Purification and physical-chemical characterization of the three hydroperoxidases from the symbiotic bacterium Sinorhizobium meliloti.
Ardissone
Silvia
S
Dipartimento di Chimica I. F. M., Università di Torino, via Pietro Giuria 7, 10125 Torino, Italy.
Frendo
Pierre
P
Laurenti
Enzo
E
Jantschko
Walter
W
Obinger
Christian
C
Puppo
Alain
A
Ferrari
Rosa Pia
RP
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000502:physiology; D003001:Cloning, Molecular; D004578:Electron Spin Resonance Spectroscopy; D006418:Heme / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D010544:Peroxidases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000502:physiology; D011524:Protoporphyrins / Q000737:chemistry; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D016962:Sinorhizobium meliloti / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D013056:Spectrophotometry, Ultraviolet; D013559:Symbiosis
D001426:Bacterial Proteins; D011524:Protoporphyrins; D011994:Recombinant Proteins; C448299:iron protoporphyrin IX; D006418:Heme; D010544:Peroxidases; C081610:catalase-peroxidase, bacteria