Cytochrome c1 exhibits two binding sites for cytochrome c in plants

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Cytochrome c1 exhibits two binding sites for cytochrome c in plants.

In plants, channeling of cytochrome c molecules between complexes III and IV has been purported to shuttle electrons within the supercomplexes instead of carrying electrons by random diffusion across the intermembrane bulk phase. However, the mode plant cytochrome c behaves inside a supercomplex such as the respirasome, formed by complexes I, III and IV, remains obscure from a structural point ...

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Identification of the binding site on cytochrome c1 for cytochrome c.

The reagent 1-ethyl-3-(3-[14C]trimethylaminopropyl)carbodiimide (ETC) was used to identify specific carboxyl groups on the cytochrome bc1 complex (ubiquinol-cytochrome c reductase, EC 1.10.2.2) involved in binding cytochrome c. Treatment of the cytochrome bc1 complex with 2 mM ETC led to inhibition of the electron transfer activity with cytochrome c. Sodium dodecyl sulfate-polyacrylamide gel el...

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A complex of cardiac cytochrome c1 and cytochrome c.

The interactions of cytochrome c1 and cytochrome c from bovine cardiac mitochondria were investigated. Cytochrome c1 and cytochrome c formed a 1:1 molecular complex in aqueous solutions of low ionic strength. The complex was stable to Sephadex G-75 chromatography. The formation and stability of the complex were independent of the oxidation state of the cytochrome components as far as those reac...

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The cytochrome c binding site on cytochrome c oxidase.

Cytochrome c oxidase (EC 1.9.3.1) is the terminal enzyme of the mitochondria respiratory chain catalysing electron transfer from cytochrome c to molecular oxygen [ 1,2]. The molecular mechanism of this process is still not understood. At present, little is known about such important structural features as the position of the prosthetic groups or the location and characteristics of the cytochrom...

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Biogenesis of Cytochrome c1

The biogenesis of cytochrome c1 involves a number of steps including: synthesis as a precursor with a bipartite signal sequence, transfer across the outer and inner mitochondrial membranes, removal of the first part of the presequence in the matrix, reexport to the outer surface of the inner membrane, covalent addition of heme, and removal of the remainder of the presequence. In this report we ...

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ژورنال

عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics

سال: 2014

ISSN: 0005-2728

DOI: 10.1016/j.bbabio.2014.07.017