ISSN:
1573-6881
Keywords:
cytochrome bc 1 complex
;
cytochrome c reductase
;
bovine heart mitochondria
;
Rieske Fe–S protein
;
protein crystallography
;
membrane protein
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract Structures of mitochondrial bc 1 complex have been reported based on four different crystalforms by three different groups. In these structures, the extrinsic domain of the Rieske [2Fe–2S]protein, surprisingly, appeared at three different positions: the “c 1” position, where the [2Fe–2S]cluster exists in close proximity to the heme c 1; the “b” position, where the [2Fe–2S] clusterexist in close proximity to the cytochrome b; and the “intermediate” position where the[2Fe–2S] cluster exists in between “c 1” and “b” positions. The conformational changes betweenthese three positions can be explained by a combination of two rotations; (1) a rotation of theentire extrinsic domain and (2) a relative rotation between the cluster-binding fold and thebase fold within the extrinsic domain. The hydroquinone oxidation and the electron bifurcationmechanism at the QP binding pocket of the bc 1 complex is well explained using theseconformational changes of the Rieske [2Fe–2S] protein.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1005407410005
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