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Title: Time-resolved electrochromism associated with the formation of quinone anions in the rhodobacter sphaeroides R26 reaction center

Journal Article · · Biochemistry (Eaton)
DOI:https://doi.org/10.1021/bi9605907· OSTI ID:505166
; ; ;  [1]
  1. Argonne National Lab., IL (United States)

The bacterial photosynthetic reaction center contains bacteriochlorophyll (Bchl) and bacteriochlorophyll (Bchl) and bacteriopheophytin (Bph) cofactors that provide natural probes of electrostatic fields within this protein. We have examined the electrochromic responses of these cofactors, resolved during the lifetimes of the quinone anion states, P{sup +}Q{sub A}{sup -Q}{sub B} and P{sup +}Q{sub A}Q{sub B}{sup -}, and measured as a function of temperature. These measurements provide information on the time-dependent variation in electrostatic field strength on the Bchl and Bph cofactors. Measurements in the near-infrared absorbance bands are described. 60 refs., 11 figs., 1 tab.

OSTI ID:
505166
Journal Information:
Biochemistry (Eaton), Vol. 35, Issue 33; Other Information: PBD: 20 Aug 1996
Country of Publication:
United States
Language:
English