title: Mutational analyses of the photosynthetic reaction center-bound triheme cytochrome subunit and cytochrome c2 in the purple bacterium Rhodovulum sulfidophilum.
abstract: The purple photosynthetic bacterium Rhodovulum sulfidophilum has an unusual reaction center- (RC-) bound cytochrome subunit with only three hemes, although the subunits of other purple bacteria have four hemes. To understand the electron-transfer pathway through this subunit, three mutants of R. sulfidophilum were constructed and characterized: one lacking the RC-bound cytochrome subunit, another one lacking cytochrome c(2), and another one lacking both of these. The mutant lacking the RC-bound cytochrome subunit was grown photosynthetically with about half the growth rate of the wild type, indicating that the presence of the cytochrome subunit, while not indispensable, is still advantageous for the photosynthetic electron transfer to support its growth. The mutant lacking both the cytochrome subunit and cytochrome c(2) showed a slower rate of growth by photosynthesis (about a fourth of that of the wild type), indicating that cytochrome c(2) is the dominant electron donor to the RC mutationally devoid of the cytochrome subunit. On the other hand, the mutant lacking only the cytochrome c(2) gene grew photosynthetically as fast as the wild type, indicating that cytochrome c(2) is not the predominant donor to the RC-bound triheme cytochrome subunit. We further show that newly isolated soluble cytochrome c-549 with a redox midpoint potential of +238 mV reduced the photooxidized cytochrome subunit in vitro, suggesting that c-549 mediates the cytochrome c(2)-independent electron transfer from the bc(1) complex to the RC-bound cytochrome subunit. These results indicate that the soluble components donating electrons to the RC-bound triheme cytochrome subunit are somewhat different from those of other purple bacteria.
authors.affiliation: Department of Biology, Tokyo Metropolitan University, Minamiohsawa, Hachioji, Tokyo 192-0397, Japan. masuda-shinji@c.metro-u.ac.jp
authors.forename: Shinji
authors.initials: S
authors.lastname: Masuda
authors.forename: Yusuke
authors.initials: Y
authors.lastname: Tsukatani
authors.forename: Yasuaki
authors.initials: Y
authors.lastname: Kimura
authors.forename: Kenji V P
authors.initials: KV
authors.lastname: Nagashima
authors.forename: Keizo
authors.initials: K
authors.lastname: Shimada
authors.forename: Katsumi
authors.initials: K
authors.lastname: Matsuura
mesh_terms: D020561:Alphaproteobacteria / Q000201:enzymology* / Q000235:genetics*; D003574:Cytochrome c Group / Q000737:chemistry* / Q000172:deficiency / Q000235:genetics* / Q000302:isolation & purification; D045362:Cytochromes c2; D004252:DNA Mutational Analysis; D004579:Electron Transport / Q000235:genetics; D006418:Heme / Q000737:chemistry* / Q000235:genetics; D016254:Mutagenesis, Insertional; D010084:Oxidation-Reduction; D010641:Phenotype; D010788:Photosynthesis / Q000235:genetics; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000235:genetics*; D010957:Plasmids / Q000138:chemical synthesis; D021122:Protein Subunits; D012995:Solubility; D013056:Spectrophotometry, Ultraviolet
chemical_list: D003574:Cytochrome c Group; D045322:Photosynthetic Reaction Center Complex Proteins; D021122:Protein Subunits; D006418:Heme; D045362:Cytochromes c2; C031732:cytochrome C-550