Role of phospholipid in the low affinity reactions between cytochrome c and cytochrome oxidase.

Abstract:

:The steady-state oxidation of ferrocytochrome c by cytochrome oxidase monitored spectrophotometrically showed that: (1) the kinetics were strictly biphasic with purified enzyme, while mitochondrial membrane-bound enzyme exhibited multiphasic kinetics with extended low affinity phases; (2) the TNmax for the highest affinity phase was as slow as 5-10 electron X s-1 for both preparations, while for the low affinity phases it was about 45 electron X s-1 for the purified enzyme and 150 electron X s-1 for the mitochondrial membrane-bound enzyme; (3) reconstitution of purified enzyme into acidic phospholipid vesicles partially repleted the extended low affinity phases, while reconstitution into uncharged vesicles had no effect.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Speck SH,Neu CA,Swanson MS,Margoliash E

doi

10.1016/0014-5793(83)80321-4

subject

Has Abstract

pub_date

1983-12-12 00:00:00

pages

379-82

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(83)80321-4

journal_volume

164

pub_type

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