132 related articles for article (PubMed ID: 214124)
1. Magnetic susceptibility of laccases and ceruloplasmin.
Petersson L; Angström J; Ehrenberg A
Biochim Biophys Acta; 1978 Oct; 526(2):311-7. PubMed ID: 214124
[TBL] [Abstract][Full Text] [Related]
2. Pulsed electron paramagnetic resonance studies of types I and II coper of Rhus vernicifera laccase and porcine ceruloplasmin.
Mondoví B; Graziani MT; Mims WB; Oltzik R; Peisach J
Biochemistry; 1977 Sep; 16(19):4198-202. PubMed ID: 197989
[TBL] [Abstract][Full Text] [Related]
3. The phenoloxidases of the ascomycete Podospora anserina. XI. The state of copper of laccases I, II and III.
Molitoris HP; Reinhammar B
Biochim Biophys Acta; 1975 Apr; 386(2):493-502. PubMed ID: 166666
[TBL] [Abstract][Full Text] [Related]
4. The state of copper in stellacyanin and laccase from the lacquer tree Rhus vernicifera.
Malmström BG; Reinhammar B; Vänngård T
Biochim Biophys Acta; 1970 Apr; 205(1):48-57. PubMed ID: 4314765
[No Abstract] [Full Text] [Related]
5. Magnetic studies of the trinuclear center in laccase and ascorbate oxidase approached by EPR spectroscopy and magnetic susceptibility measurements.
Huang HW; Sakurai T; Monjushiro H; Takeda S
Biochim Biophys Acta; 1998 Apr; 1384(1):160-70. PubMed ID: 9602107
[TBL] [Abstract][Full Text] [Related]
6. A new copper(II) electron paramagnetic resonance signal in two laccases and in cytochrome c oxidase.
Reinhammar B; Malkin R; Jensen P; Karlsson B; Andréasson LE; Aasa R; Vänngård T; Malmström BG
J Biol Chem; 1980 Jun; 255(11):5000-3. PubMed ID: 6246091
[TBL] [Abstract][Full Text] [Related]
7. Magnetic susceptibility studies of laccase and oxyhemocyanin.
Dooley DM; Scott RA; Ellinghaus J; Solomon EI; Gray HB
Proc Natl Acad Sci U S A; 1978 Jul; 75(7):3019-22. PubMed ID: 98765
[TBL] [Abstract][Full Text] [Related]
8. Kinetic studies of Rhus vernicifera laccase. Role of the metal centers in electron transfer.
Andréasson LE; Reinhammar B
Biochim Biophys Acta; 1976 Oct; 445(3):579-97. PubMed ID: 9990
[TBL] [Abstract][Full Text] [Related]
9. Magnetic susceptibility of lacquer tree laccase.
Moss TH; Vänngård T
Biochim Biophys Acta; 1974 Nov; 371(1):39-43. PubMed ID: 4371856
[No Abstract] [Full Text] [Related]
10. Coordination environment for the type 3 copper center of tree laccase and CuB of cytochrome c oxidase as determined by electron nuclear double resonance.
Cline J; Reinhammar B; Jensen P; Venters R; Hoffman BM
J Biol Chem; 1983 Apr; 258(8):5124-8. PubMed ID: 6300117
[TBL] [Abstract][Full Text] [Related]
11. Kinetic studies of Rhus vernicifera laccase. Evidence for multi-electron transfer and an oxygen intermediate in the reoxidation reaction.
Andréasson LE; Brändén R; Reinhammar B
Biochim Biophys Acta; 1976 Jul; 438(2):370-9. PubMed ID: 182231
[TBL] [Abstract][Full Text] [Related]
12. Stereochemistry of anion complexes of type 2 Cu(II) in Rhus vernicifera laccase. Analogy with superoxide dismutase and Cu(II) carbonic anhydrase.
Desideri A; Morpurgo L; Rotilio G; Mondovì B
FEBS Lett; 1979 Feb; 98(2):339-41. PubMed ID: 217736
[No Abstract] [Full Text] [Related]
13. Dependence on freezing of the geometry and redox potential of type 1 and type 2 copper sites of Japanese-lacquer-tree (Rhus vernicifera) laccase.
Morpurgo L; Calabrese L; Desideri A; Rotilio G
Biochem J; 1981 Feb; 193(2):639-42. PubMed ID: 6272712
[TBL] [Abstract][Full Text] [Related]
14. Photoreduction of copper chromophores in blue oxidases.
Henry Y; Peisach J
J Biol Chem; 1978 Nov; 253(21):7751-6. PubMed ID: 212433
[TBL] [Abstract][Full Text] [Related]
15. Intramolecular electron transfer in laccases.
Farver O; Wherland S; Koroleva O; Loginov DS; Pecht I
FEBS J; 2011 Sep; 278(18):3463-71. PubMed ID: 21790996
[TBL] [Abstract][Full Text] [Related]
16. Primary structure of a Japanese lacquer tree laccase as a prototype enzyme of multicopper oxidases.
Nitta K; Kataoka K; Sakurai T
J Inorg Biochem; 2002 Jul; 91(1):125-31. PubMed ID: 12121769
[TBL] [Abstract][Full Text] [Related]
17. Studies on laccases of lacquer trees. II. Copper exchange studies of Rhus vernicifera laccase using radioactive copper.
OMURA T
J Biochem; 1961 Oct; 50():305-11. PubMed ID: 14482009
[No Abstract] [Full Text] [Related]
18. Yeast copper-thionein can reconstitute the Japanese-lacquer-tree (Rhus vernicifera) laccase from the Type 2-copper-depleted enzyme via a direct copper(I)-transfer mechanism.
Morpurgo L; Hartmann HJ; Desideri A; Weser U; Rotilio G
Biochem J; 1983 May; 211(2):515-7. PubMed ID: 6307284
[TBL] [Abstract][Full Text] [Related]
19. Oxidation and reduction of copper ions in catalytic reactions of Rhus laccase.
Nakamura T
Adv Exp Med Biol; 1976; 74():408-23. PubMed ID: 134627
[TBL] [Abstract][Full Text] [Related]
20. Investigation of the anomalous spectroscopic features of the copper sites in chicken ceruloplasmin: comparison to human ceruloplasmin.
Machonkin TE; Musci G; Zhang HH; Bonaccorsi di Patti MC; Calabrese L; Hedman B; Hodgson KO; Solomon EI
Biochemistry; 1999 Aug; 38(34):11093-102. PubMed ID: 10460165
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
