Frank Müh, MR Jones, W. Lubitz,
"Reorientation of the acetyl group of the photoactive bacteriopheophytin in reaction centers of Rhodobacter sphaeroides: An ENDOR TRIPLE resonance study"
, in John Wiley and Sons Ltd., in Biospectroscopy, Vol. 5, 9-1999, ISSN: 1075-4261
Reorientation of the acetyl group of the photoactive bacteriopheophytin in reaction centers of Rhodobacter sphaeroides: An ENDOR TRIPLE resonance study
Sprache des Titels:
The freeze-trapped bacteriopheophytin a radical anion Phi(A)(.-) has been investigated by H-1-ENDOR/Special TRIPLE resonance spectroscopy in photosynthetic reaction centers of Rhodabacter sphaeroides, in which the Tyr at position M210 had been replaced by either Phe, Leu, His or Trp. In the wild type reaction center and the mutants YF(M210) and YW(M210) two distinct states of Phi(A)(.-), denoted I-1(.-) and I-2(.-), can be stabilized below 200 K. The state I-1(.-) is metastable and relaxes to I-2(.-) as the temperature is raised from 135 K to 180 K. The difference in the electronic structure of Phi(A)(.-) between the two states is interpreted in terms of a conformational change of Phi(A) after freeze-trapping, involving a reorientation of the 3-acetyl group with respect to the macrocycle of the bacteriopheophytin. This interpretation is supported by the results of RHF-INDO/SP calculations. In the YH(M210) reaction center only one Phi(A)(.-) state is obtained that is distinct from I-1(.-) and I-2(.-), and the observed electronic structure indicates an almost in-plane orientation of the 3-acetyl group. This is consistent with the proposal that a hydrogen bond is formed between His M210 and the 3(1)-keto oxygen of Phi(A) that impedes the reorientation of the acetyl group. Only one Phi(A)(.-) state is observed in the YL(M210) reaction center, which is similar to the metastable state I-1(.-) in the wild type complex. This result is interpreted in terms of a steric hindrance of the reorientation of the 3-acetyl group that is exerted by the side chain of Leu at position M210. Possible implications of these findings for the mechanism of electron transfer in bacterial reaction centers are discussed. (C) 1999 John Wiley & Sons, Inc.