Jack Peisach - Publications

Affiliations: 
Physiology & Biophysics Albert Einstein College of Medicine, New York, New York, United States 
Website:
http://www.einstein.yu.edu/faculty/669/jack-peisach/

244 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
2014 Mazzarella L, Merlino A, Vitagliano L, Verde C, Di Prisco G, Peisach J, Vergara A. Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin Rsc Advances. 4: 25852-25856. DOI: 10.1039/c4ra03317e  1
2010 Hirota S, Tanaka N, Micetic I, Di Muro P, Nagao S, Kitagishi H, Kano K, Magliozzo RS, Peisach J, Beltramini M, Bubacco L. Structural basis of the lactate-dependent allosteric regulation of oxygen binding in arthropod hemocyanin. The Journal of Biological Chemistry. 285: 19338-45. PMID 20406810 DOI: 10.1074/jbc.M109.076067  1
2009 Vergara A, Franzese M, Merlino A, Bonomi G, Verde C, Giordano D, di Prisco G, Lee HC, Peisach J, Mazzarella L. Correlation between hemichrome stability and the root effect in tetrameric hemoglobins. Biophysical Journal. 97: 866-74. PMID 19651045 DOI: 10.1016/j.bpj.2009.04.056  1
2009 Colaneri MJ, Vitali J, Peisach J. Aspects of structure and bonding in copper-amino acid complexes revealed by single-crystal EPR/ENDOR spectroscopy and density functional calculations. The Journal of Physical Chemistry. A. 113: 5700-9. PMID 19378965 DOI: 10.1021/jp811249s  1
2008 Hirota S, Kawahara T, Beltramini M, Di Muro P, Magliozzo RS, Peisach J, Powers LS, Tanaka N, Nagao S, Bubacco L. Molecular basis of the Bohr effect in arthropod hemocyanin. The Journal of Biological Chemistry. 283: 31941-8. PMID 18725416 DOI: 10.1074/jbc.M803433200  1
2007 Giordano D, Vergara A, Lee HC, Peisach J, Balestrieri M, Mazzarella L, Parisi E, di Prisco G, Verde C. Hemoglobin structure/function and globin-gene evolution in the Arctic fish Liparis tunicatus. Gene. 406: 58-68. PMID 17618067 DOI: 10.1016/j.gene.2007.06.002  1
2007 Vergara A, Franzese M, Merlino A, Vitagliano L, Verde C, di Prisco G, Lee HC, Peisach J, Mazzarella L. Structural characterization of ferric hemoglobins from three antarctic fish species of the suborder notothenioidei. Biophysical Journal. 93: 2822-9. PMID 17545238 DOI: 10.1529/biophysj.107.105700  1
2005 Chattopadhyay M, Walter ED, Newell DJ, Jackson PJ, Aronoff-Spencer E, Peisach J, Gerfen GJ, Bennett B, Antholine WE, Millhauser GL. The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4. Journal of the American Chemical Society. 127: 12647-56. PMID 16144413 DOI: 10.1021/ja053254z  1
2003 Burns CS, Aronoff-Spencer E, Legname G, Prusiner SB, Antholine WE, Gerfen GJ, Peisach J, Millhauser GL. Copper coordination in the full-length, recombinant prion protein. Biochemistry. 42: 6794-803. PMID 12779334 DOI: 10.1021/bi027138+  1
2003 Peisach J. An appreciation of William H. Orme-Johnson III. Journal of Inorganic Biochemistry. 93: 6-10. PMID 12538047  1
2002 Legler PM, Lee HC, Peisach J, Mildvan AS. Kinetic and magnetic resonance studies of the role of metal ions in the mechanism of Escherichia coli GDP-mannose mannosyl hydrolase, an unusual nudix enzyme. Biochemistry. 41: 4655-68. PMID 11926828 DOI: 10.1021/bi012118d  1
2002 Burns CS, Aronoff-Spencer E, Dunham CM, Lario P, Avdievich NI, Antholine WE, Olmstead MM, Vrielink A, Gerfen GJ, Peisach J, Scott WG, Millhauser GL. Molecular features of the copper binding sites in the octarepeat domain of the prion protein. Biochemistry. 41: 3991-4001. PMID 11900542 DOI: 10.1021/bi011922x  1
2000 Aronoff-Spencer E, Burns CS, Avdievich NI, Gerfen GJ, Peisach J, Antholine WE, Ball HL, Cohen FE, Prusiner SB, Millhauser GL. Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy. Biochemistry. 39: 13760-71. PMID 11076515 DOI: 10.1021/bi001472t  1
2000 Lee HC, Goroncy AK, Peisach J, Cavada BS, Grangeiro TB, Ramos MV, Sampaio AH, Dam TK, Brewer CF. Demonstration of a conserved histidine and two water ligands at the Mn2+ site in Diocleinae lectins by pulsed EPR spectroscopy. Biochemistry. 39: 2340-6. PMID 10694401 DOI: 10.1021/bi992102b  1
2000 Colaneri MJ, Vitali J, Peisach J. Electron spin-echo envelope modulation study of multicrystalline Cu(2+)-insulin: effects of Cd(2+) on the nuclear quadrupole interaction of the Cu(2+)-coordinated imidazole remote nitrogen. Biochemistry. 39: 584-91. PMID 10642183 DOI: 10.1021/bi991613v  1
1999 Das TK, Couture M, Lee HC, Peisach J, Rousseau DL, Wittenberg BA, Wittenberg JB, Guertin M. Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: evidence for ligation of tyrosine-63 (B10) to the heme. Biochemistry. 38: 15360-8. PMID 10563822 DOI: 10.1021/bi991237e  1
1999 Couture M, Das TK, Lee HC, Peisach J, Rousseau DL, Wittenberg BA, Wittenberg JB, Guertin M. Chlamydomonas chloroplast ferrous hemoglobin. Heme pocket structure and reactions with ligands. The Journal of Biological Chemistry. 274: 6898-910. PMID 10066743 DOI: 10.1074/jbc.274.11.6898  1
1999 Das TK, Lee HC, Duff SM, Hill RD, Peisach J, Rousseau DL, Wittenberg BA, Wittenberg JB. The heme environment in barley hemoglobin. The Journal of Biological Chemistry. 274: 4207-12. PMID 9933618 DOI: 10.1074/jbc.274.7.4207  1
1999 Lippai I, Magliozzo RS, Peisach J. EPR spectroscopic reinvestigation of the activation of iron complexes of PMAH as a bleomycin model Journal of the American Chemical Society. 121: 780-784. DOI: 10.1021/ja980458p  1
1998 Sam JW, Takahashi S, Lippai I, Peisach J, Rousseau DL. Sequence-specific changes in the metal site of ferric bleomycin induced by the binding of DNA. The Journal of Biological Chemistry. 273: 16090-7. PMID 9632661 DOI: 10.1074/jbc.273.26.16090  1
1998 Reddy SG, Wong KK, Parast CV, Peisach J, Magliozzo RS, Kozarich JW. Dioxygen inactivation of pyruvate formate-lyase: EPR evidence for the formation of protein-based sulfinyl and peroxyl radicals. Biochemistry. 37: 558-63. PMID 9425077 DOI: 10.1021/bi972086n  1
1998 Bender CJ, Peisach J. Electron spin-echo modulation spectroscopic study of the type I copper center associated with stellacyanin from Rhus vernicifera: Examination of the graphical analysis of ESEEM spectra for two dissimilar weakly coupled 14N nuclei Journal of the Chemical Society - Faraday Transactions. 94: 375-386. DOI: 10.1039/A706120J  1
1997 Bender CJ, Casimiro DR, Peisach J, Jane Dyson H. Electron spin echo modulation study of the Type I copper protein rusticyanin and its mutant variant His85Ala Implications for the general analysis of weak14N superhyperfine interactions Journal of the Chemical Society - Faraday Transactions. 93: 3967-3980. DOI: 10.1039/A704541G  1
1997 Lee HC, Scheuring E, Peisach J, Chance MR. Electron spin echo envelope modulation and extended X-ray absorption fine structure studies of active site models of oxygenated cobalt-substituted hemoproteins: Correlating electron-nuclear couplings and metal-ligand bond lengths Journal of the American Chemical Society. 119: 12201-12209. DOI: 10.1021/ja9717166  1
1996 Lu Y, Roe JA, Bender CJ, Peisach J, Banci L, Bertini I, Gralla EB, Valentine JS. New Type 2 Copper-Cysteinate Proteins. Copper Site Histidine-to-Cysteine Mutants of Yeast Copper-Zinc Superoxide Dismutase. Inorganic Chemistry. 35: 1692-1700. PMID 11666393 DOI: 10.1021/ic9513189  1
1996 Bubacco L, Magliozzo RS, Beltramini M, Peisach J, Salvato B. Nitrite Reductase Activity of Deoxy Carcinus maenas Hemocyanin: Formation of the Half-Met Derivative. Inorganic Chemistry. 35: 1393-1394. PMID 11666340  1
1996 Nersissian AM, Mehrabian ZB, Nalbandyan RM, Hart PJ, Fraczkiewicz G, Czernuszewicz RS, Bender CJ, Peisach J, Herrmann RG, Valentine JS. Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form. Protein Science : a Publication of the Protein Society. 5: 2184-92. PMID 8931137 DOI: 10.1002/pro.5560051105  1
1996 Tipton PA, Quinn TP, Peisach J, Cook PF. Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex. Protein Science : a Publication of the Protein Society. 5: 1648-54. PMID 8844853 DOI: 10.1002/pro.5560050818  1
1996 Coffino AR, Peisach J. Simulation of Mn (II) EPR spectra using a full spin-Hamiltonian approach. Journal of Magnetic Resonance. Series B. 111: 127-34. PMID 8661270  1
1996 Hüber M, Bubacco L, Beltramini M, Salvato B, Elias H, Peisach J, Larsen E, Harnung SE, Haase W. Cobalt(II) Substituted Derivatives of Carcinus maenas Hemocyanin: Magnetic Characterization, Magnetooptic, and Kinetic Studies Regarding the Geometry of the Active Site Inorganic Chemistry. 35: 7482-7492.  1
1995 Parast CV, Wong KK, Lewisch SA, Kozarich JW, Peisach J, Magliozzo RS. Hydrogen exchange of the glycyl radical of pyruvate formate-lyase is catalyzed by cysteine 419. Biochemistry. 34: 2393-9. PMID 7873518 DOI: 10.1021/bi00008a001  1
1995 Bubacco L, Magliozzo RS, Wirt MD, Beltramini M, Salvato B, Peisach J. Structural characterization of mononuclear Cu(II) and its nitrite complex in the active site of Carcinus maenas hemocyanin. Biochemistry. 34: 1524-33. PMID 7849011 DOI: 10.1021/bi00005a008  1
1995 Bubacco L, Magliozzo RS, Wirt MD, Beltramini M, Salvato B, Peisach J. Structural characterization of mononuclear Cu(II) and its nitrite complex in the active site of Carcinus maenas hemocyanin. Biochemistry. 34: 1524-33. PMID 7849011 DOI: 10.1021/bi00005a008  1
1995 Magliozzo RS, Bubacco L, McCracken J, Jiang F, Beltramini M, Salvato B, Peisach J. Cu(II) coordination in arthropod and mollusk green half-methemocyanins analyzed by electron spin-echo envelope modulation spectroscopy. Biochemistry. 34: 1513-23. PMID 7849010 DOI: 10.1021/bi00005a007  1
1995 Lee HC, Peisach J, Tsuneshige A, Yonetani T. Electron spin echo envelope modulation study of oxygenated iron-cobalt hybrid hemoglobins reveals molecular features analogous to those of the oxy ferrous protein. Biochemistry. 34: 6883-91. PMID 7756320 DOI: 10.1021/bi00020a036  1
1995 Lee HC, Peisach J, Tsuneshige A, Yonetani T. Electron spin echo envelope modulation study of oxygenated iron-cobalt hybrid hemoglobins reveals molecular features analogous to those of the oxy ferrous protein. Biochemistry. 34: 6883-91. PMID 7756320 DOI: 10.1021/bi00020a036  1
1995 Parast CV, Wong KK, Kozarich JW, Peisach J, Magliozzo RS. Electron paramagnetic resonance evidence for a cysteine-based radical in pyruvate formate-lyase inactivated with mercaptopyruvate. Biochemistry. 34: 5712-7. PMID 7727431 DOI: 10.1021/bi00017a002  1
1995 Theodorakis JL, Garber EA, McCracken J, Peisach J, Schejter A, Margoliash E. A chemical modification of cytochrome-c lysines leading to changes in heme iron ligation. Biochimica Et Biophysica Acta. 1252: 103-13. PMID 7548152 DOI: 10.1016/0167-4838(95)00097-E  1
1995 Sam JW, Tang XJ, Magliozzo RS, Peisach J. Electrospray mass spectrometry of iron bleomycin II: Investigation of the reaction of Fe(III)-bleomycin with iodosylbenzene Journal of the American Chemical Society. 117: 1012-1018. DOI: 10.1021/ja00108a017  1
1995 Wirt MD, Bubacco L, Peisach J. Investigation of solid and solution structures of N-substituted Cu(II) salicyldimines by X-ray absorption spectroscopy Inorganic Chemistry. 34: 2377-2381.  1
1995 Wirt MD, Bender CJ, Peisach J. Electron spin echo envelope modulation (ESEEM) spectroscopy of cobalt(II) bis(dimethylglyoximes): Equatorial Co-N coupling parameters Inorganic Chemistry. 34: 1663-1667.  1
1995 Parast CV, Wong KK, Kozarich JW, Peisach J, Magliozzo RS. Mechanism-based inactivation of pyruvate formate-lyase by fluoropyruvate: Direct observation of an α-keto carbon radical Journal of the American Chemical Society. 117: 10601-10602.  1
1995 Colaneri MJ, Peisach J. A single crystal EPR and ESEEM analysis of Cu(II)-doped bis(L-histidinato)cadmium dihydrate Journal of the American Chemical Society. 117: 6308-6315.  1
1995 Crowder MW, Stewart JD, Roberts VA, Bender CJ, Tevelrakh E, Peisach J, Getzoff ED, Gaffney BJ, Benkovic SJ. Spectroscopic studies on the designed metal-binding sites of the 43C9 single chain antibody Journal of the American Chemical Society. 117: 5627-5634.  1
1994 Bender CJ, Rosenzweig AC, Lippard SJ, Peisach J. Nuclear hyperfine coupling of nitrogen in the coordination sphere of the diiron center of methane monooxygenase hydroxylase. The Journal of Biological Chemistry. 269: 15993-8. PMID 8206895  1
1994 Bender CJ, Rosenzweig AC, Lippard SJ, Peisach J. Nuclear hyperfine coupling of nitrogen in the coordination sphere of the diiron center of methane monooxygenase hydroxylase. The Journal of Biological Chemistry. 269: 15993-8. PMID 8206895  1
1994 Balasubramanian S, Carr RT, Bender CJ, Peisach J, Benkovic SJ. Identification of metal ligands in Cu(II)-inhibited Chromobacterium violaceum phenylalanine hydroxylase by electron spin echo envelope modulation analysis of histidine to serine mutations. Biochemistry. 33: 8532-7. PMID 8031788  1
1994 Lee HC, Peisach J, Dou Y, Ikeda-Saito M. Electron-nuclear coupling to the proximal histidine in oxy cobalt-substituted distal histidine mutants of human myoglobin. Biochemistry. 33: 7609-18. PMID 8011627 DOI: 10.1021/bi00190a014  1
1994 Sam JW, Tang XJ, Peisach J. Electrospray mass spectrometry of iron bleomycin: Demonstration that activated bleomycin is a ferric peroxide complex Journal of the American Chemical Society. 116: 5250-5256. DOI: 10.1021/ja00091a032  1
1994 Takahashi S, Sam JW, Peisach J, Rousseau DL. Structural characterization of iron-bleomycin by resonance Raman spectroscopy Journal of the American Chemical Society. 116: 4408-4413. DOI: 10.1021/ja00089a032  1
1994 Jiang F, Peisach J. Electron Spin Echo Envelope Modulation (ESEEM) study of CuII(dien)-pyrazole (dien = diethylenetriamine) and -pyridazine complexes Inorganic Chemistry. 33: 1348-1353.  1
1993 Magliozzo RS, Peisach J. Evaluation of nitrogen nuclear hyperfine and quadrupole coupling parameters for the proximal imidazole in myoglobin-azide, -cyanide, and -mercaptoethanol complexes by electron spin echo envelope modulation spectroscopy. Biochemistry. 32: 8446-56. PMID 8395204 DOI: 10.1021/bi00084a009  1
1993 Longa SD, Bianconi A, Palladino L, Simonelli B, Castellano AC, Borghi E, Barteri M, Beltramini M, Rocco GP, Salvato B, Bubacco L, Magliozzo RS, Peisach J. An x-ray absorption near edge structure spectroscopy study of metal coordination in Co(II)-substituted Carcinus maenas hemocyanin Biophysical Journal. 65: 2680-2691. PMID 8312502  1
1993 Balasubramanian S, Carr RT, Bender CJ, Peisach J, Benkovic SJ. Histidines 138 and 143 are copper binding ligands in Chromobacterium violaceum phenylalanine hydroxylase. Advances in Experimental Medicine and Biology. 338: 67-70. PMID 8304204  1
1993 Balasubramanian S, Carr RT, Bender CJ, Peisach J, Benkovic SJ. Histidines 138 and 143 are copper binding ligands in Chromobacterium violaceum phenylalanine hydroxylase. Advances in Experimental Medicine and Biology. 338: 67-70. PMID 8304204  1
1993 Salowe S, Bollinger JM, Ator M, Stubbe J, McCraken J, Peisach J, Samano MC, Robins MJ. Alternative model for mechanism-based inhibition of Escherichia coli ribonucleotide reductase by 2'-azido-2'-deoxyuridine 5'-diphosphate. Biochemistry. 32: 12749-60. PMID 8251496 DOI: 10.1021/bi00210a026  1
1993 Salowe S, Bollinger JM, Ator M, Stubbe J, McCraken J, Peisach J, Samano MC, Robins MJ. Alternative model for mechanism-based inhibition of Escherichia coli ribonucleotide reductase by 2'-azido-2'-deoxyuridine 5'-diphosphate. Biochemistry. 32: 12749-60. PMID 8251496 DOI: 10.1021/bi00210a026  1
1993 Van de Kamp M, Canters GW, Andrew CR, Sanders-Loehr J, Bender CJ, Peisach J. Effect of lysine ionization on the structure and electrochemical behaviour of the Met44-->Lys mutant of the blue-copper protein azurin from Pseudomonas aeruginosa. European Journal of Biochemistry / Febs. 218: 229-38. PMID 8243468 DOI: 10.1111/j.1432-1033.1993.tb18369.x  1
1993 Lee HC, Wittenberg JB, Peisach J. Role of hydrogen bonding to bound dioxygen in soybean leghemoglobin. Biochemistry. 32: 11500-6. PMID 8218216 DOI: 10.1021/bi00094a005  1
1993 Sam JW, Peisach J. EPR spectroscopic investigation of the lability of oxygen in activated bleomycin: implications for the mechanism of bleomycin-mediated DNA degradation. Biochemistry. 32: 1488-91. PMID 7679285  1
1993 Colaneri MJ, Peisach J. Enhanced Resolution of EPR Single-Crystal Spectral Parameters Using Field-Swept Electron Spin-Echo Spectroscopy Journal of Magnetic Resonance, Series A. 102: 360-363. DOI: 10.1006/jmra.1993.1118  1
1993 Lu Y, LaCroix LB, Lowery MD, Solomon EI, Bender CJ, Peisach J, Roe JA, Gralla EB, Valentine JS. Construction of a "blue" copper site at the native zinc site of yeast copper-zinc superoxide dismutase Journal of the American Chemical Society. 115: 5907-5918.  1
1993 Gurbiel RJ, Peoples R, Doan PE, Cline JF, McCracken J, Peisach J, Hoffman BM, Valentine JS. ENDOR and ESEEM investigation of AgI 2CuII 2 bovine superoxide dismutase Inorganic Chemistry. 32: 1813-1819.  1
1993 Jiang F, Karlin KD, Peisach J. An Electron Spin Echo Envelope Modulation (ESEEM) study of electron-nuclear hyperfine and nuclear quadrupole interactions of dz2 ground state copper(II) complexes with substituted imidazoles Inorganic Chemistry. 32: 2576-2582.  1
1993 Jiang F, Conry RR, Bubacco L, Tyeklár Z, Jacobson RR, Karlin KD, Peisach J. Crystal structure and electron spin echo envelope modulation study of [Cu(II)(TEPA)(NO2)]PF6 (TEPA = tris[2-(2-pyridyl)ethyl]amine): A model for the purported structure of the nitrite derivative of hemocyanin Journal of the American Chemical Society. 115: X-2101.  1
1992 Bubacco L, Magliozzo RS, Beltramini M, Salvato B, Peisach J. Preparation and spectroscopic characterization of a coupled binuclear center in cobalt(II)-substituted hemocyanin. Biochemistry. 31: 9294-303. PMID 1327111 DOI: 10.1021/bi00153a024  1
1992 Bubacco L, Magliozzo RS, Beltramini M, Salvato B, Peisach J. Preparation and spectroscopic characterization of a coupled binuclear center in cobalt(II)-substituted hemocyanin. Biochemistry. 31: 9294-303. PMID 1327111 DOI: 10.1021/bi00153a024  1
1992 Lee HC, Ikeda-Saito M, Yonetani T, Magliozzo RS, Peisach J. Hydrogen bonding to the bound dioxygen in oxy cobaltous myoglobin reduces the superhyperfine coupling to the proximal histidine. Biochemistry. 31: 7274-81. PMID 1324709 DOI: 10.1021/bi00147a010  1
1992 Lu J, Bender CJ, McCracken J, Peisach J, Severns JC, McMillin DR. Pulsed EPR studies of the type 2 copper binding site in the mercury derivative of laccase. Biochemistry. 31: 6265-72. PMID 1320933  1
1992 Magliozzo RS, Peisach J. Electron spin echo envelope modulation spectroscopic study of iron-nitrogen interactions in myoglobin hydroxide and Fe(III) tetraphenylporphyrin models. Biochemistry. 31: 189-99. PMID 1310029 DOI: 10.1021/bi00116a028  1
1992 Colaneri MJ, Peisach J. An electron spin-echo envelope modulation study of Cu(II)-doped single crystals of L-histidine hydrochloride monohydrate Journal of the American Chemical Society. 114: 5335-5341. DOI: 10.1021/ja00039a051  1
1992 Coffino AR, Peisach J. Nuclear modulation effects in high-spin electron systems with small zero-field splittings The Journal of Chemical Physics. 97: 3072-3091.  1
1992 Raitsimring A, Peisach J, Lee HC, Chen X. Measurement of distance distribution between spin labels in spin-labeled hemoglobin using an electron spin echo method Journal of Physical Chemistry. 96: 3526-3531.  1
1992 McCracken J, Peisach J, Cote CE, McGuirl MA, Dooley DM. Pulsed EPR studies of the semiquinone state of copper-containing amine oxidases Journal of the American Chemical Society. 114: 3715-3720.  1
1991 Zer H, Freedman JH, Peisach J, Chevion M. Inverse correlation between resistance towards copper and towards the redox-cycling compound paraquat: a study in copper-tolerant hepatocytes in tissue culture. Free Radical Biology & Medicine. 11: 9-16. PMID 1937132 DOI: 10.1016/0891-5849(91)90182-3  1
1991 McCracken J, Peisach J, Bhattacharyya L, Brewer F. Electron spin echo envelope modulation studies of lectins: evidence for a conserved Mn(2+)-binding site. Biochemistry. 30: 4486-91. PMID 1850625  1
1991 Tipton PA, Peisach J. Pulsed EPR analysis of tartrate dehydrogenase active-site complexes. Biochemistry. 30: 739-44. PMID 1846305  1
1991 Jiang F, Peisach J, Ming LJ, Que L, Chen VJ. Electron spin echo envelope modulation studies of the Cu(II)-substituted derivative of isopenicillin N synthase: a structural and spectroscopic model. Biochemistry. 30: 11437-45. PMID 1660301  1
1991 Cammack R, Chapman A, McCracken J, Peisach J. Electron spin-echo spectroscopy of the iron-sulphur clusters of xanthine oxidase from milk Journal of the Chemical Society, Faraday Transactions. 87: 3203-3206. DOI: 10.1039/FT9918703203  1
1990 Tipton PA, Peisach J. Characterization of the multiple catalytic activities of tartrate dehydrogenase. Biochemistry. 29: 1749-56. PMID 2184888  1
1990 Kraus DW, Wittenberg JB, Lu JF, Peisach J. Hemoglobins of the Lucina pectinata/bacteria symbiosis. II. An electron paramagnetic resonance and optical spectral study of the ferric proteins. The Journal of Biological Chemistry. 265: 16054-9. PMID 2168877  1
1990 Morgan TV, McCracken J, Orme-Johnson WH, Mims WB, Mortenson LE, Peisach J. Pulsed electron paramagnetic resonance studies of the interaction of Mg-ATP and D2O with the iron protein of nitrogenase. Biochemistry. 29: 3077-82. PMID 2159783  1
1990 Cornelius JB, McCracken J, Clarkson RB, Belford RL, Peisach J. Electron spin echo envelope modulation angle selection studies of axial pyridine coordination to copper(II) benzoylacetonate Journal of Physical Chemistry. 94: 6977-6982. DOI: 10.1021/j100381a013  1
1990 Mims WB, Dams JL, Peisach J. The exchange of hydrogen ions and of water molecules near the active site of cytochrome c Journal of Magnetic Resonance (1969). 86: 273-292. DOI: 10.1016/0022-2364(90)90260-G  1
1990 Colaneri MJ, Potenza JA, Schugar HJ, Peisach J. Single-crystal electron spin echo envelope modulation study of Cu(II)-doped zinc bis(1,2-dimethylimidazole) dichloride Journal of the American Chemical Society. 112: 9451-9458.  1
1990 Jiang F, McCracken J, Peisach J. Nuclear quadrupole interactions in copper(II)-diethylenetriamine-substituted imidazole complexes and in copper(II) proteins Journal of the American Chemical Society. 112: 9035-9044.  1
1989 Freedman JH, Ciriolo MR, Peisach J. The role of glutathione in copper metabolism and toxicity. The Journal of Biological Chemistry. 264: 5598-605. PMID 2564391  1
1989 Freedman JH, Peisach J. Intracellular copper transport in cultured hepatoma cells. Biochemical and Biophysical Research Communications. 164: 134-40. PMID 2553012 DOI: 10.1016/0006-291X(89)91693-8  1
1989 Tipton PA, McCracken J, Cornelius JB, Peisach J. Electron spin echo envelope modulation studies of pyruvate kinase active-site complexes. Biochemistry. 28: 5720-8. PMID 2550061  1
1989 Cunningham RP, Asahara H, Bank JF, Scholes CP, Salerno JC, Surerus K, Münck E, McCracken J, Peisach J, Emptage MH. Endonuclease III is an iron-sulfur protein. Biochemistry. 28: 4450-5. PMID 2548577 DOI: 10.1021/bi00436a049  1
1989 Freedman JH, Peisach J. Resistance of cultured hepatoma cells to copper toxicity. Purification and characterization of the hepatoma metallothionein. Biochimica Et Biophysica Acta. 992: 145-54. PMID 2547449 DOI: 10.1016/0304-4165(89)90003-2  1
1989 Cammack R, Kovacs KL, McCracken J, Peisach J. Spectroscopic characterization of the nickel and iron-sulphur clusters of hydrogenase from the purple photosynthetic bacterium Thiocapsa roseopersicina. 2. Electron spin-echo spectroscopy. European Journal of Biochemistry / Febs. 182: 363-6. PMID 2544425  1
1989 Salvato B, Giacometti GM, Beltramini M, Zilio F, Giacometti G, Magliozzo RS, Peisach J. The oxidation of Octopus vulgaris hemocyanin by nitrogen oxides. Biochemistry. 28: 680-4. PMID 2540804 DOI: 10.1021/bi00428a040  1
1989 Magliozzo RS, Peisach J, Ciriolo MR. Transfer RNA is cleaved by activated bleomycin. Molecular Pharmacology. 35: 428-32. PMID 2468077  1
1989 Ciriolo MR, Peisach J, Magliozzo RS. A comparative study of the interactions of bleomycin with nuclei and purified DNA. The Journal of Biological Chemistry. 264: 1443-9. PMID 2463984  1
1989 Ciriolo MR, Peisach J, Magliozzo RS. A comparative study of the interactions of bleomycin with nuclei and purified DNA. The Journal of Biological Chemistry. 264: 1443-9. PMID 2463984  1
1989 Magliozzo RS, Peisach J. Undesirable reactions in bleomycin biomimetic catalysis systems caused by iodosobenzene Inorganic Chemistry. 28: 608-611.  1
1988 Serpersu EH, McCracken J, Peisach J, Mildvan AS. Electron spin echo modulation and nuclear relaxation studies of staphylococcal nuclease and its metal-coordinating mutants. Biochemistry. 27: 8034-44. PMID 2852950  1
1988 Serpersu EH, McCracken J, Peisach J, Mildvan AS. Electron spin echo modulation and nuclear relaxation studies of staphylococcal nuclease and its metal-coordinating mutants. Biochemistry. 27: 8034-44. PMID 2852950  1
1988 Chapman A, Cammack R, Hatchikian CE, McCracken J, Peisach J. A pulsed EPR study of redox-dependent hyperfine interactions for the nickel centre of Desulfovibrio gigas hydrogenase. Febs Letters. 242: 134-8. PMID 2849556 DOI: 10.1016/0014-5793(88)81001-9  1
1988 Cammack R, Chapman A, McCracken J, Cornelius JB, Peisach J, Weiner JH. Electron spin-echo spectroscopic studies of Escherichia coli fumarate reductase. Biochimica Et Biophysica Acta. 956: 307-12. PMID 2844272 DOI: 10.1016/0167-4838(88)90148-3  1
1988 Cammack R, Chapman A, McCracken J, Cornelius JB, Peisach J, Weiner JH. Electron spin-echo spectroscopic studies of Escherichia coli fumarate reductase. Biochimica Et Biophysica Acta. 956: 307-12. PMID 2844272 DOI: 10.1016/0167-4838(88)90148-3  1
1988 McCracken J, Desai PR, Papadopoulos NJ, Villafranca JJ, Peisach J. Electron spin-echo studies of the copper(II) binding sites in dopamine beta-hydroxylase. Biochemistry. 27: 4133-7. PMID 2843225  1
1988 McCracken J, Desai PR, Papadopoulos NJ, Villafranca JJ, Peisach J. Electron spin-echo studies of the copper(II) binding sites in dopamine beta-hydroxylase. Biochemistry. 27: 4133-7. PMID 2843225  1
1988 Doi K, McCracken J, Peisach J, Aisen P. The binding of molybdate to uteroferrin. Hyperfine interactions of the binuclear center with 95Mo, 1H, and 2H. The Journal of Biological Chemistry. 263: 5757-63. PMID 2833515  1
1988 Nakamura M, Peisach J. Self-inactivation of Fe(II)-bleomycin. The Journal of Antibiotics. 41: 638-47. PMID 2454908  1
1988 McCracken J, Pember S, Benkovic SJ, Villafranca JJ, Miller RJ, Peisach J. Electron spin-echo studies of the copper binding site in phenylalanine hydroxylase from Chromobacterium violaceum Journal of the American Chemical Society. 110: 1069-1074.  1
1988 Traylor TG, Hill KW, Tian ZQ, Rheingold AL, Peisach J, McCracken J. Ene diimidazoles: Ligands for biomimetic chemistry Journal of the American Chemical Society. 110: 5571-5573.  1
1987 Dooley DM, McGuirl MA, Peisach J, McCracken J. The generation of an organic free radical in substrate-reduced pig kidney diamine oxidase-cyanide. Febs Letters. 214: 274-8. PMID 3106087 DOI: 10.1016/0014-5793(87)80069-8  1
1987 Antanaitis BC, Brown RD, Chasteen ND, Freedman JH, Koenig SH, Lilienthal HR, Peisach J, Brewer CF. Electron paramagnetic resonance and magnetic susceptibility studies of dimanganese concanavalin A. Evidence for antiferromagnetic exchange coupling. Biochemistry. 26: 7932-7. PMID 2827763  1
1987 Magliozzo RS, McCracken J, Peisach J. Electron-nuclear coupling in nitrosyl heme proteins and in nitrosyl ferrous and oxy cobaltous tetraphenylporphyrin complexes. Biochemistry. 26: 7923-31. PMID 2827762 DOI: 10.1021/bi00398a057  1
1987 Frydman RB, Rosenfeld J, Camoretti-Mercado B, Peisach J. Porphobilinogen oxygenase. Purification and evidence of its hemoprotein structure. The Journal of Biological Chemistry. 262: 15118-26. PMID 2822713  1
1987 Mondovi B, Morpurgo L, Agostinelli E, Befani O, McCracken J, Peisach J. A comparison of the local environment of Cu(II) in native and half-Cu-depleted bovine serum amine oxidase. European Journal of Biochemistry / Febs. 168: 503-7. PMID 2822417  1
1987 Ciriolo MR, Magliozzo RS, Peisach J. Microsome-stimulated activation of ferrous bleomycin in the presence of DNA. The Journal of Biological Chemistry. 262: 6290-5. PMID 2437117  1
1987 Melnyk DL, Band Horwitz S, Peisach J. The oxidation-reduction potential of copper-bleomycin Inorganica Chimica Acta. 138: 75-78. DOI: 10.1016/S0020-1693(00)81184-6  1
1987 Benkovic SJ, Peisach J, Gorenstein DG, Poulter CD. Abstracts, division of biological chemistry, 194th national meeting of the american chemical society, august 30-september 4, 1987 Biochemistry. 26: 4157-4178.  1
1987 McCracken J, Peisach J, Dooley DM. Cu(II) Coordination chemistry of amine oxidases: Pulsed EPR studies of histidine imidazole, water, and exogenous ligand coordination Journal of the American Chemical Society. 109: 4064-4072.  1
1986 Freedman JH, Weiner RJ, Peisach J. Resistance to copper toxicity of cultured hepatoma cells. Characterization of resistant cell lines. The Journal of Biological Chemistry. 261: 11840-8. PMID 3745169  1
1986 Magliozzo RS, Peisach J. A proton nuclear magnetic resonance study of sulfmyoglobin cyanide. Biochimica Et Biophysica Acta. 872: 158-62. PMID 3730393 DOI: 10.1016/0167-4838(86)90160-3  1
1986 Magliozzo RS, Peisach J. A proton nuclear magnetic resonance study of sulfmyoglobin cyanide. Biochimica Et Biophysica Acta. 872: 158-62. PMID 3730393 DOI: 10.1016/0167-4838(86)90160-3  1
1986 Hirsch RE, Peisach J. A comparison of the intrinsic fluorescence of red kangaroo, horse and sperm whale metmyoglobins. Biochimica Et Biophysica Acta. 872: 147-53. PMID 3730392 DOI: 10.1016/0167-4838(86)90158-5  1
1986 Park CM, Nagel RL, Blumberg WE, Peisach J, Magliozzo RS. Sulfhemoglobin. Properties of partially sulfurated tetramers. The Journal of Biological Chemistry. 261: 8805-10. PMID 3722175  1
1986 Freedman JH, Powers L, Peisach J. Structure of the copper cluster in canine hepatic metallothionein using X-ray absorption spectroscopy. Biochemistry. 25: 2342-9. PMID 3718956  1
1986 Burger RM, Projan SJ, Horwitz SB, Peisach J. The DNA cleavage mechanism of iron-bleomycin. Kinetic resolution of strand scission from base propenal release. The Journal of Biological Chemistry. 261: 15955-9. PMID 2430964  1
1986 Salvato B, Beltramini M, Piazzesi A, Alviggi M, Ricchelli F, Magliozzo RS, Peisach J. Preparation, spectroscopic characterization and anion binding studies of a mononuclear Co(II) derivative of carcinus maenas hemocyanin Inorganica Chimica Acta. 125: 55-62. DOI: 10.1016/S0020-1693(00)85484-5  1
1985 Malikayil JA, Sweeney WV, McCracken J, Peisach J. The lack of a solvent accessible hydroxide or water ligand to iron at the 3Fe center of Azotobacter vinelandii ferredoxin I. Biochemical and Biophysical Research Communications. 133: 1119-24. PMID 3002366 DOI: 10.1016/0006-291X(85)91252-5  1
1985 Malikayil JA, Sweeney WV, McCracken J, Peisach J. The lack of a solvent accessible hydroxide or water ligand to iron at the 3Fe center of Azotobacter vinelandii ferredoxin I. Biochemical and Biophysical Research Communications. 133: 1119-24. PMID 3002366 DOI: 10.1016/0006-291X(85)91252-5  1
1985 Antanaitis BC, Peisach J, Mims WB, Aisen P. Linear electric field effect and electron spin-echo studies of uteroferrin. Evidence for iron coordination by a nitrogen-containing ligand. The Journal of Biological Chemistry. 260: 4572-4. PMID 2985558  1
1985 Antanaitis BC, Peisach J, Mims WB, Aisen P. Linear electric field effect and electron spin-echo studies of uteroferrin. Evidence for iron coordination by a nitrogen-containing ligand. The Journal of Biological Chemistry. 260: 4572-4. PMID 2985558  1
1985 Burger RM, Blanchard JS, Horwitz SB, Peisach J. The redox state of activated bleomycin. The Journal of Biological Chemistry. 260: 15406-9. PMID 2415520  1
1985 Burger RM, Blanchard JS, Horwitz SB, Peisach J. The redox state of activated bleomycin. The Journal of Biological Chemistry. 260: 15406-9. PMID 2415520  1
1985 Burger RM, Horwitz SB, Peisach J. Stimulation of iron(II) bleomycin activity by phosphate-containing compounds. Biochemistry. 24: 3623-9. PMID 2412580  1
1985 Burger RM, Horwitz SB, Peisach J. Stimulation of iron(II) bleomycin activity by phosphate-containing compounds. Biochemistry. 24: 3623-9. PMID 2412580  1
1984 Freedman JH, Peisach J. Determination of copper in biological materials by atomic absorption spectroscopy: a reevaluation of the extinction coefficients for azurin and stellacyanin. Analytical Biochemistry. 141: 301-10. PMID 6496940 DOI: 10.1016/0003-2697(84)90046-0  1
1984 Freedman JH, Peisach J. Determination of copper in biological materials by atomic absorption spectroscopy: a reevaluation of the extinction coefficients for azurin and stellacyanin. Analytical Biochemistry. 141: 301-10. PMID 6496940 DOI: 10.1016/0003-2697(84)90046-0  1
1984 Magliozzo RS, Park CM, Peisach J. Direct spectrophotometric analysis of hemoglobin in isoelectric focusing tube gels. Analytical Biochemistry. 140: 276-83. PMID 6486414 DOI: 10.1016/0003-2697(84)90165-9  1
1984 Fujita S, Suzuki M, Peisach J, Suzuki T. Induction of hepatic microsomal drug metabolism by azo compounds: a structure-activity relationship. Chemico-Biological Interactions. 52: 15-37. PMID 6437688 DOI: 10.1016/0009-2797(84)90080-2  1
1984 Fujita S, Peisach J, Ohkawa H, Yoshida Y, Adachi S, Uesugi T, Suzuki M, Suzuki T. The effect of Sudan III on drug metabolizing enzymes. Chemico-Biological Interactions. 48: 129-43. PMID 6421495 DOI: 10.1016/0009-2797(84)90115-7  1
1984 Fujita S, Peisach J, Ohkawa H, Yoshida Y, Adachi S, Uesugi T, Suzuki M, Suzuki T. The effect of Sudan III on drug metabolizing enzymes. Chemico-Biological Interactions. 48: 129-43. PMID 6421495 DOI: 10.1016/0009-2797(84)90115-7  1
1984 Mims WB, Davis JL, Peisach J. The accessibility of type I Cu(II) centers in laccase, azurin, and stellacyanin to exchangeable hydrogen and ambient water. Biophysical Journal. 45: 755-66. PMID 6326878 DOI: 10.1016/S0006-3495(84)84219-8  1
1984 Ackrell BA, Kearney EB, Mims WB, Peisach J, Beinert H. Iron-sulfur cluster 3 of beef heart succinate-ubiquinone oxidoreductase is a 3-iron cluster. The Journal of Biological Chemistry. 259: 4015-8. PMID 6323451  1
1984 Peisach J, Mims WB, Davis JL. Water coordination by heme iron in metmyoglobin. The Journal of Biological Chemistry. 259: 2704-6. PMID 6321478  1
1984 Kiyotaki C, Peisach J, Bloom BR. Oxygen metabolism in cloned macrophage cell lines: glucose dependence of superoxide production, metabolic and spectral analysis. Journal of Immunology (Baltimore, Md. : 1950). 132: 857-66. PMID 6317750  1
1984 Woolery GL, Powers L, Peisach J, Spiro TG. X-ray absorption study of Rhus laccase: evidence for a copper-copper interaction, which disappears on type 2 copper removal. Biochemistry. 23: 3428-34. PMID 6235850 DOI: 10.1021/BI00310A008  1
1984 Di Iorio EE, Winterhalter KH, Mansouri A, Blumberg WE, Peisach J. Studies on the oxidation of hemoglobin Zurich (beta 63 E7 Arg). European Journal of Biochemistry / Febs. 145: 549-54. PMID 6096143  1
1984 Burger RM, Freedman JH, Horwitz SB, Peisach J. DNA degradation by manganese(II)-bleomycin plus peroxide [2] Inorganic Chemistry. 23: 2215-2217.  1
1983 Peisach J, Beinert H, Emptage MH, Mims WB, Fee JA, Orme-Johnson WH, Rendina AR, Orme-Johnson NR. Characterization of 3-iron ferredoxins by means of the linear electric field effect in EPR. The Journal of Biological Chemistry. 258: 13014-6. PMID 6313686  1
1983 Peisach J, Beinert H, Emptage MH, Mims WB, Fee JA, Orme-Johnson WH, Rendina AR, Orme-Johnson NR. Characterization of 3-iron ferredoxins by means of the linear electric field effect in EPR. The Journal of Biological Chemistry. 258: 13014-6. PMID 6313686  1
1983 Orme-Johnson NR, Mims WB, Orme-Johnson WH, Bartsch RG, Cusanovich MA, Peisach J. Oxidation state dependence of proton exchange near the iron-sulfur centers in ferredoxins and high-potential iron-sulfur proteins. Biochimica Et Biophysica Acta. 748: 68-72. PMID 6311272 DOI: 10.1016/0167-4838(83)90028-6  1
1983 Burger RM, Kent TA, Horwitz SB, Münck E, Peisach J. Mössbauer study of iron bleomycin and its activation intermediates. The Journal of Biological Chemistry. 258: 1559-64. PMID 6185486  1
1983 Shimizu T, Mims WB, Davis JL, Peisach J. Studies of the coordination of rare earth and transition metal nucleotide complexes by an electron spin echo method Bba - General Subjects. 757: 29-39. DOI: 10.1016/0304-4165(83)90149-6  1
1982 Fujita S, Peisach J. The stimulation of microsomal azoreduction by flavins. Biochimica Et Biophysica Acta. 719: 178-89. PMID 7150636 DOI: 10.1016/0304-4165(82)90087-3  1
1982 Peisach J, Powers L, Blumberg WE, Chance B. Stellacyanin. Studies of the metal-binding site using x-ray absorption spectroscopy. Biophysical Journal. 38: 277-85. PMID 7104439 DOI: 10.1016/S0006-3495(82)84559-1  1
1982 Freedman JH, Pickart L, Weinstein B, Mims WB, Peisach J. Structure of the Glycyl-L-histidyl-L-lysine--copper(II) complex in solution. Biochemistry. 21: 4540-4. PMID 6291585  1
1982 Zweier JL, Peisach J, Mims WB. Electron spin echo studies of the copper complexes of conalbumin. The Journal of Biological Chemistry. 257: 10314-6. PMID 6286648  1
1982 Burger RM, Peisach J, Horwitz SB. Stoichiometry of DNA strand scission and aldehyde formation by bleomycin. The Journal of Biological Chemistry. 257: 8612-4. PMID 6178735  1
1982 Freedman JH, Horwitz SB, Peisach J. Reduction of copper(II)-bleomycin: A model for in vivo drug activity Biochemistry. 21: 2203-2210. PMID 6178433  1
1982 Burger RM, Peisach J, Horwitz SB. Effects of O2 on the reactions of activated bleomycin. The Journal of Biological Chemistry. 257: 3372-5. PMID 6174519  1
1981 Fujita S, Okada Y, Peisach J. Inhibition of azoreductase activity by antibodies against cytochromes P-450 and P-448 Biochemical and Biophysical Research Communications. 102: 492-498. PMID 7306168 DOI: 10.1016/0006-291X(81)91546-1  1
1981 Lerch K, Mims WB, Peisach J. Pulsed EPR studies of peroxide-activated cytochrome c peroxidase and of the mercaptoethanol derivative of Neurospora tyrosinase Journal of Biological Chemistry. 256: 10088-10091. PMID 6268624  1
1981 Fee JA, Peisach J, Mims WB. Superoxide dismutase. Examination of the metal binding sites by electron spin echo spectroscopy Journal of Biological Chemistry. 256: 1910-1914. PMID 6257693  1
1981 Burger RM, Peisach J, Horwitz SB. Activated bleomycin. A transient complex of drug, iron, and oxygen that degrades DNA. The Journal of Biological Chemistry. 256: 11636-44. PMID 6170635  1
1981 Melnyk DL, Horwitz SB, Peisach J. Redox potential of iron-bleomycin. Biochemistry. 20: 5327-31. PMID 6170321  1
1981 Burger RM, Peisach J, Horwitz SB. Mechanism of bleomycin action: in vitro studies. Life Sciences. 28: 715-27. PMID 6164898 DOI: 10.1016/0024-3205(81)90153-3  1
1981 Burger RM, Adler AD, Horwitz SB, Mims WB, Peisach J. Demonstration of nitrogen coordination in metal--bleomycin complexes by electron spin--echo envelope spectroscopy. Biochemistry. 20: 1701-4. PMID 6164390  1
1981 Avigliano L, Davis JL, Graziani MT, Marchesini A, Mims WB, Mondovi B, Peisach J. Electron spin echo spectroscopic studies of type 1 and type 2 copper in Rhus vernicifera laccase and in Cucurbita pepo medullosa ascorbate oxidase Febs Letters. 136: 80-84. DOI: 10.1016/0014-5793(81)81218-5  1
1981 Uyeda M, Peisach J. Ultraviolet difference spectroscopy of myoglobin: Assignment of pK values of tyrosyl phenolic groups and the stability of the ferryl derivatives Biochemistry. 20: 2028-2035.  1
1981 Burger RM, Peisach J, Horwitz SB. DNA degradation by activated iron-bleomycin Federation Proceedings. 40: 1107.  1
1980 Pickart L, Freedman JH, Loker WJ, Peisach J, Perkins CM, Stenkamp RE, Weinstein B. Growth-modulating plasma tripeptide may function by facilitating copper uptake into cells. Nature. 288: 715-7. PMID 7453802 DOI: 10.1038/288715a0  1
1980 Kampa L, Peisach J. Purification and characterization of hydroxyindole oxidase from the gills of Mytilus edulis Journal of Biological Chemistry. 255: 595-601. PMID 7356633  1
1980 Damiani C, Kiyotaki C, Soeller W, Sasada M, Peisach J, Bloom BR. Macrophage variants in oxygen metabolism Journal of Experimental Medicine. 152: 808-822. PMID 6252274 DOI: 10.1084/jem.152.4.808  1
1980 Mims WB, Peisach J, Shaw RW, Beinert H. Electron spin echo studies of cytochrome c oxidase. The Journal of Biological Chemistry. 255: 6843-6. PMID 6248535  1
1980 Kosman DJ, Peisach J, Mims WB. Pulsed electron paramagnetic resonance studies of the copper(II) site in galactose oxidase Biochemistry. 19: 1304-1308. PMID 6248103 DOI: 10.1021/bi00548a007  1
1980 Hollenberg PF, Hager LP, Blumberg WE, Peisach J. An electron paramagnetic resonance study of the high and low spin forms of chloroperoxidase. The Journal of Biological Chemistry. 255: 4801-7. PMID 6246083  1
1980 Burger RM, Berkowitz AR, Peisach J, Horwitz SB. Origin of malondialdehyde from DNA degraded by Fe(II) x bleomycin. The Journal of Biological Chemistry. 255: 11832-8. PMID 6160153  1
1980 Roberts JE, Brown TG, Hoffman BM, Peisach J. Electron nuclear double resonance spectra of stellacyanin, a blue copper protein Journal of the American Chemical Society. 102: 825-829.  1
1979 Peisach J, Mims WB, Davis JL. Studies of the electron-nuclear coupling between Fe(III) and 14N in cytochrome P-450 and in a series of low spin heme compounds Journal of Biological Chemistry. 254: 12379-12389. PMID 227893  1
1979 Powers L, Blumberg WE, Chance B, Barlow CH, Leigh JS, Smith J, Yonetani T, Vik S, Peisach J. The nature of the copper atoms of cytochrome c oxidase as studied by optical and x-ray absorption edge spectroscopy. Biochimica Et Biophysica Acta. 546: 520-38. PMID 222313  1
1979 Mims WB, Peisach J. Measurement of 14N superhyperfine frequencies in stellacyanin by an electron spin echo method Journal of Biological Chemistry. 254: 4321-4323. PMID 220240  1
1979 Goldberg B, Stern A, Peisach J, Blumberg WE. The detection of superoxide anion from the reaction of oxyhemoglobin and phenylhydrazine using EPR spectroscopy. Experientia. 35: 488-9. PMID 220081  1
1979 Zweier J, Aisen P, Peisach J, Mims WB. Pulsed electron paramagnetic resonance studies of the copper complexes of transferrin Journal of Biological Chemistry. 254: 3512-3515. PMID 218971  1
1979 Burger RM, Horwitz SB, Peisach J, Wittenberg JB. Oxygenated iron bleomycin. A short-lived intermediate in the reaction of ferrous bleomycin with O2. The Journal of Biological Chemistry. 254: 12999-302. PMID 91616  1
1979 Burger RM, Peisach J, Blumberg WE, Horwitz SB. Iron-bleomycin interactions with oxygen and oxygen analogues. Effects on spectra and drug activity. The Journal of Biological Chemistry. 254: 10906-12. PMID 91607  1
1979 Chevion M, Peisach J, Blumberg WE. Electron paramagnetic resonance study of nitrosyl haemoglobin M Iwate International Journal of Biological Macromolecules. 1: 208-210. DOI: 10.1016/0141-8130(79)90014-X  1
1979 Shimizu T, Mims WB, Peisach J, Davis JL. Analysis of the electron spin echo decay envelope for Nd3+:ATP complexes The Journal of Chemical Physics. 70: 2249-2254.  1
1978 Blumberg WE, Peisach J, Eisenberger P, Fee JA. Superoxide dismutase, a study of the electronic properties of the copper and zinc by X-ray absorption spectroscopy. Biochemistry. 17: 1842-6. PMID 566111  1
1978 Henry Y, Peisach J. Photoreduction of copper chromophores in blue oxidases Journal of Biological Chemistry. 253: 7751-7756. PMID 212433  1
1978 Peisach J, Mims WB. The linear electric field effect in stellacyanin, azurin and in some simple model compounds European Journal of Biochemistry. 84: 207-214. PMID 206431  1
1978 Carrico RJ, Peisach J, Alben JO. The preparation and some physical properties of sulfhemoglobin Journal of Biological Chemistry. 253: 2386-2391. PMID 204647  1
1978 Burger RM, Peisach J, Horwitz SB. Effect of light and oxygen on neocarzinostatin stability and DNA-cleaving activity. The Journal of Biological Chemistry. 253: 4830-2. PMID 149790  1
1978 Fujita S, Peisach J. Liver microsomal cytochromes P-450 and azoreductase activity Journal of Biological Chemistry. 253: 4512-4513. PMID 96118  1
1978 Sausville EA, Stein RW, Peisach J, Horwitz SB. Properties and products of the degradation of DNA by bleomycin and iron(II). Biochemistry. 17: 2746-54. PMID 80227  1
1978 Sausville EA, Peisach J, Horwitz SB. Effect of chelating agents and metal ions on the degradation of dna by bleomycin Biochemistry. 17: 2740-2746. PMID 80226  1
1978 Carrico RJ, Blumberg WE, Peisach J. The reversible binding of oxygen to sulfhemoglobin. The Journal of Biological Chemistry. 253: 7212-5. PMID 29895  1
1978 Chevion M, Stern A, Peisach J, Blumberg WE, Simon S. Analogous effect of protons and inositol hexaphosphate on the alteration of structure of nitrosyl fetal human hemoglobin. Biochemistry. 17: 1745-50. PMID 26386  1
1978 Mims WB, Peisach J. The nuclear modulation effect in electron spin echoes for complexes of Cu2+ and imidazole with 14N and 15N The Journal of Chemical Physics. 69: 4921-4930.  1
1977 Chevion M, Stegeman JJ, Peisach J, Blumberg WE. Electron paramagnetic resonance studies on hepatic microsomal cytochrome P-450 from a marine teleost fish. Life Sciences. 20: 895-9. PMID 15714776  1
1977 Fujita S, Peisach J. Electron transfer between liver microsomal cytochrome b5 and cytochrome P-450 in the azo reductase reaction Biochemical and Biophysical Research Communications. 78: 328-335. PMID 907682 DOI: 10.1016/0006-291X(77)91258-X  1
1977 Mondoví B, Graziani MT, Mims WB, Oltzik R, Peisach J. Pulsed electron paramagnetic resonance studies of types I and II copper of Rhus vernicifera laccase and porcine ceruloplasmin Biochemistry. 16: 4198-4202. PMID 197989  1
1977 Peisach J, Mims WB. Linear electric field effect in electron paramagnetic resonance for two bisimidazole-heme complexes, model compounds for B and H hemichromes of hemoglobin and for cytochrome b5 Biochemistry. 16: 2795-2799. PMID 196621  1
1977 Peisach J, Orme-Johnson NR, Mims WB, Orme-Johnson WH. Linear electric field effect and nuclear modulation studies of ferredoxins and high potential iron-sulfur proteins. The Journal of Biological Chemistry. 252: 5643-50. PMID 195957  1
1977 Chevion M, Peisach J, Blumberg WE. Imidazole, the ligand trans to mercaptide in ferric cytochrome P-450. An EPR study of proteins and model compounds. The Journal of Biological Chemistry. 252: 3637-45. PMID 193841  1
1977 Peisach J, Gersonde K. Binding of CO to mutant α chains of hemoglobin M iwate; evidence for distal imidazole ligation Biochemistry. 16: 2539-2545. PMID 193562  1
1977 Chevion M, Traum MM, Blumberg WE, Peisach J. High resolution EPR studies of the fine structure of heme proteins. Third harmonic detection approach. Biochimica Et Biophysica Acta. 490: 272-8. PMID 189827  1
1977 D'Adamo AF, Peisach J, Manner G, Weiler CT. N acetyl aspartate amidohydrolase: purification and properties Journal of Neurochemistry. 28: 739-744. PMID 19559 DOI: 10.1111/J.1471-4159.1977.TB10621.X  1
1977 Mims WB, Peisach J, Davis JL. Nuclear modulation of the electron spin echo envelope in glassy materials The Journal of Chemical Physics. 66: 5536-5550.  1
1977 Sausville EA, Peisach J, Horwitz SB. Degradation of DNA by bleomycin and FE(II) Federation Proceedings. 36: No. 350.  1
1976 Stern JO, Peisach J. A model compound for nitrosyl cytochrome P-450; further evidence for mercaptide sulfur ligation to heme Febs Letters. 62: 364-368. PMID 1278381 DOI: 10.1016/0014-5793(76)80095-6  1
1976 Blumberg WE, Eisenberger P, Peisach J, Shulman RG. X-ray absorption spectroscopy: probing the chemical and electronic structure of metalloproteins. Advances in Experimental Medicine and Biology. 74: 389-99. PMID 961537  1
1976 Appleby CA, Blumberg WE, Peisach J, Wittenberg BA, Wittenberg JB. Leghemoglobin. An electron paramagnetic resonance and optical spectral study of the free protein and its complexes with nicotinate and acetate. The Journal of Biological Chemistry. 251: 6090-6. PMID 184092  1
1976 Henry Y, Ishimura Y, Peisach J. Binding of nitric oxide to reduced L tryptophan 2,3 dioxygenase as studied by electron paramagnetic resonance Journal of Biological Chemistry. 251: 1578-1581. PMID 176157  1
1976 Sausville EA, Peisach J, Horwitz SB. A role for ferrous ion and oxygen in the degradation of DNA by bleomycin Biochemical and Biophysical Research Communications. 73: 814-822. PMID 64249 DOI: 10.1016/0006-291X(76)90882-2  1
1976 Goldberg B, Stern A, Peisach J. The mechanism of superoxide anion generation by the interaction of phenylhydrazine with hemoglobin Journal of Biological Chemistry. 251: 3045-3051. PMID 5452  1
1976 Peisach J, Mims WB. Deviations from centrosymmetry in some simple Cu2+ complexes Chemical Physics Letters. 37: 307-310. DOI: 10.1016/0009-2614(76)80221-7  1
1976 Fujita S, Peisach J. Amaranth reductase, a cytochrome P 450 diaphorase activity in rat liver microsomes Pharmacologist. 18: No.508.  1
1976 Mims WB, Peisach J. The linear electric field effect for low spin ferric heme compounds The Journal of Chemical Physics. 64: 1074-1091.  1
1975 Peisach J. An interim report on electronic control of oxygenation of heme proteins Annals of the New York Academy of Sciences. 187-203. PMID 1056163  1
1975 Peisach J. An anlysis of the optical titrations of the 430 and 455 NM chromophores of ethyl isocyanide complexes of mammalian hepatic cytochrome P-450 Advances in Experimental Medicine and Biology. 58: 203-212. PMID 239537  1
1975 Stern JO, Peisach E, Peisach J, Blumberg WE, Lu AY, Ryan WD, Levin W, West S. Studies on the spin state of 3-methylcholanthrene induced cytochrome P-450 from rat liver. Advances in Experimental Medicine and Biology. 58: 189-202. PMID 168749 DOI: 10.1007/978-1-4615-9026-2_13  1
1975 Peisach J, Blumberg WE, Rachmilewitz EA. The demonstration of ferrihemochrome intermediates in heinz body formation following the reduction of oxyhemoglobin A by acetylphenylhydrazone. Biochimica Et Biophysica Acta. 393: 404-18. PMID 167836  1
1975 Peisach J, Mannering GJ. A re-evaluation of the optical titrations of the 430 and 455 nm chromophore of ethyl isocyanide complexes of mamalian hepatic cytochrome P-450. Molecular Pharmacology. 11: 818-23. PMID 1667  1
1975 Mims WB, Peisach J. MEASUREMENT OF THE LINEAR ELECTRIC FIELD EFFECT FOR LOW SPIN IRON PORPHYRINS . 275-276.  1
1975 Peisach J, Blumberg WE, Rachmilewitz EA. The reduction of oxyhemoglobin by acetylphenylhydrazine and other aromatic reducing agents: the chemical mechanism for Heinz body formation Federation Proceedings. 34: No. 2662.  1
1974 Stern JO, Peisach J. A model compound study of the CO adduct of cytochrome P 450 Journal of Biological Chemistry. 249: 7495-7498. PMID 4436320  1
1974 Peisach J, Blumberg WE. Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins. Archives of Biochemistry and Biophysics. 165: 691-708. PMID 4374138 DOI: 10.1016/0003-9861(74)90298-7  1
1974 Mims WB, Peisach J. Linear electric field effect measurements of variant low-spin forms of ferric cytochrome c Biochemistry. 13: 3346-3349. PMID 4366473  1
1974 Blumberg WE, Peisach J. On the interpretation of electron paramagnetic resonance spectra of binuclear iron-sulfur proteins. Archives of Biochemistry and Biophysics. 162: 502-12. PMID 4366147 DOI: 10.1016/0003-9861(74)90210-0  1
1974 Stern JO, Peisach J. A model compound of the CO adduct of ferrous cytochrome P 450 Pharmacologist. 16: No.740.  1
1973 Blumberg WE, Peisach J. The measurement of zero field splitting and the determination of ligand composition in mononuclear nonheme iron proteins. Annals of the New York Academy of Sciences. 222: 539-60. PMID 4361868 DOI: 10.1111/j.1749-6632.1973.tb15286.x  1
1973 Peisach J, Blumberg WE, Adler A. Electron paramagnetic resonance studies of iron porphin and chlorin systems. Annals of the New York Academy of Sciences. 206: 310-27. PMID 4356182 DOI: 10.1111/j.1749-6632.1973.tb43219.x  1
1973 Stern JO, Peisach J, Blumberg WE, Lu AY, Levin W. A low-temperature EPR study of partially purified, soluble ferric cytochromes P-450 and P-448 from rat liver microsomes. Archives of Biochemistry and Biophysics. 156: 404-13. PMID 4352418 DOI: 10.1016/0003-9861(73)90289-0  1
1972 Peisach J, Appleby CA, Blumberg WE. Electron paramagnetic resonance and temperature dependent spin state studies of ferric cytochrome P-450 from Rhizobium japonicum. Archives of Biochemistry and Biophysics. 150: 725-32. PMID 4339738 DOI: 10.1016/0003-9861(72)90091-4  1
1972 Seamonds B, Blumberg WE, Peisach J. Electron paramagnetic resonance studies of monomeric ferric Glycera hemoglobin. Biochimica Et Biophysica Acta. 263: 507-14. PMID 4338309 DOI: 10.1016/0005-2795(72)90032-3  1
1971 Peisach J, Oltzik R, Blumberg WE. The electron paramagnetic resonance of molybdenum in rat liver and in rat liver mitochondria. Biochimica Et Biophysica Acta. 253: 58-63. PMID 4331273 DOI: 10.1016/0005-2728(71)90233-7  1
1970 Wittenberg JB, Wittenberg BA, Peisach J, Blumberg WE. On the state of the iron and the nature of the ligand in oxyhemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 67: 1846-53. PMID 4321348 DOI: 10.1073/PNAS.67.4.1846  1
1970 Tsai R, Yu CA, Gunsalus IC, Peisach J, Blumberg W, Orme-Johnson WH, Beinert H. Spin-state changes in cytochrome P-450cam on binding of specific substrates. Proceedings of the National Academy of Sciences of the United States of America. 66: 1157-63. PMID 4319883  1
1970 Peisach J, Blumberg WE. Electron paramagnetic resonance study of the high- and low-spin forms of cytochrome P-450 in liver and in liver microsomes from a methylcholanthrene-treated rabbit. Proceedings of the National Academy of Sciences of the United States of America. 67: 172-9. PMID 4318775 DOI: 10.1073/PNAS.67.1.172  1
1969 Peisach J, Blumberg WE, Wittenberg BA, Wittenberg JB, Kampa L. Hemoglobin A: an electron paramagnetic resonance study of the effects of interchain contacts on the heme symmetry of high-spin and low-spin derivatives of ferric alpha chains. Proceedings of the National Academy of Sciences of the United States of America. 63: 934-9. PMID 4310518 DOI: 10.1073/PNAS.63.3.934  1
1969 Shulman RG, Ogawa S, Wüthrich K, Yamane T, Peisach J, Blumberg WE. The absence of "heme-heme" interactions in hemoglobin. Science (New York, N.Y.). 165: 251-7. PMID 4306914  1
1969 Rachmilewitz EA, Peisach J, Bradley TB, Blumberg WE. Role of haemichromes in the formation of inclusion bodies in haemoglobin H disease. Nature. 222: 248-50. PMID 4305116 DOI: 10.1038/222248A0  1
1968 Wüthrich K, Shulman RG, Peisach J. High-resolution proton magnetic resonance spectra of sperm whale cyanometmyoglobin. Proceedings of the National Academy of Sciences of the United States of America. 60: 373-80. PMID 5248802  1
1966 Blumberg WE, Peisach J. The optical and magnetic properties of copper in Chenopodium album plastocyanin. Biochimica Et Biophysica Acta. 126: 269-73. PMID 4291366 DOI: 10.1016/0926-6585(66)90063-X  1
1965 BLUMBERG WE, GOLDSTEIN M, LAUBER E, PEISACH J. MAGNETIC RESONANCE STUDIES ON THE MECHANISM OF THE ENZYMIC BETA-HYDROXYLATION OF 3,4-DIHYDROXYPHENYLETHYLAMINE. Biochimica Et Biophysica Acta. 99: 187-90. PMID 14325947 DOI: 10.1016/S0926-6593(65)80025-X  1
1964 Blumberg WE, Levine WG, Margolis S, Peisach J. On the nature of copper in two proteins obtained from Rhus vernicifera latex. Biochemical and Biophysical Research Communications. 15: 277-83. PMID 4284280 DOI: 10.1016/0006-291X(64)90160-3  1
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