Dataset Information

The High-Spin Heme b _L Mutant Exposes Dominant Reaction Leading to the Formation of the Semiquinone Spin-Coupled to the [2Fe-2S]⁺ Cluster at the Q_o Site of Rhodobacter capsulatus Cytochrome bc ₁.

ABSTRACT: Cytochrome bc ₁ (mitochondrial complex III) catalyzes electron transfer from quinols to cytochrome c and couples this reaction with proton translocation across lipid membrane; thus, it contributes to the generation of protonmotive force used for the synthesis of ATP. The energetic efficiency of the enzyme relies on a bifurcation reaction taking place at the Q_o site which upon oxidation of ubiquinol directs one electron to the Rieske 2Fe2S cluster and the other to heme b _L. The molecular mechanism of this reaction remains unclear. A semiquinone spin-coupled to the reduced 2Fe2S cluster (SQ_o-2Fe2S) was identified as a state associated with the operation of the Q_o site. To get insights into the mechanism of the format

SUBMITTER: Sarewicz M

PROVIDER: S-EPMC8138165 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature

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Dataset Information

The High-Spin Heme b _L Mutant Exposes Dominant Reaction Leading to the Formation of the Semiquinone Spin-Coupled to the [2Fe-2S]⁺ Cluster at the Q_o Site of Rhodobacter capsulatus Cytochrome bc ₁.

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Dataset Information

The High-Spin Heme b L Mutant Exposes Dominant Reaction Leading to the Formation of the Semiquinone Spin-Coupled to the [2Fe-2S]+ Cluster at the Qo Site of Rhodobacter capsulatus Cytochrome bc 1.

OmicsDI is part of the ELIXIR infrastructure

Tweets

The High-Spin Heme b _L Mutant Exposes Dominant Reaction Leading to the Formation of the Semiquinone Spin-Coupled to the [2Fe-2S]⁺ Cluster at the Q_o Site of Rhodobacter capsulatus Cytochrome bc ₁.