A new metal-binding site in photosynthetic bacterial reaction centers that modulates QA to QB electron transfer.
Isolated reaction centers (RCs) from Rhodobacter sphaeroides were found to bind Zn(II) stoichiometrically and reversibly in addition to the 1 equiv of non-heme Fe(II). Metal and EPR analyses confirm that Zn(II) is ligated to a binding site that is distinct from the Fe site. When Zn(II) is bound to this site, electron transfer between the quinones QA and QB (QA-QB --> QAQB-) is slowed and the room-temperature kinetics become distributed across the microsecond to millisecond time domain. This effect of metal binding on the kinetics is similar to the more global effect of cooling RCs to 2 degreesC in the absence of Zn(II). This suggests that Zn(II) binding alters localized protein motions that are necessary for rapid QA-QB --> QAQB- electron transfer. Inspection of the RC crystal structure suggests a cluster of histidine ligands located beneath the QB binding pocket as a potential binding site.
Utschig
L M
LM
Chemistry Division, Argonne National Laboratory, Illinois 60439, USA. utschig@anlchm.chm.anl.gov
Ohigashi
Y
Y
Thurnauer
M C
MC
Tiede
D M
DM
D001665:Binding Sites; D002413:Cations, Divalent; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D005296:Ferrous Compounds / Q000737:chemistry / Q000378:metabolism; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D012242:Rhodobacter sphaeroides / Q000737:chemistry* / Q000378:metabolism*; D013054:Spectrophotometry, Atomic; D013696:Temperature; D015032:Zinc / Q000737:chemistry* / Q000378:metabolism*
D002413:Cations, Divalent; D005296:Ferrous Compounds; D045322:Photosynthetic Reaction Center Complex Proteins; D015032:Zinc