Pulse radiolysis study of daunorubicin redox reactions: Redox cycles or glycosidic cleavage?

1986 ◽  
Vol 2 (2) ◽  
pp. 89-97
Author(s):  
C HOUEELEVIN ◽  
M GARDESALBERT ◽  
C FERRADINI
Keyword(s):  
Redox Reactions ◽  
Pulse Radiolysis ◽  
Glycosidic Cleavage ◽  
Redox Cycles

scholarly journals Redox Reactions of Sanazole (AK- 2123) in Aqueous Solutions: A Pulse Radiolysis Study

2000 ◽  
Vol 41 (4) ◽  
pp. 355-366 ◽  
Author(s):  
SUDHIR KAPOOR ◽  
ROBIN MATHEW ◽  
NAGARAJ G. HUILGOL ◽  
TSUTOMU V. KAGIYA ◽  
CHERUPALLY KRISHNAN K. NAIR
Keyword(s):  
Aqueous Solutions ◽  
Redox Reactions ◽  
Pulse Radiolysis

Pulse radiolysis studies on the redox reactions of aqueous solutions of .gamma.-cyclodextrine/C60 complexes

1994 ◽  
Vol 98 (38) ◽  
pp. 9565-9569 ◽  
Author(s):  
K. I. Priyadarsini ◽  
H. Mohan ◽  
J. P. Mittal ◽  
D. M. Guldi ◽  
K.-D. Asmus
Keyword(s):  
Aqueous Solutions ◽  
Redox Reactions ◽  
Pulse Radiolysis

redox reactions of methylene blue: A pulse radiolysis study

1989 ◽  
Vol 34 (4) ◽  
pp. 721-727 ◽  
Author(s):  
Kamal Kishore ◽  
S.N. Guha ◽  
J. Mahadevan ◽  
P.N. Moorthy ◽  
J.P. Mittal
Keyword(s):  
Methylene Blue ◽  
Redox Reactions ◽  
Pulse Radiolysis

Redox reactions of disulfiram: a pulse-radiolysis study

2003 ◽  
Vol 29 (3) ◽  
pp. 317-324
Author(s):  
M. Rele ◽  
S. Kapoor ◽  
T. Mukherjee
Keyword(s):  
Redox Reactions ◽  
Pulse Radiolysis

scholarly journals Evidence for catalytic dismutation of superoxide by cobalt(II) derivatives of bovine superoxide dismutase in aqueous solution as studied by pulse radiolysis

1982 ◽  
Vol 205 (1) ◽  
pp. 181-187 ◽  
Author(s):  
P O'Neill ◽  
E M Fielden ◽  
D Cocco ◽  
G Rotilio ◽  
L Calabrese
Keyword(s):  
Aqueous Solution ◽  
Superoxide Dismutase ◽  
Rate Constants ◽  
Redox Reactions ◽  
Pulse Radiolysis ◽  
Turnover Rate ◽  
Copper Site ◽  
Initial Interaction ◽  
Derivatives Of ◽  
Reaction Schemes

By using the technique of pulse radiolysis to generate O2-., it is demonstrated that Co(II) derivatives of bovine superoxide dismutase in which the copper alone and both the copper and zinc of the enzyme have been substituted by Co(II), resulting in (Co, Zn)- and (Co, Co)-proteins, are capable of catalytically dismutating O2-. with ‘turnover’ rate constants of 4.8×10(6) dm3.s-1.mol-1 and 3.1×10(6) dm3.s-1.mol-1 respectively. The activities of the proteins are independent of the pH (7.4-9.4) and are about three orders of magnitude less than that of the native (Cu, Zn)-protein. The rate constants for the initial interaction of O2-. with the Co-proteins were determined to be (1.5-1.6) X 10(9) dm3.s-1.mol-1; however, in the presence of phosphate, partial inhibition is apparent [k approximately (1.9-2.3) X 10(8) dm3.s-1.mol-1]. To account for the experimental observations, two reaction schemes are presented, involving initially either complex-formation or redox reactions between O2-. and Co(II). This is the first demonstration that substitution of a metal into the vacant copper site of (Cu, Zn)-protein results in proteins that retain superoxide dismutase activity.

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