| Year |
Citation |
Score |
| 1996 |
Hirota S, Svensson-Ek M, Adelroth P, Sone N, Nilsson T, Malmström BG, Brzezinski P. A flash-photolysis study of the reactions of a caa3-type cytochrome oxidase with dioxygen and carbon monoxide. Journal of Bioenergetics and Biomembranes. 28: 495-501. PMID 8953381 DOI: 10.1007/Bf02110439 |
0.594 |
|
| 1996 |
Mitchell DM, Fetter JR, Mills DA, Adelroth P, Pressler MA, Kim Y, Aasa R, Brzezinski P, Malmström BG, Alben JO, Båbcock GT, Ferguson-Miller S, Gennis RB. Site-directed mutagenesis of residues lining a putative proton transfer pathway in cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry. 35: 13089-93. PMID 8855945 DOI: 10.1021/Bi961416L |
0.521 |
|
| 1996 |
Mitchell DM, Adelroth P, Hosler JP, Fetter JR, Brzezinski P, Pressler MA, Aasa R, Malmström BG, Alben JO, Babcock GT, Gennis RB, Ferguson-Miller S. A ligand-exchange mechanism of proton pumping involving tyrosine-422 of subunit I of cytochrome oxidase is ruled out. Biochemistry. 35: 824-8. PMID 8547262 DOI: 10.1021/Bi951897T |
0.548 |
|
| 1995 |
Adelroth P, Brzezinski P, Malmström BG. Internal electron transfer in cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry. 34: 2844-9. PMID 7893697 DOI: 10.1021/bi00009a014 |
0.563 |
|
| 1995 |
Brzezinski P, Sundahl M, Adelroth P, Wilson MT, el-Agez B, Wittung P, Malmström BG. Triplet-state quenching in complexes between Zn-cytochrome c and cytochrome oxidase or its CuA domain. Biophysical Chemistry. 54: 191-7. PMID 7756569 DOI: 10.1016/0301-4622(94)00128-7 |
0.533 |
|
| 1995 |
Mitchell DM, Aasa R, Adelroth P, Brzezinski P, Gennis RB, Malmström BG. EPR studies of wild-type and several mutants of cytochrome c oxidase from Rhodobacter sphaeroides: Glu286 is not a bridging ligand in the cytochrome a3-CuB center. Febs Letters. 374: 371-4. PMID 7589573 DOI: 10.1016/0014-5793(95)01149-9 |
0.537 |
|
| 1994 |
Hallén S, Brzezinski P, Malmström BG. Internal electron transfer in cytochrome c oxidase is coupled to the protonation of a group close to the bimetallic site. Biochemistry. 33: 1467-72. PMID 8312266 DOI: 10.1021/bi00172a024 |
0.529 |
|
| 1993 |
Lappalainen P, Aasa R, Malmström BG, Saraste M. Soluble CuA-binding domain from the Paracoccus cytochrome c oxidase. The Journal of Biological Chemistry. 268: 26416-21. PMID 8253767 |
0.309 |
|
| 1992 |
Oliveberg M, Malmström BG. Reaction of dioxygen with cytochrome c oxidase reduced to different degrees: indications of a transient dioxygen complex with copper-B. Biochemistry. 31: 3560-3. PMID 1314642 DOI: 10.1021/bi00129a002 |
0.386 |
|
| 1989 |
Oliveberg M, Brzezinski P, Malmström BG. The effect of pH and temperature on the reaction of fully reduced and mixed-valence cytochrome c oxidase with dioxygen. Biochimica Et Biophysica Acta. 977: 322-8. PMID 2556181 DOI: 10.1016/S0005-2728(89)80087-8 |
0.532 |
|
| 1988 |
Thörnström PE, Brzezinski P, Fredriksson PO, Malmström BG. Cytochrome c oxidase as an electron-transport-driven proton pump: pH dependence of the reduction levels of the redox centers during turnover. Biochemistry. 27: 5441-7. PMID 2846037 DOI: 10.1021/bi00415a009 |
0.581 |
|
| 1988 |
Brzezinski P, Malmström BG, Lorentzon P, Wallmark B. The catalytic mechanism of gastric H+/K+-ATPase: simulations of pre-steady-state and steady-state kinetic results. Biochimica Et Biophysica Acta. 942: 215-9. PMID 2840118 DOI: 10.1016/0005-2736(88)90022-3 |
0.472 |
|
| 1987 |
Fabian M, Thörnström PE, Brzezinski P, Malmström BG. Two-electron reduction is required for rapid internal electron transfer in resting, pulsed and oxygenated cytochrome c oxidase. Febs Letters. 213: 396-400. PMID 3030819 DOI: 10.1016/0014-5793(87)81529-6 |
0.584 |
|
| 1987 |
Brzezinski P, Malmström BG. The mechanism of electron gating in proton pumping cytochrome c oxidase: the effect of pH and temperature on internal electron transfer. Biochimica Et Biophysica Acta. 894: 29-38. PMID 2444256 DOI: 10.1016/0005-2728(87)90209-X |
0.544 |
|
| 1986 |
Brzezinski P, Malmström BG. Electron-transport-driven proton pumps display nonhyperbolic kinetics: Simulation of the steady-state kinetics of cytochrome c oxidase. Proceedings of the National Academy of Sciences of the United States of America. 83: 4282-6. PMID 16593710 DOI: 10.1073/pnas.83.12.4282 |
0.549 |
|
| 1986 |
Brzezinski P, Thörnström PE, Malmström BG. The rate-limiting step and nonhyperbolic kinetics in the oxidation of ferrocytochrome c catalyzed by cytochrome c oxidase. Febs Letters. 194: 1-5. PMID 3000820 DOI: 10.1016/0014-5793(86)80040-0 |
0.556 |
|
| 1986 |
Feiters MC, Aasa R, Malmström BG, Veldink GA, Vliegenthart JFG. Spectroscopic studies on the interactions between lipoxygenase-2 and its product hydroperoxides Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 873: 182-189. DOI: 10.1016/0167-4838(86)90044-0 |
0.594 |
|
| 1985 |
Brzezinski P, Malmström BG. The reduction of cytochrome c oxidase by carbon monoxide. Febs Letters. 187: 111-4. PMID 2991001 DOI: 10.1016/0014-5793(85)81224-2 |
0.584 |
|
| 1985 |
Feiters MC, Aasa R, Malmström BG, Slappendel S, Veldink GA, Vliegenthart JFG. Substrate fatty acid activation in soybean lipoxygenase-1 catalysis Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 831: 302-305. DOI: 10.1016/0167-4838(85)90111-6 |
0.621 |
|
| 1983 |
Feiters MC, Vliegent-Hart JF, Reedijk J, Malmström BG. Iron coordination in soybean lipoxygenase-1 Inorganica Chimica Acta. 79: 148. DOI: 10.1016/S0020-1693(00)95184-3 |
0.569 |
|
| 1982 |
Slappendel S, Malmström BG, Petersson L, Ehrenberg A, Veldink GA, Vliegenthart JF. On the spin and valence state of iron in native soybean lipoxygenase-1. Biochemical and Biophysical Research Communications. 108: 673-7. PMID 6816235 DOI: 10.1016/0006-291X(82)90882-8 |
0.506 |
|
| 1982 |
Slappendel S, Aasa R, Falk KE, Malmström BG, Vänngård T, Veldink GA, Vliegenthart JFG. 1H-NMR spectroscopic study on the binding of alcohols to soybean lipoxygenase-1 Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 708: 266-271. DOI: 10.1016/0167-4838(82)90436-8 |
0.479 |
|
| 1982 |
Slappendel S, Aasa R, Malmström BG, Verhagen J, Veldink GA, Vliegenthart JFG. Factors affecting the line-shape of the EPR signal of high-spin Fe(III) in soybean lipoxygenase-1 Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 708: 259-265. DOI: 10.1016/0167-4838(82)90435-6 |
0.497 |
|
| 1981 |
Martin CT, Morse RH, Kanne RM, Gray HB, Malmström BG, Chan SI. Reactions of nitric oxide with tree and fungal laccase. Biochemistry. 20: 5147-55. PMID 6271178 DOI: 10.1021/Bi00521A008 |
0.319 |
|
| 1981 |
Slappendel S, Veldink GA, Vliegenthart JF, Aasa R, Malmström BG. EPR spectroscopy of soybean lipoxygenase-1. Description and quantification of the high-spin fe(III) signals. Biochimica Et Biophysica Acta. 667: 77-86. PMID 6260216 DOI: 10.1016/0005-2795(81)90068-4 |
0.579 |
|
| 1980 |
Slappendel S, Veldink GA, Vliegenthart JF, Aasa R, Malmström BG. EPR spectroscopy of soybean lipoxygenase-1. Determination of the zero-field splitting constants of high-spin Fe(III) signals from temperature and microwave frequency dependence. Biochimica Et Biophysica Acta. 624: 30-9. PMID 6250632 DOI: 10.1016/0005-2795(80)90222-6 |
0.517 |
|
| 1980 |
Reinhammar B, Malkin R, Jensen P, Karlsson B, Andréasson LE, Aasa R, Vänngård T, Malmström BG. A new copper(II) electron paramagnetic resonance signal in two laccases and in cytochrome c oxidase. The Journal of Biological Chemistry. 255: 5000-3. PMID 6246091 |
0.585 |
|
| 1977 |
Rosén S, Brändén R, Vänngård T, Malmström BG. EPR evidence for an active form of cytochrome c oxidase different from the resting enzyme. Febs Letters. 74: 25-30. PMID 190041 DOI: 10.1016/0014-5793(77)80744-8 |
0.738 |
|
| 1976 |
Aasa R, Brändén R, Deinum J, Malmström BG, Reinhammar B, Vänngård T. A 17O-effect on the EPR spectrum of the intermediate in the dioxygen-laccase reaction. Biochemical and Biophysical Research Communications. 70: 1204-9. PMID 182162 DOI: 10.1016/0006-291X(76)91030-5 |
0.712 |
|
| 1976 |
Aasa R, Brändén R, Deinum J, Malmström BG, Reinhammar B, Vänngård T. A paramagnetic intermediate in the reduction of oxygen by reduced laccase. Febs Letters. 61: 115-9. PMID 174942 DOI: 10.1016/0014-5793(76)81016-2 |
0.753 |
|
| 1973 |
Brändén R, Malmström BG, Vänngård T. The effect of fluoride on the spectral and catalytic properties of the three copper-containing oxidases. European Journal of Biochemistry / Febs. 36: 195-200. PMID 4354619 DOI: 10.1111/J.1432-1033.1973.Tb02901.X |
0.751 |
|
| 1971 |
Brändén R, Malmström BG, Vänngård T. The interaction of fungal laccase with hydrogen peroxide and the removal of fluoride from the inhibited enzyme. European Journal of Biochemistry / Febs. 18: 238-41. PMID 4993335 DOI: 10.1111/J.1432-1033.1971.Tb01236.X |
0.746 |
|
| 1971 |
Antonini E, Brunori M, Greenwood C, Malmström BG, Rotilio GC. The interaction of cyanide with cytochrome oxidase. European Journal of Biochemistry / Febs. 23: 396-400. PMID 4333368 DOI: 10.1111/J.1432-1033.1971.Tb01633.X |
0.36 |
|
| 1970 |
Malkin R, Malmström BG. The state and function of copper in biological systems. Advances in Enzymology and Related Areas of Molecular Biology. 33: 177-244. PMID 4318312 DOI: 10.1002/9780470122785.ch4 |
0.496 |
|
| 1969 |
Malmström BG, Agrò AF, Antonini E. The mechanism of laccase-catalyzed oxidations: kinetic evidence for the involvement of several electron-accepting sites in the enzyme. European Journal of Biochemistry / Febs. 9: 383-91. PMID 4978609 DOI: 10.1111/j.1432-1033.1969.tb00620.x |
0.314 |
|
| 1969 |
Malkin R, Malmström BG, Vänngård T. Spectroscopic differentiation of the electron-accepting sites in fungal laccase. Association of a near ultraviolet band with a two electron-accepting unit. European Journal of Biochemistry / Febs. 10: 324-9. PMID 4309868 DOI: 10.1111/j.1432-1033.1969.tb00693.x |
0.533 |
|
| 1969 |
Fee JA, Malkin R, Malmström BG, Vänngård T. Anaerobic oxidation-reduction titrations of fungal laccase. Evidence for several high potential electron-accepting sites. The Journal of Biological Chemistry. 244: 4200-7. PMID 4308170 |
0.553 |
|
| 1969 |
Malkin R, Malmström BG, Vänngård T. The reversible removal of one specific copper(II) from fungal laccase. European Journal of Biochemistry / Febs. 7: 253-9. PMID 4303912 DOI: 10.1111/j.1432-1033.1969.tb19600.x |
0.518 |
|
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