Interaction of horse cytochrome c with the photosynthetic reaction center of Rhodospirillum rubrum.

Abstract:

:Mitochondrial cytochrome c (horse), which is a very efficient electron donor to bacterial photosynthetic reaction centers in vitro, binds to the reaction center of Rhodospirillum rubrum with an approximate dissociation constant of 0.3-0.5 microM at pH 8.2 and low ionic strength. The binding site for the reaction center is on the frontside of cytochrome c which is the side with the exposed heme edge, as revealed by differential chemical acetylation of lysines of free and reaction-center-bound cytochrome c. In contrast, bacterial cytochrome c2 was found previously to bind to the detergent-solubilized reaction center through its backside, i.e., the side opposite to the heme cleft [Rieder, R., Wiemken, V., Bachofen, R., and Bosshard, H. R. (1985). Biochem. Biophys. Res. Commun. 128, 120-126]. Binding of mitochondrial cytochrome c but not of mitochondrial cytochrome c2 is strongly inhibited by low concentrations of poly-L-lysine. The results are difficult to reconcile with the existence of an electron transfer site on the backside of cytochrome c2.

journal_name

J Bioenerg Biomembr

authors

Bosshard HR,Snozzi M,Bachofen R

doi

10.1007/BF00768540

subject

Has Abstract

pub_date

1987-08-01 00:00:00

pages

375-82

issue

4

eissn

0145-479X

issn

1573-6881

journal_volume

19

pub_type

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