Structure at 1.0 resolution of a high-potential iron-sulfur protein involved in the aerobic respiratory chain of Rhodothermus marinus

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Abstract

The aerobic respiratory chain of the thermohalophilic bacterium Rhodothermus marinus, a nonphotosynthetic organism from the Bacteroidetes/Chlorobi group, contains a high-potential iron-sulfur protein (HiPIP) that transfers electrons from a bc (1) analog complex to a caa (3) oxygen reductase. Here, we describe the crystal structure of the reduced form of R. marinus HiPIP, solved by the single-wavelength anomalous diffraction method, based on the anomalous scattering of the iron atoms from the [4Fe-4S](3+/2+) cluster and refined to 1.0 resolution. This is the first structure of a HiPIP isolated from a nonphotosynthetic bacterium involved in an aerobic respiratory chain. The structure shows a similar environment around the cluster as the other HiPIPs from phototrophic bacteria, but reveals several features distinct from those of the other HiPIPs of phototrophic bacteria, such as a different fold of the N-terminal region of the polypeptide due to a disulfide bridge and a ten-residue-long insertion.
Original languageUnknown
Pages (from-to)303-313
JournalJournal Of Biological Inorganic Chemistry
Volume15
Issue number3
DOIs
Publication statusPublished - 1 Jan 2010

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