7.1.1.8	Fe2+	iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview	724452	
7.1.1.8	Fe2+	Rieske iron-sulfur protein	724562, 725396	
7.1.1.8	Fe2+	Rieske iron-sulfur protein possessing a high potential [2Fe-2S] cluster	724433	
7.1.1.8	Fe2+	Rieske iron–sulfur protein	725396	
7.1.1.8	Fe2+	Rieske protein, the subunit iron-sulfur protein is made up of three domains. The membrane anchor is an N-terminal TMH (Asp17-Gln41) with pronounced tilt which brings the catalytic domain in contact with the second monomer providing the structural basis for the functional dimer. The catalytic domain is interconnected with the TMH by the hinge region, Met42-Leu51, which harbours the ADV motif, Ala46-Val48	724419	
7.1.1.8	Iron	contains [2Fe–2S] cluster	689387	
7.1.1.8	Iron	enzyme complex contains a Rieske Fe-S protein which controls the rate of reduction of the cytochrome b	658160	
7.1.1.8	Iron	enzyme complex contains a [2Fe-2S] cluster	658161	
7.1.1.8	Iron	enzyme complex contains an iron-sulfur protein, and heme groups in the cytochrome molecules	659318	
7.1.1.8	Iron	enzyme contains 2 cytochromes with heme groups, enzyme contains a Rieske [2Fe-2S] cluster, structure analysis of the Rieske ISP and of soluble fragments thereof	657962