Probing the primary quinone environment in photosynthetic bacterial reaction centers by light-induced FTIR difference spectroscopy.
The photoreduction of the primary electron acceptor, QA, has been characterized by light-induced Fourier transform infrared difference spectroscopy for Rb. sphaeroides reaction centers and for Rsp. rubrum and Rp. viridis chromatophores. The samples were treated both with redox compounds, which rapidly reduce the photooxidized primary electron P+, and with inhibitors of electron transfer from QA- to the secondary quinone QB. This approach yields spectra free from P and P+ contributions which makes possible the study of the microenvironment of QA and QA-.
Breton
J
J
DBCM, CEN, Saclay, Gif-sur-Yvette, France.
Thibodeau
D L
DL
Berthomieu
C
C
Mäntele
W
W
Verméglio
A
A
Nabedryk
E
E
D005583:Fourier Analysis; D066298:In Vitro Techniques; D008027:Light; D010777:Photochemistry; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D011809:Quinones / Q000737:chemistry*; D012242:Rhodobacter sphaeroides; D012247:Rhodospirillum rubrum; D013055:Spectrophotometry, Infrared
D045322:Photosynthetic Reaction Center Complex Proteins; D011809:Quinones