The road to the crystal structure of the cytochrome bc1 complex from the anoxigenic, photosynthetic bacterium Rhodobacter sphaeroides.

ABSTRACT: The advantages of using bacterial systems to study the mechanism and function of cytochrome bc (1) complexes do not extend readily to their structural investigations. High quality crystals of bacterial complexes have been difficult to obtain despite the enzymes' smaller sizes and simpler subunit compositions compared to their mitochondrial counterparts. In the course of the structure determination of the bc (1) complex from R. sphaeroides, we observed that the growth of only low quality crystals correlated with low activity and stability of the purified complex, which was mitigated in part by introducing a double mutations to the enzyme. The S287R(cyt b)/V135S(ISP) mutant shows 40% increase in electron transfer activity and displays a 4.3 degrees C increase in thermal stability over wild-t

SUBMITTER: Xia D 

PROVIDER: S-EPMC4788495 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature