The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1.1 Å resolution

Heiko Bönisch, Christian L. Schmidt, Günter Schäfer, Rudolf Ladenstein*

*Corresponding author for this work
59 Citations (Scopus)


The first crystal structure of an archaeal Rieske iron-sulfur protein, the soluble domain of Rieske iron-sulfur protein II (soxF) from the hyperthermo-acidophile Sulfolobus acidocaldarius, has been solved by multiple wavelength anomalous dispersion (MAD) and has been refined to 1.1 Å resolution. SoxF is a subunit of the terminal oxidase super-complex SoxM in the plasma membrane of S. acidocaldarius that combines features of a cytochrome bc1 complex and a cytochrome c oxidase. The [2Fe-2S] cluster of soxF is most likely the primary electron acceptor during the oxidation of caldariella quinone by the cytochrome a587/Rieske subcomplex. The geometry of the [2Fe-2S] cluster and the structure of the cluster-binding site are almost identical in soxF and the Rieske proteins from eucaryal cytochrome bc1 and b6f complexes, suggesting a strict conservation of the catalytic mechanism. The main domain of soxF and part of the cluster-binding domain, though structurally related, show a significantly divergent structure with respect to topology, non-covalent interactions and surface charges. The divergent structure of soxF reflects a different topology of the soxM complex compared to eucaryal bc complexes and the adaptation of the protein to the extreme ambient conditions on the outer membrane surface of a hyperthermo-acidophilic organism.

Original languageEnglish
JournalJournal of Molecular Biology
Issue number3
Pages (from-to)791-805
Number of pages15
Publication statusPublished - 2002

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


Dive into the research topics of 'The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1.1 Å resolution'. Together they form a unique fingerprint.

Cite this