |
|
1969 |
Ballou D, Palmer G, Massey V. Direct demonstration of superoxide anion production during the oxidation of reduced flavin and of its catalytic decomposition by erythrocuprein. Biochemical and Biophysical Research Communications. 36: 898-904. PMID 4310146 DOI: 10.1016/0006-291X(69)90288-5 |
0.659 |
|
1969 |
Palmer G, Massey V. Electron paramagnetic resonance and circular dichroism studies on milk xanthine oxidase. The Journal of Biological Chemistry. 244: 2614-20. PMID 4306032 |
0.53 |
|
1969 |
Komai H, Massey V, Palmer G. The preparation and properties of deflavo xanthine oxidase. The Journal of Biological Chemistry. 244: 1692-700. PMID 4305460 |
0.42 |
|
1968 |
Rajagopalan KV, Handler P, Palmer G, Beinert H. Studies of aldehyde oxidase by electron paramagnetic resonance spectroscopy. II. Kinetic studies by rapid freezing. The Journal of Biological Chemistry. 243: 3797-806. PMID 4298513 |
0.553 |
|
1968 |
Rajagopalan KV, Handler P, Palmer G, Beinert H. Studies of aldehyde oxidase by electron paramagnetic resonance spectroscopy. I. Spectra at equilibrium states. The Journal of Biological Chemistry. 243: 3784-96. PMID 4298512 |
0.554 |
|
1968 |
Aleman V, Handler P, Palmer G, Beinert H. Studies on dihydroorotate dehydrogenase by electron paramagnetic resonance spectroscopy. 3. Kinetic studies by rapid freezing. The Journal of Biological Chemistry. 243: 2569-78. PMID 4297264 |
0.771 |
|
1968 |
Aleman V, Handler P, Palmer G, Beinert H. Studies on dihydroorotate dehydrogenase by electron paramagnetic resonance spectroscopy. II. Electron paramagnetic resonance and optical spectra and titrations. The Journal of Biological Chemistry. 243: 2560-8. PMID 4297263 |
0.764 |
|
1968 |
Salmeen I, Palmer G. Electron Paramagnetic Resonance of Beef‐Heart Ferricytochrome c Journal of Chemical Physics. 48: 2049-2052. PMID 4297179 DOI: 10.1063/1.1669014 |
0.32 |
|
1968 |
Mackler B, Erickson RJ, Davis SD, Mehl TD, Sharp C, Wedgwood RJ, Palmer G, King TE. Studies of the electron transport systems of heart muscle: biochemical and antigenic properties of a soluble DPNH dehydrogenase. Archives of Biochemistry and Biophysics. 125: 40-5. PMID 4296959 DOI: 10.1016/0003-9861(68)90636-X |
0.384 |
|
1968 |
Palmer G, Horgan DJ, Tisdale H, Singer TP, Beinert H. Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. XIV. Location of the sites of inhibition of rotenone, barbiturates, and piericidin by means of electron paramagnetic resonance spectroscopy. The Journal of Biological Chemistry. 243: 844-7. PMID 4295607 |
0.528 |
|
1968 |
Palmer G, Mackler B, Duncan HM. Electron paramagnetic resonance studies on the cytochrome oxidase from yeast. Biochimica Et Biophysica Acta. 143: 636-8. PMID 4294895 DOI: 10.1016/0005-2728(67)90072-2 |
0.412 |
|
1968 |
Salmeen I, Palmer G. Erratum: Electron Paramagnetic Resonance of Beef Heart Ferricytochrome c Journal of Chemical Physics. 48: 4331-4331. DOI: 10.1063/1.1669788 |
0.351 |
|
1967 |
Zand R, Palmer G. Ultraviolet, visible, circular dichroism, and electron paramagnetic resonance spectra of the copper (II) complexes of thyroxine and thyroxine analogs. Biochemistry. 6: 999-1007. PMID 4291764 DOI: 10.1021/Bi00856A007 |
0.38 |
|
1966 |
Massey V, Palmer G. On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones. Biochemistry. 5: 3181-9. PMID 4382016 DOI: 10.1021/Bi00874A016 |
0.461 |
|
1966 |
Palmer G, Brintzinger H. Nature of the non-haem iron in ferredoxin and rubredoxin [23] Nature. 211: 189-190. PMID 4290604 DOI: 10.1038/211189A0 |
0.306 |
|
1966 |
Palmer G, Sands RH, Mortenson LE. Electron paramagnetic resonance studies on the ferredoxin from Clostridiumpasteurianum Biochemical and Biophysical Research Communications. 23: 357-362. PMID 4289757 DOI: 10.1016/0006-291X(66)90733-9 |
0.344 |
|
1966 |
Brintzinger H, Palmer G, Sands RH. An electron paramagnetic resonance study of metal-aromatic bonding in bis(hexamethylbenzene)iron(I) [17] Journal of the American Chemical Society. 88: 623. DOI: 10.1021/Ja00955A053 |
0.348 |
|
1965 |
Beinert H, Palmer G. Contributions of EPR spectroscopy to our knowledge of oxidative enzymes. Advances in Enzymology and Related Areas of Molecular Biology. 27: 105-98. PMID 4303031 DOI: 10.1002/9780470122723.Ch3 |
0.556 |
|
1964 |
BRAY RC, PALMER G, BEINERT H. DIRECT STUDIES ON THE ELECTRON TRANSFER SEQUENCE IN XANTHINE OXIDASE BY ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY. II. KINETIC STUDIES EMPLOYING RAPID FREEZING. The Journal of Biological Chemistry. 239: 2667-76. PMID 14235551 |
0.542 |
|
1964 |
PALMER G, BRAY RC, BEINERT H. DIRECT STUDIES ON THE ELECTRON TRANSFER SEQUENCE IN XANTHINE OXIDASE BY ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY. I. TECHNIQUES AND DESCRIPTION OF SPECTRA. The Journal of Biological Chemistry. 239: 2657-66. PMID 14235550 |
0.542 |
|
1964 |
PALMER G, BEINERT H. DIFFUSE REFLECTANCE SPECTROSCOPY OF FROZEN SAMPLES AS AN ADJUNCT TO LOW-TEMPERATURE ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY. Analytical Biochemistry. 8: 95-103. PMID 14167279 DOI: 10.1016/0003-2697(64)90172-1 |
0.515 |
|
1964 |
BEINERT H, PALMER G. OXIDATION-REDUCTION OF THE COPPER COMPONENT OF CYTOCHROME OXIDASE. KINETIC STUDIES WITH A RAPID FREEZING TECHNIQUE. The Journal of Biological Chemistry. 239: 1221-7. PMID 14165930 |
0.491 |
|
1963 |
BEINERT H, PALMER G, CREMONA T, SINGER TP. CORRELATION OF ENZYMATIC ACTIVITY AND THE APPEARANCE OF THE EPR SIGNAL AT G = 1.94 IN NADH DEHYDROGENASE AND ITS THERMAL BREAKDOWN PRODUCTS. Biochemical and Biophysical Research Communications. 12: 432-8. PMID 14068479 DOI: 10.1016/0006-291X(63)90310-3 |
0.439 |
|
1962 |
RAJAGOPALAN KV, ALEMAN V, HANDLER P, HEINEN W, PALMER G, BEINERT H. Electron paramagnetic resonance studies of iron reduction and semiquinone formation in metalloflavoproteins. Biochemical and Biophysical Research Communications. 8: 220-6. PMID 14489969 DOI: 10.1016/0006-291X(62)90267-X |
0.766 |
|
1962 |
PALMER G, MASSEY V. On the sulphydryl groups of lipoamide dehydrogenase. Biochimica Et Biophysica Acta. 58: 349-50. PMID 14483404 DOI: 10.1016/0006-3002(62)91019-3 |
0.447 |
|
1962 |
MASSEY V, PALMER G. Charge transfer complexes of lipoyl dehydrogenase and free flavins. The Journal of Biological Chemistry. 237: 2347-58. PMID 14470919 |
0.408 |
|
1962 |
BEINERT H, HEINEN W, PALMER G. Applications of combined low temperature optical and electron paramagnetic resonance spectroscopy to the study of oxidative enzymes. Brookhaven Symposia in Biology. 15: 229-65. PMID 13970331 |
0.546 |
|
1962 |
NICHOLAS DJ, WILSON PW, HEINEN W, PALMER G, BEINERT H. Use of electron paramagnetic resonance spectroscopy in investigations of functional metal components in micro-organisms. Nature. 196: 433-6. PMID 13938326 DOI: 10.1038/196433A0 |
0.494 |
|
1962 |
MASSEY V, HOFMANN T, PALMER G. The relation of function and structure in lipoyl dehydrogenase. The Journal of Biological Chemistry. 237: 3820-8. PMID 13933422 |
0.383 |
|
1961 |
MASSEY V, PALMER G, BENNETT R. The purification and some properties of D-amino acid oxidase. Biochimica Et Biophysica Acta. 48: 1-9. PMID 13767909 |
0.384 |
|
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