A study in vivo into the kinetics of the dissociation of oxygen from oxyhaemoglobin compared with changes in the redox state of cytochrome oxidase in rat brain utilizing near-i.r. spectroscopy

1990 ◽  
Vol 18 (5) ◽  
pp. 1019-1020 ◽  
Author(s):  
MAUREEN S. THORNILEY ◽  
NICOLA LIVERA ◽  
YAPA A. B. D. WICKRAMASINGHE ◽  
PETER ROLFE
Keyword(s):  
Rat Brain ◽  
Cytochrome Oxidase ◽  
Redox State ◽  
Kinetics Of

The in vitro dissociation kinetics of (R,R)-[125I]4IQNB is reflected in the in vivo washout of the radioligand from rat brain

Life Sciences ◽  
1992 ◽  
Vol 50 (9) ◽  
pp. 629-637 ◽  
Author(s):  
Raymond E. Gibson ◽  
Terry Moody ◽  
Timothy A. Schneidau ◽  
Elaine M. Jagoda ◽  
Richard C. Reba
Keyword(s):  
Rat Brain ◽  
Dissociation Kinetics ◽  
Kinetics Of

In vivo GABA release and kinetics of transgene loss in a GABAergic cell line after long-term transplantation into the rat brain

Neuroscience ◽  
2012 ◽  
Vol 203 ◽  
pp. 244-254 ◽  
Author(s):  
J. Mejía-Toiber ◽  
J.H. Limón-Pacheco ◽  
A. Gonzalez-Gallardo ◽  
M. Giordano
Keyword(s):  
Rat Brain ◽  
Cell Line ◽  
Gaba Release ◽  
Kinetics Of

c-fos expression and redox state of cytochrome oxidase of rat brain in hypoxia

Neuroreport ◽  
2000 ◽  
Vol 11 (2) ◽  
pp. 301-304 ◽  
Author(s):  
Yasutomo Nomura ◽  
Masataka Kinjo ◽  
Mamoru Tamura
Keyword(s):  
Rat Brain ◽  
Cytochrome Oxidase ◽  
Redox State ◽  
Fos Expression

scholarly journals Studies on partially reduced mammalian cytochrome oxidase. Reactions with carbon monoxide and oxygen

1974 ◽  
Vol 137 (2) ◽  
pp. 205-215 ◽  
Author(s):  
Colin Greenwood ◽  
Michael T. Wilson ◽  
Maurizio Brunori
Keyword(s):  
Cytochrome Oxidase ◽  
Redox State ◽  
Mixed Valence ◽  
Order Rate Constant ◽  
Low Oxygen ◽  
Difference Spectra ◽  
Ferrocytochrome C ◽  
Kinetics Of ◽  
Enzyme Species ◽  
Binding Behaviour

A number of methods were used to prepare a species of mammalian cytochrome oxidase (EC 1.9.3.1, ferrocytochrome c–oxygen oxidoreductase) in which only cytochrome a3 is reduced and in combination with CO. The kinetics of CO binding by cytochrome a32+ in this species is significantly different from that exhibited by cytochrome a32+ in the fully reduced enzyme. The second-order rate constant for combination was 5X104m−1·s−1 and the ‘off’ constant was 3X10−2s−1. The kinetic difference spectra cytochrome a32+–cytochrome a32+–CO reveal further differences between the mixed-valence and the fully reduced enzyme. The reaction between cytochrome a32+ and oxygen in the mixed-valence species was followed in flow–flash experiments and reveals a fast, oxygen-dependent (8X107m−1·s−1 at low oxygen) rate followed by a slow process, whose rate is independent of oxygen but whose amplitude is dependent on [O2]. The fast oxygen-dependent reaction yields as the first product the so-called ‘oxygenated’ enzyme. We conclude from these experiments that the ligand-binding behaviour of cytochrome a3 depends on the redox state of its partners, a fact which represents clear evidence for site–site interaction in this enzyme. The fact that oxygen reacts rapidly with this enzyme species in which only one component, namely cytochrome a3, is reduced represents clear and unequivocal evidence that this is indeed the O2-binding site in cytochrome oxidase and may indicate that reduction of oxygen can proceed via single electron steps.

The Cytochrome Oxidase Redox State in Vivo

1997 ◽  
pp. 449-456 ◽  
Author(s):  
Chris Cooper ◽  
Martyn Sharpe ◽  
Clare Elwell ◽  
Roger Springett ◽  
Juliet Penrice ◽  
...  
Keyword(s):  
Cytochrome Oxidase ◽  
Redox State

scholarly journals Nitric Oxide does not Inhibit Cerebral Cytochrome Oxidase In Vivo or in the Reactive Hyperemic Phase after Brief Anoxia in the Adult Rat

2002 ◽  
Vol 22 (5) ◽  
pp. 515-519 ◽  
Author(s):  
Geofrey De Visscher ◽  
Roger Springett ◽  
David T. Delpy ◽  
Jos Van Reempts ◽  
Marcel Borgers ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Infrared Spectroscopy ◽  
Cytochrome Oxidase ◽  
Time Course ◽  
Redox State ◽  
Near Infrared ◽  
Adult Rats ◽  
Adult Rat ◽  
Cerebral Saturation

In this study, near-infrared spectroscopy was applied to examine whether cytochrome oxidase in the rat brain is inhibited by nitric oxide in vivo. During normoxia, intravenous NG-nitro-l-arginine methyl ester (l-NAME) administration significantly decreased the cerebral saturation of hemoglobin with oxygen but did not alter the cytochrome oxidase redox state. Anoxia significantly reduced the cytochrome oxidase. The time course of the recovery of the redox state during reoxygenation was not altered by l-NAME. The results suggest that in adult rats, cytochrome oxidase is not inhibited by nitric oxide, either in physiologic conditions or during reoxygenation after a brief anoxic period.

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