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By Walter W. Wainio

The Mammalian Mitochondrial breathing chain

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5 milliseconds, while t h e A N S response was slower b y a factor of 4 0 0 . T h e latter h a d a half-time of approximately 2 seconds. Azzi et al stated in this article and in an abstract ( 3 5 ) that the A N S changes p r e c e d e d the energy-linked reactions o f electron transfer and transhydrogenation. T h e hypothesis that results is that I. M I T O C H O N D R I A L STRUCTURE A N D C O M P O S I T I O N 52 m e m b r a n e - c o n f o r m a t i o n a l changes p r o b e d by the fluorescent dyes are essential to, r a t h e r t h a n secondary indications of, e n e r g y conservation.

I t was therefore assumed that the knobs w e r e the seat of A T P a s e activity. , K I or K S C N , facilitated the cold inactivation of A T P a s e and the removal of the inner m e m b r a n e spheres. A reconstituted preparation of oligomycin-sensitive A T P a s e m a d e from an amorphous oligomycin sensitivity-conferring factor ( C F 0 ) and F a c t o r 1 ( A T P a s e ) revealed characteristic fragments of m e m b r a n e s with projecting spheres. , it did not depend on anything b e i n g added.

T h e low molar content o f the dehydrogenases results in a sparse distribution over the surface. T h u s , there are relatively large distances b e t w e e n one dehydrogenase m o l e c u l e and the five to ten cytoc h r o m e chains w h i c h might receive r e d u c i n g equivalents from it. H e postulated, therefore, that hydrogen-transport components are required which c a n b r i d g e these distances b y diffusion. U b i q u i n o n e is considered to b e eminently suited for this role since it occurs in large excess over the cytochromes and is a small nonprotein-bound molecule.

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